Journal articles: 'CAP2'

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Schneider, Felix, Isabell Metz, Sharof Khudayberdiev, and Marco B. Rust. "Functional Redundancy of Cyclase-Associated Proteins CAP1 and CAP2 in Differentiating Neurons." Cells 10, no. 6 (June 17, 2021): 1525. http://dx.doi.org/10.3390/cells10061525.

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Cyclase-associated proteins (CAPs) are evolutionary-conserved actin-binding proteins with crucial functions in regulating actin dynamics, the spatiotemporally controlled assembly and disassembly of actin filaments (F-actin). Mammals possess two family members (CAP1 and CAP2) with different expression patterns. Unlike most other tissues, both CAPs are expressed in the brain and present in hippocampal neurons. We recently reported crucial roles for CAP1 in growth cone function, neuron differentiation, and neuron connectivity in the mouse brain. Instead, CAP2 controls dendritic spine morphology and synaptic plasticity, and its dysregulation contributes to Alzheimer’s disease pathology. These findings are in line with a model in which CAP1 controls important aspects during neuron differentiation, while CAP2 is relevant in differentiated neurons. We here report CAP2 expression during neuron differentiation and its enrichment in growth cones. We therefore hypothesized that CAP2 is relevant not only in excitatory synapses, but also in differentiating neurons. However, CAP2 inactivation neither impaired growth cone morphology and motility nor neuron differentiation. Moreover, CAP2 mutant mice did not display any obvious changes in brain anatomy. Hence, differently from CAP1, CAP2 was dispensable for neuron differentiation and brain development. Interestingly, overexpression of CAP2 rescued not only growth cone size in CAP1-deficient neurons, but also their morphology and differentiation. Our data provide evidence for functional redundancy of CAP1 and CAP2 in differentiating neurons, and they suggest compensatory mechanisms in single mutant neurons.

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Hong, Suk-Joo, Youn-Kwan Park, Jung Hyuk Kim, Soon Hyuck Lee, Kyung Nam Ryu, Cheol Min Park, and Yeon Soo Kim. "The biomechanical evaluation of calcium phosphate cements for use in vertebroplasty." Journal of Neurosurgery: Spine 4, no. 2 (February 2006): 154–59. http://dx.doi.org/10.3171/spi.2006.4.2.154.

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Object The authors evaluate the biomechanical properties of vertebral bodies (VBs) stabilized with calcium phosphate (CaP) cements for use in vertebroplasty in comparison with polymethylmethacrylate (PMMA). Methods In the first phase of the study, 73 VBs (T3–L2; thoracic region [T3–8] and thoracolumbar region [T9–L2]) were collected from seven fresh human cadavers. Compression tests were performed before and after vertebroplasty using PMMA (compression strength 80 MPa) and three kinds of CaP cements—CaP1 (5 MPa), CaP2 (20 MPa), and CaP3 (50 MPa). The authors compared the maximal compression loads (MCLs) and stiffness before and after vertebroplasty in each of the four cement groups. In the second phase of the study, 18 paired spinal units (PSUs) were collected from three fresh human cadavers, and the authors injected two types of cement selected from the first phase of the study into the lower level of six PSUs. They compared the MCLs of the untreated and two treated groups (there were six PSUs in each type of group) to analyze the tendency of inducing compression fractures in the upper level of the PSUs. The MCLs of the PMMA-injected vertebrae were significantly increased after vertebroplasty. The MCL levels of the CaP3-injected vertebrae and the CaP2-injected thoracolumbar vertebrae were decreased from those of untreated vertebrae without being significant. The MCLs of CaP1-injected vertebrae and CaP2-injected thoracic vertebrae were significantly decreased after vertebroplasty. The stiffness of all cement groups was decreased after vertebroplasty compared with initial stiffness, significantly so in all three thoracic CaP groups. In the second compression test with PSUs, the MCLs of the CaP2- and CaP3-injected PSUs were not significantly different from those of the untreated control PSUs. Conclusions The CaP3-injected vertebrae restored the MCLs of human vertebrae closer to their initial levels than the PMMA-injected vertebrae did. The CaP2- and CaP3-injected PSUs showed no tendency to induce compression fractures in adjacent VBs.

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Mears, Harriet V., and Trevor R. Sweeney. "Mouse Ifit1b is a cap1-RNA–binding protein that inhibits mouse coronavirus translation and is regulated by complexing with Ifit1c." Journal of Biological Chemistry 295, no. 51 (October 19, 2020): 17781–801. http://dx.doi.org/10.1074/jbc.ra120.014695.

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Knockout mouse models have been extensively used to study the antiviral activity of IFIT (interferon-induced protein with tetratricopeptide repeats). Human IFIT1 binds to cap0 (m7GpppN) RNA, which lacks methylation on the first and second cap-proximal nucleotides (cap1, m7GpppNm, and cap2, m7GpppNmNm, respectively). These modifications are signatures of “self” in higher eukaryotes, whereas unmodified cap0-RNA is recognized as foreign and, therefore, potentially harmful to the host cell. IFIT1 inhibits translation at the initiation stage by competing with the cap-binding initiation factor complex, eIF4F, restricting infection by certain viruses that possess “nonself” cap0-mRNAs. However, in mice and other rodents, the IFIT1 orthologue has been lost, and the closely related Ifit1b has been duplicated twice, yielding three paralogues: Ifit1, Ifit1b, and Ifit1c. Although murine Ifit1 is similar to human IFIT1 in its cap0-RNA–binding selectivity, the roles of Ifit1b and Ifit1c are unknown. Here, we found that Ifit1b preferentially binds to cap1-RNA, whereas binding is much weaker to cap0- and cap2-RNA. In murine cells, we show that Ifit1b can modulate host translation and restrict WT mouse coronavirus infection. We found that Ifit1c acts as a stimulatory cofactor for both Ifit1 and Ifit1b, promoting their translation inhibition. In this way, Ifit1c acts in an analogous fashion to human IFIT3, which is a cofactor to human IFIT1. This work clarifies similarities and differences between the human and murine IFIT families to facilitate better design and interpretation of mouse models of human infection and sheds light on the evolutionary plasticity of the IFIT family.

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Tublitz, N. J., and J. W. Truman. "Insect cardioactive peptides. I. Distribution and molecular characteristics of two cardioacceleratory peptides in the tobacco hawkmoth, Manduca sexta." Journal of Experimental Biology 114, no. 1 (January 1, 1985): 365–79. http://dx.doi.org/10.1242/jeb.114.1.365.

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Using an in vitro heart bioassay, the pharmacological and biochemical properties of two cardioactive peptides derived from neural tissues of the moth, Manduca sexta, were analysed. Gel filtration of ventral nerve cords (VNC) from pharate adults identified two cardioacceleratory peptides (CAP1 and CAP2) with apparent molecular weights of 1000 and 500 Da, respectively. Both CAPs were localized to the abdominal perivisceral organs, the major neurohaemal release sites in the insect VNC. Pulse application of CAP1 or CAP2 on the in vitro Manduca heart produced a dose-dependent increase in rate but had no effect on beat amplitude. The threshold dose for the action of each peptide on the isolated heart bioassay was less than 0.05 abdominal nerve cord equivalents. Both CAPs were present in the pharate adult VNC of several other Lepidopteran species. Neither CAP1 nor CAP2 was detected in the prepupal VNC of Manduca sexta.

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Grini, Paul E., Gerd Jürgens, and Martin Hülskamp. "Embryo and Endosperm Development Is Disrupted in the Female Gametophytic capulet Mutants of Arabidopsis." Genetics 162, no. 4 (December 1, 2002): 1911–25. http://dx.doi.org/10.1093/genetics/162.4.1911.

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Abstract The female gametophyte of higher plants gives rise, by double fertilization, to the diploid embryo and triploid endosperm, which develop in concert to produce the mature seed. What roles gametophytic maternal factors play in this process is not clear. The female-gametophytic effects on embryo and endosperm development in the Arabidopsis mea, fis, and fie mutants appear to be due to gametic imprinting that can be suppressed by METHYL TRANSFERASE1 antisense (MET1 a/s) transgene expression or by mutation of the DECREASE IN DNA METHYLATION1 (DDM1) gene. Here we describe two novel gametophytic maternal-effect mutants, capulet1 (cap1) and capulet2 (cap2). In the cap1 mutant, both embryo and endosperm development are arrested at early stages. In the cap2 mutant, endosperm development is blocked at very early stages, whereas embryos can develop to the early heart stage. The cap mutant phenotypes were not rescued by wild-type pollen nor by pollen from tetraploid plants. Furthermore, removal of silencing barriers from the paternal genome by MET1 a/s transgene expression or by the ddm1 mutation also failed to restore seed development in the cap mutants. Neither cap1 nor cap2 displayed autonomous seed development, in contrast to mea, fis, and fie mutants. In addition, cap2 was epistatic to fis1 in both autonomous endosperm and sexual development. Finally, both cap1 and cap2 mutant endosperms, like wild-type endosperms, expressed the paternally inactive endosperm-specific FIS2 promoter GUS fusion transgene only when the transgene was introduced via the embryo sac, indicating that imprinting was not affected. Our results suggest that the CAP genes represent novel maternal functions supplied by the female gametophyte that are required for embryo and endosperm development.

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Kohtz, DS, V. Georgieva-Hanson, JD Kohtz, WJ Schook, and S. Puszkin. "Mapping two functional domains of clathrin light chains with monoclonal antibodies." Journal of Cell Biology 104, no. 4 (April 1, 1987): 897–903. http://dx.doi.org/10.1083/jcb.104.4.897.

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The two forms of clathrin light chains (LCA and LCB) or clathrin-associated proteins (CAP1 and CAP2) have presented an immunochemical paradox. Biochemically similar, both possess two known functional parameters: binding the clathrin heavy chain and mediating the action of an uncoating ATPase. All previously reported anti-CAP mAbs, however, react specifically with only CAP1 (Brodsky, F. M., 1985, J. Cell Biol., 101:2047-2054; Kirchhausen, T., S. C. Harrison, P. Parham, and F. M. Brodsky, 1983, Proc. Natl. Acad. Sci. USA, 80:2481-2485). Four new anti-CAP mAbs are reported here: two, C-7H12 and C-6C1, react with both forms; two others, C-10B2 and C-4E5, react only with the lower form. Sandwich ELISAs indicated that C-10B2, C-4E5, C-6C1, and C-7H12 react with distinct epitopes. Monoclonal antibodies C-10B2 and C-4E5 immunoprecipitate clathrin-coated vesicles (CCVs) and react with CAP2 epitopes accessible to chymotrypsin on the vesicle. These mAbs inhibit phosphorylation of CAP2 by endogenous CCV casein kinase II. In contrast, C-6C1 and C-7H12 react with epitopes that are relatively insensitive to chymotrypsin. CAP peptide fragments containing these epitopes remain bound to reassembled cages or CCVs after digestion. Immunoprecipitation and ELISAs demonstrate that C-7H12 and C-6C1 react with unbound CAPs but not with CAPs bound to triskelions or CCVs. The data indicate that the CAPs consist of at least two discernible structural domains: a nonconserved, accessible domain that is relevant to the phosphorylation of CAP2 and a conserved, inaccessible domain that mediates the binding of CAPs to CCVs.

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Aspit, Liam, Aviva Levitas, Sharon Etzion, Hanna Krymko, Leonel Slanovic, Raz Zarivach, Yoram Etzion, and Ruti Parvari. "CAP2 mutation leads to impaired actin dynamics and associates with supraventricular tachycardia and dilated cardiomyopathy." Journal of Medical Genetics 56, no. 4 (December 5, 2018): 228–35. http://dx.doi.org/10.1136/jmedgenet-2018-105498.

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BackgroundDilated cardiomyopathy (DCM) is a primary myocardial disease leading to contractile dysfunction, progressive heart failure and excessive risk of sudden cardiac death. Around half of DCM cases are idiopathic, and genetic factors seem to play an important role.AimWe investigated a possible genetic cause of DCM in two consanguineous children from a Bedouin family.Methods and resultsUsing exome sequencing and searching for rare homozygous variations, we identified a nucleotide change in the donor splice consensus sequence of exon 7 in CAP2 as the causative mutation. Using patient-derived fibroblasts, we demonstrated that the mutation causes skipping of exons 6 and 7. The resulting protein is missing 64 amino acids in its N-CAP domain that should prevent its correct folding. CAP2 protein level was markedly reduced without notable compensation by the homolog CAP1. However, β-actin mRNA was elevated as demonstrated by real-time qPCR. In agreement with the essential role of CAP2 in actin filament polymerization, we demonstrate that the mutation affects the kinetics of repolymerization of actin in patient fibroblasts.ConclusionsThis is the first report of a recessive deleterious mutation in CAP2 and its association with DCM in humans. The clinical phenotype recapitulates the damaging effects on the heart observed in Cap2 knockout mice including DCM and cardiac conduction disease, but not the other effects on growth, viability, wound healing and eye development. Our data underscore the importance of the proper kinetics of actin polymerization for normal function of the human heart.

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Kumar, Parimal, Trevor R. Sweeney, Maxim A. Skabkin, Olga V. Skabkina, Christopher U. T. Hellen, and Tatyana V. Pestova. "Inhibition of translation by IFIT family members is determined by their ability to interact selectively with the 5′-terminal regions of cap0-, cap1- and 5′ppp- mRNAs." Nucleic Acids Research 42, no. 5 (December 25, 2013): 3228–45. http://dx.doi.org/10.1093/nar/gkt1321.

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AbstractRibosomal recruitment of cellular mRNAs depends on binding of eIF4F to the mRNA’s 5′-terminal ‘cap’. The minimal ‘cap0’ consists of N7-methylguanosine linked to the first nucleotide via a 5′-5′ triphosphate (ppp) bridge. Cap0 is further modified by 2′-O-methylation of the next two riboses, yielding ‘cap1’ (m7GpppNmN) and ‘cap2’ (m7GpppNmNm). However, some viral RNAs lack 2′-O-methylation, whereas others contain only ppp- at their 5′-end. Interferon-induced proteins with tetratricopeptide repeats (IFITs) are highly expressed effectors of innate immunity that inhibit viral replication by incompletely understood mechanisms. Here, we investigated the ability of IFIT family members to interact with cap1-, cap0- and 5′ppp- mRNAs and inhibit their translation. IFIT1 and IFIT1B showed very high affinity to cap-proximal regions of cap0-mRNAs (K1/2,app ∼9 to 23 nM). The 2′-O-methylation abrogated IFIT1/mRNA interaction, whereas IFIT1B retained the ability to bind cap1-mRNA, albeit with reduced affinity (K1/2,app ∼450 nM). The 5′-terminal regions of 5′ppp-mRNAs were recognized by IFIT5 (K1/2,app ∼400 nM). The activity of individual IFITs in inhibiting initiation on a specific mRNA was determined by their ability to interact with its 5′-terminal region: IFIT1 and IFIT1B efficiently outcompeted eIF4F and abrogated initiation on cap0-mRNAs, whereas inhibition on cap1- and 5′ppp- mRNAs by IFIT1B and IFIT5 was weaker and required higher protein concentrations.

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Adachi, Masataka, Yohei Masugi, Ken Yamazaki, Katsura Emoto, Yusuke Kobayashi, Eiichiro Tominaga, Kouji Banno, Daisuke Aoki, and Michiie Sakamoto. "Upregulation of cyclase-associated actin cytoskeleton regulatory protein 2 in epithelial ovarian cancer correlates with aggressive histologic types and worse outcomes." Japanese Journal of Clinical Oncology 50, no. 6 (March 24, 2020): 643–52. http://dx.doi.org/10.1093/jjco/hyaa026.

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Abstract Objective Cyclase-associated actin cytoskeleton regulatory protein 2 (CAP2) regulates actin dynamics to control cell cycles and cell migration. CAP2 overexpression contributes to cancer progression in several tumor types; however, the role of CAP2 expression in ovarian cancer remains unclear. This study aimed to clarify the significance of CAP2 expression in epithelial ovarian tumor. Methods We evaluated CAP2 expression in ovarian cancer cell lines using quantitative real-time polymerase chain reaction, western blotting and immunocytochemistry and examined the effect of CAP2 silencing in migration and proliferation assays. CAP2 immunohistochemistry was conducted using tissue specimens from 432 ovarian carcinoma patients; a further 55 borderline and benign 65 lesions were analyzed. CAP2 expression levels were defined as low, intermediate or high, for correlation analysis with clinicopathological factors. Results CAP2 expression was significantly higher in cell lines from Type II ovarian cancer than in those in Type I, and knockdown of CAP2 showed decreased migration and proliferation. Higher levels of CAP2 expression in human tissues were associated with Type II histology, residual lesion, lymph node metastasis, ascites cytology and higher clinical stage. High CAP2 expression levels were observed in 26 (23.4%) of 111 Type II ovarian cancers and in 16 (5.0%) of 321 Type I cancers but not in any borderline or benign lesions. Multivariate analyses showed that CAP2 expression in ovarian cancer is an independent prognostic factor for recurrence-free survival (P = 0.019). Conclusion CAP2 expression is upregulated in aggressive histologic types of epithelial ovarian cancer and serves as a novel prognostic biomarker for patient survival.

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Tublitz, N. J., A. T. Allen, C. C. Cheung, K. K. Edwards, D. P. Kimble, P. K. Loi, and A. W. Sylwester. "Insect cardioactive peptides: regulation of hindgut activity by cardioacceleratory peptide 2 (CAP2) during wandering behaviour in Manduca sexta larvae." Journal of Experimental Biology 165, no. 1 (April 1, 1992): 241–64. http://dx.doi.org/10.1242/jeb.165.1.241.

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The functional relationship between cardioacceleratory peptide 2 (CAP2) and hindgut activity during wandering behaviour was investigated in fifth-instar larvae of the tobacco hawkmoth Manduca sexta. Inspection of the alimentary canal on the day prior to wandering showed that the gut, in preparation for metamorphosis, was voided of all contents by 18:00 h. Associated with this event, which we refer to as ‘gut emptying’, was an increase in the frequency of hindgut contractions measured in vivo. No change in heart activity was seen during this developmental period. Measurements of the amount of CAP2 in the central nervous system (CNS) of fifth-instar caterpillars revealed that CAP2 storage levels declined sharply on the day of gut emptying. The drop in CNS levels of CAP2 at gut emptying was temporally correlated with the appearance of CAP2 in the haemolymph. CAP2, when applied at physiological concentrations to an in vitro larval hindgut bioassay, caused changes in several parameters, including contraction frequency and amplitude, and basal tension. In vivo administration of CAP2 elicited hindgut responses that were qualitatively and quantitatively similar to those seen in vitro. Developmental studies on changes in CAP2 responsiveness during the last larval instar demonstrated that the hindgut is maximally sensitive to CAP2 on the day of gut emptying. Direct evidence in support of a role for CAP2 in fifth-instar larvae was provided by experiments in which the increase in gut activity in vivo seen at gut emptying was significantly reduced by injections of an anti-CAP antibody. Based on data from cobalt backfills and anti-CAP immunohistochemical staining, we propose that CAP2 exerts its effect on the larval hindgut at wandering via a local release from CAP-containing neurones in the terminal ganglion that project directly to the hindgut.

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Broadie, K. S., A. W. Sylwester, M. Bate, and N. J. Tublitz. "Immunological, biochemical and physiological analyses of cardioacceleratory peptide 2 (CAP2) activity in the embryo of the tobacco hawkmoth Manduca sexta." Development 108, no. 1 (January 1, 1990): 59–71. http://dx.doi.org/10.1242/dev.108.1.59.

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The cells in the embryonic CNS of the tobacco hawkmoth, Manduca sexta, that synthesize a cardioacceleratory peptide 2 (CAP2)-like antigen were identified using immunohistochemical techniques. Two distinct neurosecretory cell types were present in the abdominal ventral nerve cord (VNC) that contain CAP2-like immunoreactivity during late embryogenesis: a pair of large (diameter range 15–20 microns) cells lying along the posterior, dorsal midline of abdominal ganglia A4-A8, and a bilateral set of four smaller (diameter range 6–11 microns) neurons which lie at the base of each ventral root in abdominal ganglia A2-A8. CAP2-like accumulation appeared to follow independent patterns in the two cell types. CAP2-like immunoreactivity began at 60% of embryo development (DT) in the medial cells, accumulated steadily throughout embryogenesis, and dropped markedly during hatching. Lateral cells synthesized the CAP2-like antigen later in development (70% DT) and showed a sharp drop in antigen levels between 75% and 80% of embryonic development. Extracts from developing M. sexta embryos were found to contain a cardioactive factor capable of accelerating the contraction frequency of the pharate adult moth heart in a fashion similar to CAP2. Immunoprecipitation with a monoclonal antibody that specifically recognizes the two endogenous Manduca cardioacceleratory peptides and purification using high pressure liquid chromatography identified this factor as cardioacceleratory peptide 2 (CAP2). Using an in vitro heart bioassay, the levels of this cardioactive neuropeptide were traced during the development of the M. sexta embryo. As with the immunohistochemical results, two periods during embryogenesis were identified in which the level of CAP2 dropped markedly: between 75% and 80% development, and at hatching. Embryo bioassays of CAP2 activity were used to identify possible target tissues for physiological activity during these two putative release times. CAP2 was found to accelerate contraction frequency in the embryonic heart and hindgut of Manduca in a dose-dependent fashion. Of these two possible targets, the hindgut proved to be more sensitive to CAP2, having a lower response threshold and a longer duration of response to a given concentration of the exogenously applied peptide. Based on these immunocytochemical, pharmacological and biochemical results, and on a previously published detailed analysis of Manduca embryogenesis, we conclude that CAP2 is probably released from a specific set of identified neurosecretory cells in the abdominal VNC to modulate embryonic gut activity at 75–80% of embryo development during ingestion of the extra-embryonic yolk.

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Loi, P. K., and N. J. Tublitz. "Hormonal control of transmitter plasticity in insect peptidergic neurons. I. Steroid regulation of the decline in cardioacceleratory peptide 2 (CAP2) expression." Journal of Experimental Biology 181, no. 1 (August 1, 1993): 175–94. http://dx.doi.org/10.1242/jeb.181.1.175.

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Transmitter plasticity, the ability to alter transmitter expression, has been documented in several different preparations both in vivo and in vitro. One of these is the tobacco hawkmoth, Manduca sexta, whose central nervous system contains four individually identified lateral neurosecretory cells (LNCs) that undergo a postembryonic transmitter switch in vivo. In larvae, the LNCs express high levels of a myoregulatory peptide, cardioacceleratory peptide 2 (CAP2). In contrast, the predominant LNC transmitter in adult moths in bursicon, a classic insect peptide hormone responsible for cuticular tanning. Here we show that the CAP2-to-bursicon conversion by the LNCs is a multi-step process beginning with a decline in CAP2 levels midway through the final larval stage. We provide several lines of evidence that this CAP2 drop is regulated by the insect steroid hormone 20-hydroxyecdysone (20-HE). The LNCs exhibit a fall in CAP2 levels at the beginning of metamorphosis, immediately after the commitment pulse of 20-HE when steroid levels are elevated. LNCs not exposed to this 20-HE rise do not exhibit a decline in CAP2 level. The transmitter switch can also be prevented by using an analog of juvenile hormone to create a larval hormonal environment during the commitment pulse of 20-HE. The CAP2 decline in the LNCs could be directly induced by exogenous steroid application, but only under conditions where the LNCs remained connected to the brain. Thus, the first step in the transmitter switch by the LNCs, the decline in CAP2 levels, is triggered by the commitment pulse of 20-HE, which may act indirectly through a set of steroid-sensitive cells in the brain.

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García-Caballero, Agustín, Yan Dang, Hong He, and M. Jackson Stutts. "ENaC Proteolytic Regulation by Channel-activating Protease 2." Journal of General Physiology 132, no. 5 (October 13, 2008): 521–35. http://dx.doi.org/10.1085/jgp.200810030.

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Epithelial sodium channels (ENaCs) perform diverse physiological roles by mediating Na+ absorption across epithelial surfaces throughout the body. Excessive Na+ absorption in kidney and colon elevates blood pressure and in the airways disrupts mucociliary clearance. Potential therapies for disorders of Na+ absorption require better understanding of ENaC regulation. Recent work has established partial and selective proteolysis of ENaCs as an important means of channel activation. In particular, channel-activating transmembrane serine proteases (CAPs) and cognate inhibitors may be important in tissue-specific regulation of ENaCs. Although CAP2 (TMPRSS4) requires catalytic activity to activate ENaCs, there is not yet evidence of ENaC fragments produced by this serine protease and/or identification of the site(s) where CAP2 cleaves ENaCs. Here, we report that CAP2 cleaves at multiple sites in all three ENaC subunits, including cleavage at a conserved basic residue located in the vicinity of the degenerin site (α-K561, β-R503, and γ-R515). Sites in α-ENaC at K149/R164/K169/R177 and furin-consensus sites in α-ENaC (R205/R231) and γ-ENaC (R138) are responsible for ENaC fragments observed in oocytes coexpressing CAP2. However, the only one of these demonstrated cleavage events that is relevant for the channel activation by CAP2 takes place in γ-ENaC at position R138, the previously identified furin-consensus cleavage site. Replacement of arginine by alanine or glutamine (α,β,γR138A/Q) completely abolished both the Na+ current (INa) and a 75-kD γ-ENaC fragment at the cell surface stimulated by CAP2. Replacement of γ-ENaC R138 with a conserved basic residue, lysine, preserved both the CAP2-induced INa and the 75-kD γ-ENaC fragment. These data strongly support a model where CAP2 activates ENaCs by cleaving at R138 in γ-ENaC.

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Karpova, T. S., M. M. Lepetit, and J. A. Cooper. "Mutations that enhance the cap2 null mutant phenotype in Saccharomyces cerevisiae affect the actin cytoskeleton, morphogenesis and pattern of growth." Genetics 135, no. 3 (November 1, 1993): 693–709. http://dx.doi.org/10.1093/genetics/135.3.693.

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Abstract Mutations conferring synthetic lethality in combination with null mutations in CAP2, the gene encoding the beta subunit of capping protein of Saccharomyces cerevisiae, were obtained in a colony color assay. Monogenic inheritance was found for four mutations, which were attributed to three genetic loci. One mutation, sac6-69, is in the gene encoding fimbrin, another actin-binding protein, which was expected because null mutations in SAC6 and CAP2 are known to be synthetic-lethal. The other two loci were designated slc for synthetic lethality with cap2. These loci include the mutations slc1-66, slc1-87 and slc2-107. The slc mutations are semi-dominant, as shown by incomplete complementation in slc/SLC cap2/cap2 heterozygotes. The slc mutations and sac6-69 interact with each other, as shown by enhanced phenotypes in diheterozygotes. Moreover, the haploid slc2-107 sac6-69 double mutant is inviable. In a CAP2 background, the slc mutations lead to temperature and osmotic sensitivity. They alter the distribution of the actin cytoskeleton, including deficits in the presence of actin cables and the polarization of cortical actin patches. The slc mutations also lead to a pseudomycelial growth pattern. Together these results suggest that slc1 and slc2 encode components of the actin cytoskeleton in yeast and that the actin cytoskeleton can regulate the patterns of growth.

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Ximin, Liu. "Totally complex submanifolds of the Cayley projective plane." Glasgow Mathematical Journal 40, no. 2 (May 1998): 161–66. http://dx.doi.org/10.1017/s001708950003247x.

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AbstractLet h be the second fundamental form of a compact submanifold M of the Cayley projective plane CaP2. We determine all compact totally complex submanifolds of complex dimension n in CaP2 satisfying |h|2 ≤ n.

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Di Maio, Anna, Arianna De Rosa, Silvia Pelucchi, Martina Garofalo, Benedetta Marciano, Tommaso Nuzzo, Fabrizio Gardoni, et al. "Analysis of mRNA and Protein Levels of CAP2, DLG1 and ADAM10 Genes in Post-Mortem Brain of Schizophrenia, Parkinson’s and Alzheimer’s Disease Patients." International Journal of Molecular Sciences 23, no. 3 (January 28, 2022): 1539. http://dx.doi.org/10.3390/ijms23031539.

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Schizophrenia (SCZ) is a mental illness characterized by aberrant synaptic plasticity and connectivity. A large bulk of evidence suggests genetic and functional links between postsynaptic abnormalities and SCZ. Here, we performed quantitative PCR and Western blotting analysis in the dorsolateral prefrontal cortex (DLPFC) and hippocampus of SCZ patients to investigate the mRNA and protein expression of three key spine shapers: the actin-binding protein cyclase-associated protein 2 (CAP2), the sheddase a disintegrin and metalloproteinase 10 (ADAM10), and the synapse-associated protein 97 (SAP97). Our analysis of the SCZ post-mortem brain indicated increased DLG1 mRNA in DLPFC and decreased CAP2 mRNA in the hippocampus of SCZ patients, compared to non-psychiatric control subjects, while the ADAM10 transcript was unaffected. Conversely, no differences in CAP2, SAP97, and ADAM10 protein levels were detected between SCZ and control individuals in both brain regions. To assess whether DLG1 and CAP2 transcript alterations were selective for SCZ, we also measured their expression in the superior frontal gyrus of patients affected by neurodegenerative disorders, like Parkinson’s and Alzheimer’s disease. Interestingly, also in Parkinson’s disease patients, we found a selective reduction of CAP2 mRNA levels relative to controls but unaltered protein levels. Taken together, we reported for the first time altered CAP2 expression in the brain of patients with psychiatric and neurological disorders, thus suggesting that aberrant expression of this gene may contribute to synaptic dysfunction in these neuropathologies.

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Amatruda, J. F., D. J. Gattermeir, T. S. Karpova, and J. A. Cooper. "Effects of null mutations and overexpression of capping protein on morphogenesis, actin distribution and polarized secretion in yeast." Journal of Cell Biology 119, no. 5 (December 1, 1992): 1151–62. http://dx.doi.org/10.1083/jcb.119.5.1151.

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CAP1, the gene encoding the alpha subunit of Saccharomyces cerevisiae capping protein, was cloned using a probe prepared by PCR with primers based on the amino acid sequence of purified alpha subunit peptides. The sequence is similar to that of capping protein alpha subunits of other species but not to that of the S. cerevisiae capping protein beta subunit or any other protein. Null mutants of capping protein, prepared by deletion of the coding region of CAP1 and CAP2 separately or together, are viable and have a similar phenotype. Deletion of the gene for one subunit leads to a loss of protein for the other subunit. The null mutant has a severe deficit of actin cables and an increased number of actin spots in the mother. Cells are round and relatively large. These features are heterogeneous within a population of cells and vary with genetic background. Overexpression of CAP1 and CAP2 also causes loss of actin cables and cell enlargement, as well as the additional traits of aberrant morphogenesis and cell wall thickening. Capping protein null strains and overexpression strains exhibited normal polarized secretion during bud growth as demonstrated by labeling with fluoresceinated Con A. Projection formation and chitin deposition in response to mating pheromone, mating efficiency, and bud site selection were also normal in capping protein null strains. In addition, bulk secretion of invertase was unimpaired. These data indicate that actin cables are not required for polarized secretion in S. cerevisiae.

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Yu, G., J. Swiston, and D. Young. "Comparison of human CAP and CAP2, homologs of the yeast adenylyl cyclase-associated proteins." Journal of Cell Science 107, no. 6 (June 1, 1994): 1671–78. http://dx.doi.org/10.1242/jcs.107.6.1671.

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We previously reported the identification of human CAP, a protein that is related to the Saccharomyces cerevisiae and Schizosaccharomyces pombe adenylyl cyclase-associated CAP proteins. The two yeast CAP proteins have similar functions: the N-terminal domains are required for the normal function of adenylyl cyclase, while loss of the C-terminal domains result in morphological and nutritional defects that are unrelated to the cAMP pathways. We have amplified and cloned cDNAs from a human glioblastoma library that encode a second CAP-related protein, CAP2. The human CAP and CAP2 proteins are 64% identical. Expression of either human CAP or CAP2 in S. cerevisiae cap- strains suppresses phenotypes associated with deletion of the C-terminal domain of CAP, but does not restore hyper-activation of adenylyl cyclase by RAS2val19. Similarly, expression of either human CAP or CAP2 in S. pombe cap- strains suppresses the morphological and temperature-sensitive phenotypes associated with deletion of the C-terminal domain of CAP in this yeast. In addition, expression of human CAP, but not CAP2, suppresses the propensity to sporulate due to deletion of the N-terminal domain of CAP in S. pombe. This latter observation suggests that human CAP restores normal adenylyl cyclase activity in S. pombe cap- cells. Thus, functional properties of both N-terminal and C-terminal domains are conserved between the human and S. pombe CAP proteins.

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A, Mu, Tak Shun Fung, Lisa M. Francomacaro, Thao Huynh, Tommi Kotila, Zdenek Svindrych, and Henry N. Higgs. "Regulation of INF2-mediated actin polymerization through site-specific lysine acetylation of actin itself." Proceedings of the National Academy of Sciences 117, no. 1 (December 23, 2019): 439–47. http://dx.doi.org/10.1073/pnas.1914072117.

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INF2 is a formin protein that accelerates actin polymerization. A common mechanism for formin regulation is autoinhibition, through interaction between the N-terminal diaphanous inhibitory domain (DID) and C-terminal diaphanous autoregulatory domain (DAD). We recently showed that INF2 uses a variant of this mechanism that we term “facilitated autoinhibition,” whereby a complex consisting of cyclase-associated protein (CAP) bound to lysine-acetylated actin (KAc-actin) is required for INF2 inhibition, in a manner requiring INF2-DID. Deacetylation of actin in the CAP/KAc-actin complex activates INF2. Here we use lysine-to-glutamine mutations as acetylmimetics to map the relevant lysines on actin for INF2 regulation, focusing on K50, K61, and K328. Biochemically, K50Q- and K61Q-actin, when bound to CAP2, inhibit full-length INF2 but not INF2 lacking DID. When not bound to CAP, these mutant actins polymerize similarly to WT-actin in the presence or absence of INF2, suggesting that the effect of the mutation is directly on INF2 regulation. In U2OS cells, K50Q- and K61Q-actin inhibit INF2-mediated actin polymerization when expressed at low levels. Direct-binding studies show that the CAP WH2 domain binds INF2-DID with submicromolar affinity but has weak affinity for actin monomers, while INF2-DAD binds CAP/K50Q-actin 5-fold better than CAP/WT-actin. Actin in complex with full-length CAP2 is predominately ATP-bound. These interactions suggest an inhibition model whereby CAP/KAc-actin serves as a bridge between INF2 DID and DAD. In U2OS cells, INF2 is 90-fold and 5-fold less abundant than CAP1 and CAP2, respectively, suggesting that there is sufficient CAP for full INF2 inhibition.

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Kepser, Lara-Jane, Fidan Damar, Teresa De Cicco, Christine Chaponnier, Tomasz J. Prószyński, Axel Pagenstecher, and Marco B. Rust. "CAP2 deficiency delays myofibril actin cytoskeleton differentiation and disturbs skeletal muscle architecture and function." Proceedings of the National Academy of Sciences 116, no. 17 (April 8, 2019): 8397–402. http://dx.doi.org/10.1073/pnas.1813351116.

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Actin filaments (F-actin) are key components of sarcomeres, the basic contractile units of skeletal muscle myofibrils. A crucial step during myofibril differentiation is the sequential exchange of α-actin isoforms from smooth muscle (α-SMA) and cardiac (α-CAA) to skeletal muscle α-actin (α-SKA) that, in mice, occurs during early postnatal life. This “α-actin switch” requires the coordinated activity of actin regulators because it is vital that sarcomere structure and function are maintained during differentiation. The molecular machinery that controls the α-actin switch, however, remains enigmatic. Cyclase-associated proteins (CAP) are a family of actin regulators with largely unknown physiological functions. We here report a function for CAP2 in regulating the α-actin exchange during myofibril differentiation. This α-actin switch was delayed in systemic CAP2 mutant mice, and myofibrils remained in an undifferentiated stage at the onset of the often excessive voluntary movements in postnatal mice. The delay in the α-actin switch coincided with the onset of motor function deficits and histopathological changes including a high frequency of type IIB ring fibers. Our data suggest that subtle disturbances of postnatal F-actin remodeling are sufficient for predisposing muscle fibers to form ring fibers. Cofilin2, a putative CAP2 interaction partner, has been recently implicated in myofibril actin cytoskeleton differentiation, and the myopathies in cofilin2 and CAP2 mutant mice showed striking similarities. We therefore propose a model in which CAP2 and cofilin2 cooperate in actin regulation during myofibril differentiation.

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Costa, Joseane Dunga da, Jeane Cruz Portela, Phâmella Kalliny Pereira Farias, Francisco Ernesto Sobrinho, Carolina Malala Martins Souza, Thaís Cristina de Souza Lopes, and Francisco Wellington Andrade Silva. "Characterization and Classification of Soils of the Terra da Esperança Settlement Project in Chapada do Apodi, Brazil." Journal of Agricultural Science 11, no. 4 (March 15, 2019): 235. http://dx.doi.org/10.5539/jas.v11n4p235.

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Soil characterization and pedological classification are essential to define its main potentials and restrictions. The objective of this work was to classify the morphological, physical, chemical, and pedological attributes of soils of the Terra da Esperança Settlement Project (TESP) in Chapada do Apodi, Brazil, and find the most sensitive attributes for distinguishing them using multivariate analysis. The research was carried out in the TESP, in the municipality of Governor Dix-Sept Rosado, state of Rio Grande do Norte, Brazil. Ten sites were chosen to open representative soil profiles: Native Forest Area 1 (NFA1), 2 (NFA2), and 3 (NFA3), Collective Area with Native Forest (CNF), Agroecological Area (AEA), Cashew crop Area (CCA) Collective Area with Pasture 1 (CAP1), and 2 (CAP2), Permanent Preservation Area (PPA), and Cajaraneira (Spondia sp.) Orchard Area (COA). Disturbed and undisturbed soil samples were collected and subjected to physical and chemical analysis for soil classification. The soils classes found were: Cambissolo Haplico Carbonatico vertissolico (NFA1), Cambissolo Haplico Carbonatico tipico (CNF, and AEA), Cambissolo Haplico Ta Eutrofico tipico (CAP2, NFA2, and COA), Cambissolo Haplico Ta Eutrofico vertissolico (NFA3), Argissolo Vermelho Distrofico latossolico (CCA), Chernossolo Rendzico Ortico saprolitico (CAP1), and Neossolo Fluvico Ta Eutrofico tipico (PPA). The material of origin of the soils contributed to the presence of a calcic horizon in the profiles NFA1, CNF, AEA, CCA (Cambissolos), and CAP1 (Chernossolos). The textural class of the soils varied from sand to clay. The Argissolo (CCA) presented acid character, high aluminum saturation, low base saturation, dystrophic character, and low cation exchange capacity, forming horizons with chemical limitations, due to its latossolico character. The most sensitive attributes for distinguishing the soil classes were related to the source material, which directly influenced the soil physical (silt and clay) and chemical (acidity, salinity, nutrient availability, and clay activity) attributes.

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Geladakis, George, Nikolaos Nikolioudakis, George Koumoundouros, and Stylianos Somarakis. "Morphometric discrimination of pelagic fish stocks challenged by variation in body condition." ICES Journal of Marine Science 75, no. 2 (September 13, 2017): 711–18. http://dx.doi.org/10.1093/icesjms/fsx186.

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Abstract Morphometric characters have traditionally been used to describe the population structure of fishes. Body shape variation, which is often environmentally induced, may provide a good record of short-term population structuring. However, factors unrelated to environmental or genetic influences on body morphology may complicate sampling and the use of morphometric features for stock discrimination. In the present study, we used geometric morphometric variables to compare the European sardine Sardina pilchardus putative stocks of the Aegean and Ionian Seas (eastern Mediterranean). Landmark data of fish collected at seven different sites were subjected to canonical analysis of principal coordinates (CAP). The average body condition of sardines from these sites was strongly and linearly related to corresponding scores along CAP1, the axis exhibiting the highest correlation with the morphometric data cloud. The average scores along CAP2 and CAP3 appeared to be linked to morphological differentiation related to temperature effects and prey availability (mesozooplankton biomass). Despite the primary and confounding effect of body condition, discrimination of different morphotypes corresponding to the Aegean and the Ionian Sea stocks was highly significant with 81% correct reallocations for the respective CAP model.

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Tublitz, N. J., and P. K. Loi. "Hormonal control of transmitter plasticity in insect peptidergic neurons. II. Steroid control of the up-regulation of bursicon expression." Journal of Experimental Biology 181, no. 1 (August 1, 1993): 195–212. http://dx.doi.org/10.1242/jeb.181.1.195.

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Each abdominal ganglion of the central nervous system of the tobacco hawkmoth, Manduca sexta contains four individually identified lateral neurosecretory cells (LNCs) that undergo a postembryonic transmitter switch in vivo. In the embryonic and caterpillar stages, the primary LNC transmitter is cardioacceleratory peptide 2 (CAP2), a myoregulatory peptide. During metamorphosis, these cells stop expressing CAP2 and instead produce bursicon, a classic insect peptide hormone responsible for cuticular tanning. We have previously reported that this transmitter plasticity is under the control of the insect steroid hormone 20-hydroxyecdysone (20-HE), which surges twice during the last larval instar. In that report we showed that the CAP2 decline is indirectly regulated by the first 20-HE rise, the commitment pulse (CP). Here we provide evidence that the rise in bursicon levels in the LNCs is directly triggered by the second 20-HE surge, the prepupal peak (PP). We performed several experimental manipulations that exposed LNCs to the PP without the CP; cells treated in this manner exhibited a significant rise in bursicon content. In contrast, bursicon levels remained unchanged in those LNCs exposed only to the CP. Exposure to the PP triggered a precocious increase in bursicon expression in LNCs from the penultimate larval stage. Increased bursicon levels in the LNCs were also induced by direct infusion of 20-HE. Taken together, the results of these experiments suggest that the rise in bursicon in the LNCs during metamorphosis is due to the direct action of the PP on the LNCs. Thus, the two 20-HE surges combine to regulate the CAP2-to-bursicon switch in the LNCs, the first acting indirectly to cause a decline in CAP2 levels and the second triggering a rise in bursicon expression, possibly by a direct action on the LNCs.

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24

Planès, Carole, Céline Leyvraz, Tokujiro Uchida, Milena Apostolova Angelova, Grégoire Vuagniaux, Edith Hummler, Michael Matthay, Christine Clerici, and Bernard Rossier. "In vitro and in vivo regulation of transepithelial lung alveolar sodium transport by serine proteases." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 6 (June 2005): L1099—L1109. http://dx.doi.org/10.1152/ajplung.00332.2004.

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The amiloride-sensitive epithelial sodium channel (ENaC) constitutes a rate-limiting step for sodium (Na+) and water absorption across lung alveolar epithelium. Recent reports suggested that ENaC is regulated by membrane-bound extracellular serine proteases, such as channel-activating proteases (CAPs). The objectives of this study were to examine the role of serine proteases in the regulation of transepithelial alveolar Na+ and water transport in vitro and in vivo and the expression of CAPs in rodent distal lung. In vitro experiments showed that inhibition of endogenous serine proteases by apical aprotinin 1) decreased ENaC-mediated currents in primary cultures of rat and mouse alveolar epithelial cells without affecting the abundance nor the electrophoretic migration pattern of biotinylated α- and β-ENaC expressed at the cell surface and 2) suppressed the increase in amiloride-sensitive short-circuit current induced by the β2-agonist terbutaline. RT-PCR experiments indicated that CAP1, CAP2, and CAP3 mRNAs were expressed in mouse alveolar epithelial cells, whereas CAP1 was also expressed in alveolar macrophages recovered by bronchoalveolar lavage. CAP1 protein was detected by Western blotting in rat and mouse alveolar epithelial cells, alveolar macrophages and bronchoalveolar lavage fluid. Finally, in vivo experiments revealed that intra-alveolar treatment with aprotinin abolished the increase in Na+-driven alveolar fluid clearance (AFC) induced by terbutaline in an in situ mouse lung model, whereas trypsin potentiated it. These results show that endogenous membrane-bound and/or secreted serine proteases such as CAPs regulate alveolar Na+ and fluid transport in vitro and in vivo in rodent lung.

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Bertling, Enni, Pirta Hotulainen, Pieta K. Mattila, Tanja Matilainen, Marjo Salminen, and Pekka Lappalainen. "Cyclase-associated Protein 1 (CAP1) Promotes Cofilin-induced Actin Dynamics in Mammalian Nonmuscle Cells." Molecular Biology of the Cell 15, no. 5 (May 2004): 2324–34. http://dx.doi.org/10.1091/mbc.e04-01-0048.

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Cyclase-associated proteins (CAPs) are highly conserved actin monomer binding proteins present in all eukaryotes. However, the mechanism by which CAPs contribute to actin dynamics has been elusive. In mammals, the situation is further complicated by the presence of two CAP isoforms whose differences have not been characterized. Here, we show that CAP1 is widely expressed in mouse nonmuscle cells, whereas CAP2 is the predominant isoform in developing striated muscles. In cultured NIH3T3 and B16F1 cells, CAP1 is a highly abundant protein that colocalizes with cofilin-1 to dynamic regions of the cortical actin cytoskeleton. Analysis of CAP1 knockdown cells demonstrated that this protein promotes rapid actin filament depolymerization and is important for cell morphology, migration, and endocytosis. Interestingly, depletion of CAP1 leads to an accumulation of cofilin-1 into abnormal cytoplasmic aggregates and to similar cytoskeletal defects to those seen in cofilin-1 knockdown cells, demonstrating that CAP1 is required for proper subcellular localization and function of ADF/cofilin. Together, these data provide the first direct in vivo evidence that CAP promotes rapid actin dynamics in conjunction with ADF/cofilin and is required for several central cellular processes in mammals.

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GORODSKI, CLAUDIO. "CLOSED MINIMAL HYPERSURFACES IN COMPACT SYMMETRIC SPACES." International Journal of Mathematics 03, no. 05 (October 1992): 629–51. http://dx.doi.org/10.1142/s0129167x92000291.

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W.Y. Hsiang, W.T. Hsiang and P. Tomter conjectured that every simply-connected, compact symmetric space of dimension ≥4 must contain some minimal hypersurfaces of sphere type. With the aid of equivariant differential geometry, they showed that this is in fact the case for many symmetric spaces of rank one and two. Let M be one of the symmetric spaces: Sn(1)×Sn(1)(n≥4), SU(6)/Sp(3), E6/F4, ℍP2 (quaternionic proj. plane) or CaP2 (Cayley proj. plane). We prove the existence of infmitely many immersed, minimal hypersurfaces of sphere type in M which are invariant under a certain group G of isometries of M. Following Hsiang and the others, the equivariant method is also used here to reduce the problem to an investigation of geodesics in M/G equipped with a metric (with singularities) depending only on the orbital geometry of the transformation group (G, M). However, our constructions are based on area minimizing homogeneous cones, corresponding to a corner singularity of M/G with the local geometry of nodal type; this can be viewed as a variation of some of their constructions which depended on some unstable minimal cones of focal type. We further apply the equivariant method to construct a minimal embedding of S1×Sn−1×Sn−1 into Sn(1)×Sn(1)(n≥2) and a minimal, embedded hypersurface of sphere type in [Formula: see text], ℍPn×ℍPn (n≥2) and CaP2×CaP2.

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27

Wolanski, Marian, Farhad Khosrowshahian, Lara Jerant, Ing-Suan Jap, Jennifer Brockman, and Michael J. Crawford. "Expression of CAP2 during early Xenopus embryogenesis." International Journal of Developmental Biology 53, no. 7 (2009): 1063–67. http://dx.doi.org/10.1387/ijdb.062158mw.

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28

Prier, K. R., O. H. Beckman, and N. J. Tublitz. "Modulating a modulator: biogenic amines at subthreshold levels potentiate peptide-mediated cardioexcitation of the heart of the tobacco hawkmoth Manduca sexta." Journal of Experimental Biology 197, no. 1 (December 1, 1994): 377–91. http://dx.doi.org/10.1242/jeb.197.1.377.

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The central nervous system of the moth Manduca sexta contains a group of myoregulatory neuropeptides, the CAPs (Cardioacceleratory Peptides), which cause a physiologically important, dose-dependent increase in heart rate during wing inflation and flight in adult moths. We report here that the response of the adult heart to a subset of the CAPs, the CAP2S, is potentiated nearly twofold in the chronic presence of subthreshold levels of the biogenic amine octopamine or near-threshold levels of the biogenic amine serotonin. Subthreshold levels of the CAP2S fail to alter the response of the heart to octopamine. We have begun to investigate the molecular mechanisms underlying this potentiation. Previous work on the adult heart has shown that the CAP2s act through an inositol-1,4,5-trisphosphate second-messenger system. Here, we demonstrate that the cardioexcitatory effects of the two amines, in contrast to those of the CAP2S, are both mediated by cyclic AMP. Application to the heart of either 10(-5) moll-1 octopamine or 10(-6)moll-1 serotonin elicits a threefold increase in intracellular cyclic AMP levels. The CAP2S have no effect on cyclic AMP levels in the heart. These results illustrate a mechanism by which the effectiveness of a neurohormone can be increased with minimal cost to the animal. In Manduca sexta, subthreshold levels of octopamine are found in the haemolymph during wing inflation and flight. Thus, it is possible that octopamine up-regulates the effects of CAP2 via a cyclic-AMP-dependent mechanism during these activities.

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Ferri, Josipa, Karmen Bartulin, and Frane Škeljo. "Variability of Otolith Morphology and Morphometry in Eight Juvenile Fish Species in the Coastal Eastern Adriatic." Croatian Journal of Fisheries 76, no. 3 (September 1, 2018): 91–98. http://dx.doi.org/10.2478/cjf-2018-0012.

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Abstract Sagittae otoliths of eight juvenile species: Boops boops, Diplodus vulgaris, Diplodus puntazzo, Sarpa salpa (family Sparidae), Liza ramada, Liza aurata (family Mugilidae), Atherina boyeri, Atherina hepsetus (family Atherinidae) were analysed and compared using descriptive morphological characters and morphometric indices. The noticeable differences among the otoliths of the investigated species are in their overall shape, margins (i.e. irregular, sinuate or crenate) and anterior region. Otolith shape varied from elliptic to pentagonal in sparids, elliptic to rectangular in mugilids and elliptic in two atherinids. Aspect ratio (OW/OL), ratio of the sulcus length occupied by the cauda length (CL/SL) and ratio of the sulcus length occupied by the ostium length (OSL/SL) were calculated for all species. The otolith contour was described using wavelets. The Canonical Analysis of Principal Coordinates (CAP) gave an overview of the otolith shape differentiation between eight juveniles. Using the Wavelet coefficients, the first principal component (CAP1) explained 58.1% of the variation among species and the second principal component (CAP2) 25.2%.

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Waddle, J. A., J. A. Cooper, and R. H. Waterston. "The alpha and beta subunits of nematode actin capping protein function in yeast." Molecular Biology of the Cell 4, no. 9 (September 1993): 907–17. http://dx.doi.org/10.1091/mbc.4.9.907.

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We cloned and analyzed two genes, cap-1 and cap-2, which encode the alpha and beta subunits of Caenorhabditis elegans capping protein (CP). The nematode CP subunits are 55% (cap-1) and 66% (cap-2) identical to the chicken CP subunits and 32% (cap-1) and 48% (cap-2) identical to the yeast CP subunits. Purified nematode CP made by expression of both subunits in yeast is functionally similar to chicken skeletal muscle CP in two different actin polymerization assays. The abnormal cell morphology and disorganized actin cytoskeleton of yeast CP null mutants are restored to wild-type by expression of the nematode CP subunits. Expression of the nematode CP alpha or beta subunit is sufficient to restore viability to yeast cap1 sac6 or cap2 sac6 double mutants, respectively. Therefore, despite evolution of the nematode actin cytoskeleton to a state far more complex than that of yeast, one important component can function in both organisms.

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Hubberstey, Andrew, Gang Yu, Robbie Loewith, Cherelyn Lakusta, and Dallan Young. "Mammalian CAP interacts with CAP, CAP2, and actin." Journal of Cellular Biochemistry 61, no. 3 (June 1, 1996): 459–66. http://dx.doi.org/10.1002/(sici)1097-4644(19960601)61:3<459::aid-jcb13>3.0.co;2-e.

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32

Tublitz, N. J., and J. W. Truman. "Insect cardioactive peptides. II. Neurohormonal control of heart activity by two cardioacceleratory peptides in the tobacco hawkmoth, Manduca sexta." Journal of Experimental Biology 114, no. 1 (January 1, 1985): 381–95. http://dx.doi.org/10.1242/jeb.114.1.381.

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The physiological characteristics of two cardioacceleratory peptides (CAPs) were analysed in the tobacco hawkmoth, Manduca sexta, to determine if either CAP functioned as a cardioregulatory neurohormone. In vivo heart recordings from pharate and newly emerged adults revealed a dramatic increase in heart rate associated with wing-spreading behaviour. Bioassay of whole blood taken from wing-spreading (WS) animals indicated the presence of a stage-specific, blood-borne cardioacceleratory factor(s). Gel filtration of WS blood identified two cardioacceleratory factors which co-eluted with the two CAPs. A depletion of the ventral nerve cord levels of both CAPs was observed during WS behaviour. Measurements of blood CAP levels showed that the peak CAP titres were coincident with the initiation of WS behaviour. Experimental manipulations that delayed the onset of WS behaviour also prevented CAP release. High potassium incubation evoked the release of both CAPs in a calcium-dependent manner. In vivo injections of CAP1 or CAP2 caused a dose-dependent increase in heart rate. These results confirm the hypothesis that both CAPs function as cardioregulatory neurohormones during wing-spreading behaviour in Manduca sexta.

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Shin, Myungjoo, Jolanda van Leeuwen, Charles Boone, and Anthony Bretscher. "Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables." Molecular Biology of the Cell 29, no. 8 (April 15, 2018): 923–36. http://dx.doi.org/10.1091/mbc.e17-10-0592.

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How cells balance the incorporation of actin into diverse structures is poorly understood. In budding yeast, a single actin monomer pool is used to build both actin cables involved in polarized growth and actin cortical patches involved in endocytosis. Here we report how Aim21/Tda2 is recruited to the cortical region of actin patches, where it negatively regulates actin assembly to elevate the available actin monomer pool. Aim21 has four polyproline regions and is recruited by two SH3-containing patch proteins, Bbc1 and Abp1. The C-terminal region, which is required for its function, binds Tda2. Cell biological and biochemical data reveal that Aim21/Tda2 is a negative regulator of barbed end filamentous actin (F-actin) assembly, and this activity is necessary for efficient endocytosis and plays a pivotal role in balancing the distribution of actin between cables and patches. Aim21/Tda2 also forms a complex with the F-actin barbed end capping protein Cap1/Cap2, revealing an interplay between regulators and showing the complexity of regulation of barbed end assembly.

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Fu, Jia, Min Li, Dan-Chun Wu, Li-Li Liu, Shi-Lu Chen, and Jing-Ping Yun. "Increased Expression of CAP2 Indicates Poor Prognosis in Hepatocellular Carcinoma." Translational Oncology 8, no. 5 (October 2015): 400–406. http://dx.doi.org/10.1016/j.tranon.2015.08.003.

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Swiston, John, Andrew Hubberstey, Gang Yu, and Dallan Young. "Differential expression of CAP and CAP2 in adult rat tissues." Gene 165, no. 2 (January 1995): 273–77. http://dx.doi.org/10.1016/0378-1119(95)00522-8.

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Peche, V., S. Shekar, M. Leichter, H. Korte, R. Schröder, M. Schleicher, T. A. Holak, et al. "CAP2, cyclase-associated protein 2, is a dual compartment protein." Cellular and Molecular Life Sciences 64, no. 19-20 (September 6, 2007): 2702–15. http://dx.doi.org/10.1007/s00018-007-7316-3.

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Peche, Vivek S., Tad A. Holak, Bhagyashri D. Burgute, Kosmas Kosmas, Sushant P. Kale, F. Thomas Wunderlich, Fatiha Elhamine, et al. "Ablation of cyclase-associated protein 2 (CAP2) leads to cardiomyopathy." Cellular and Molecular Life Sciences 70, no. 3 (September 4, 2012): 527–43. http://dx.doi.org/10.1007/s00018-012-1142-y.

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38

Ziati, Mounir, Sabir Hazourli, Sana Nouacer, and Fatma Zohra Khelaifia. "Elimination of arsenic (III) by adsorption on coal resulting from date pits and activated thermally and chemically." Water Quality Research Journal 47, no. 1 (February 1, 2012): 91–102. http://dx.doi.org/10.2166/wqrjc.2012.016.

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The objective of this study is the valorisation of a lignocellulosic natural residue, date pits, and its application in the removal by adsorption of the arsenic (III) contained in water. The chronological stages in obtaining coal were: cleaning, drying, crushing and finally either a thermal treatment by pyrolysis at 900 °C (CAP1) or a chemical pretreatment with iron oxide of the natural residue followed by carbonisation at 600 °C (CAP2). The choice of iron oxide is based on the fact that arsenic (III) has strong affinities for the hydroxide and oxide of this metal. The characterisation of the carbonaceous matter showed properties comparable with those of many industrially produced coals. Retention tests of arsenic (III) on the two adsorption materials studied gave a maximum capacity of adsorption (at 20 °C and 24 h of contact time) of about 25 mg/g for the chemically activated carbon and 21 mg/g for the thermally activated one. The study of the influence of pH and temperature showed that at neutral pH and ambient temperature (T = 20 °C), the optimal adsorption of arsenic (III) follows quite closely the Langmuir and Freundlich models. The kinetics of adsorption is slow and is of pseudo-second order type.

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Palmgren, Sandra, Pauli J. Ojala, Martin A. Wear, John A. Cooper, and Pekka Lappalainen. "Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin." Journal of Cell Biology 155, no. 2 (October 15, 2001): 251–60. http://dx.doi.org/10.1083/jcb.200106157.

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Twinfilin is a ubiquitous actin monomer–binding protein that regulates actin filament turnover in yeast and mammalian cells. To elucidate the mechanism by which twinfilin contributes to actin filament dynamics, we carried out an analysis of yeast twinfilin, and we show here that twinfilin is an abundant protein that localizes to cortical actin patches in wild-type yeast cells. Native gel assays demonstrate that twinfilin binds ADP-actin monomers with higher affinity than ATP-actin monomers. A mutant twinfilin that does not interact with actin monomers in vitro no longer localizes to cortical actin patches when expressed in yeast, suggesting that the ability to interact with actin monomers may be essential for the localization of twinfilin. The localization of twinfilin to the cortical actin cytoskeleton is also disrupted in yeast strains where either the CAP1 or CAP2 gene, encoding for the α and β subunits of capping protein, is deleted. Purified twinfilin and capping protein form a complex on native gels. Twinfilin also interacts with phosphatidylinositol 4,5-bisphosphate (PI[4,5]P2), and its actin monomer–sequestering activity is inhibited by PI(4,5)P2. Based on these results, we propose a model for the biological role of twinfilin as a protein that localizes actin monomers to the sites of rapid filament assembly in cells.

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Sizonenko, G. I., T. S. Karpova, D. J. Gattermeir, and J. A. Cooper. "Mutational analysis of capping protein function in Saccharomyces cerevisiae." Molecular Biology of the Cell 7, no. 1 (January 1996): 1–15. http://dx.doi.org/10.1091/mbc.7.1.1.

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To investigate physiologic functions and structural correlates for actin capping protein (CP), we analyzed site-directed mutations in CAP1 and CAP2, which encode the alpha and beta subunits of CP in Saccharomyces cerevisiae. Mutations in four different regions caused a loss of CP function in vivo despite the presence of mutant protein in the cells. Mutations in three regions caused a complete loss of all aspects of function, including the actin distribution, viability with sac6, and localization of CP to actin cortical patches. Mutation of the fourth region led to partial loss of only one function-formation of actin cables. Some mutations retained function and exhibited the complete wild-type phenotype, and some mutations led to a complete loss of protein and therefore loss of function. The simplest hypothesis that can explain these results is that a single biochemical property is necessary for all in vivo functions. This biochemical property is most likely binding to actin filaments, because the nonfunctional mutant CPs no longer co-localize with actin filaments in vivo and because direct binding of CP to actin filaments has been well established by studies with purified proteins in vitro. More complex hypotheses, involving the existence of additional biochemical properties important for function, cannot be excluded by this analysis.

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Kolattukudy, Pappachan E., Daoxin Li, Cheng-Shine Hwang, and Moshe A. Flaishman. "Host signals in fungal gene expression involved in penetration into the host." Canadian Journal of Botany 73, S1 (December 31, 1995): 1160–68. http://dx.doi.org/10.1139/b95-373.

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Fungal spores, on contact with their hosts, perceive the plant signals and consequently initiate gene expression that enables the fungus to penetrate through the host barriers. Germination and appressorium formation by Colletotrichum gloeosporioides spore is induced by host surface wax on the growing avocado (Persea americana) fruits and, at ripening of the fruit, ethylene induces multiple appressorium formation. Both the wax and ethylene may use phosphorylation of 29- and 43-kDa proteins in the signal transduction. Unique genes that are expressed during appressorium formation induced by the host signal were cloned and sequenced. These include cap3 and cap5 that encode cysteine-rich small proteins, cap22 that encodes a secreted glycoprotein found in the appressorial wall, and cap20 whose disruption drastically decreases virulence. Disruption of cutinase gene drastically reduces the virulence of Fusarium solani pisi on pea (Pisum sativum L.). The promoter elements in cutinase gene involved in the induction of this gene by the hydroxy fatty acid monomers of cutin were identified and transcription factors that bind these elements were cloned. One of them, that binds to a palindrome, essential for cutinase induction, was found to be phosphorylated. Several proteins kinases from F. solani pisi were cloned. Key words: appressorium, cutin, cutinase, ethylene, gene disruption, protein phosphorylation, protein kinase, transcription factor.

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Xiong, Yao, Georgina K. Cox, Kenneth Bedi, Kenneth B. Margulies, Simon Berritt, and Jeffrey M. Field. "CAP2 loss activated MRTF/SRF signaling through actin dynamics in cardiomyocytes." Proceedings for Annual Meeting of The Japanese Pharmacological Society WCP2018 (2018): OR15–5. http://dx.doi.org/10.1254/jpssuppl.wcp2018.0_or15-5.

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Mewis, A. "Eine mit Tetraederketten aufgef�llte Rutilstruktur: Die Verbindung CaCu4P2?CaP2(Cu4)." Zeitschrift f�r anorganische und allgemeine Chemie 545, no. 2 (February 1987): 43–46. http://dx.doi.org/10.1002/zaac.19875450205.

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44

Wan, Ying, Shengkui Qiu, Lei Yin, Xuesong Gao, Yasu Jiang, Shichun Feng, and Chong Tang. "CAP2 contributes to tumorigenesis in gastric cancer by targeting transcription factor SOX9." Journal of Gastrointestinal Oncology 12, no. 2 (April 2021): 268–77. http://dx.doi.org/10.21037/jgo-20-234.

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45

Peche, Vivek S., Tad A. Holak, Bhagyashri D. Burgute, Kosmas Kosmas, Sushant P. Kale, F. Thomas Wunderlich, Fatiha Elhamine, et al. "Erratum to: Ablation of cyclase-associated protein 2 (CAP2) leads to cardiomyopathy." Cellular and Molecular Life Sciences 74, no. 21 (August 29, 2017): 4045. http://dx.doi.org/10.1007/s00018-017-2630-x.

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Hurley, T. W., and R. W. Brinck. "Regulating transient and sustained changes of cytosolic Ca2+ in rat pancreatic acini." American Journal of Physiology-Cell Physiology 258, no. 1 (January 1, 1990): C54—C61. http://dx.doi.org/10.1152/ajpcell.1990.258.1.c54.

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The regulation of changes in cytosolic Ca2+ concentration (Cai2+) during exposure to carbachol was studied in rat pancreatic acini loaded with fura-2. With an extracellular Ca2+ concentration (Cao2+) of 2.5 mM, resting Cai2+ is 185 +/- 48 (SD) nM (n = 23), which rises to 696 +/- 222 nM, then falls over 2 min to a stable plateau of 401 +/- 106 nM. With Cao2+ less than 10 nM, carbachol produces an immediate threefold increase in Cai2+ that dissipates over 2-3 min, and Cai2+ steadily falls below prestimulation levels. Atropine prevents all responses to carbachol, and when it is added during a response to carbachol, Cai2+ drops to resting values within seconds. Ca2+ influx is required for the prolonged elevation of Cai2+ during carbachol exposure, but Ca2+ entry is not regulated by an increase in Cai2+ itself nor does Ca2+ enter via voltage-gated L-type channels. The muscarinic receptor-operated Ca2+ entry mechanism is sensitive to Cao2+, since sustained elevations in Cai2+ are maximal at 2.5 mM Cao2+ but are much less pronounced at lower external Ca2+ concentrations.

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Zhao, Liming, Fadi Li, Lvfeng Yuan, Xiaoxue Zhang, Deyin Zhang, Xiaolong Li, Yukun Zhang, et al. "Expression of ovine CTNNA3 and CAP2 genes and their association with growth traits." Gene 807 (January 2022): 145949. http://dx.doi.org/10.1016/j.gene.2021.145949.

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Ma, Dongying, Ivo M. B. Francischetti, Jose M. C. Ribeiro, and John F. Andersen. "The structure of hookworm platelet inhibitor (HPI), a CAP superfamily member fromAncylostoma caninum." Acta Crystallographica Section F Structural Biology Communications 71, no. 6 (May 20, 2015): 643–49. http://dx.doi.org/10.1107/s2053230x1500271x.

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Secreted protein components of hookworm species include a number of representatives of the cysteine-rich/antigen 5/pathogenesis-related 1 (CAP) protein family known asAncylostoma-secreted proteins (ASPs). Some of these have been considered as candidate antigens for the development of vaccines against hookworms. The functions of most CAP superfamily members are poorly understood, but one form, the hookworm platelet inhibitor (HPI), has been isolated as a putative antagonist of the platelet integrins αIIbβ3and α2β1. Here, the crystal structure of HPI is described and its structural features are examined in relation to its possible function. The HPI structure is similar to those of other ASPs and shows incomplete conservation of the sequence motifs CAP1 and CAP2 that are considered to be diagnostic of CAP superfamily members. The asymmetric unit of the HPI crystal contains a dimer with an extensive interaction interface, but chromatographic measurements indicate that it is primarily monomeric in solution. In the dimeric structure, the putative active-site cleft areas from both monomers are united into a single negatively charged depression. A potential Lys-Gly-Asp disintegrin-like motif was identified in the sequence of HPI, but is not positioned at the apex of a tight turn, making it unlikely that it interacts with the integrin. Recombinant HPI produced inEscherichia coliwas found not to inhibit the adhesion of human platelets to collagen or fibrinogen, despite having a native structure as shown by X-ray diffraction. This result corroborates previous analyses of recombinant HPI and suggests that it might require post-translational modification or have a different biological function.

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Yoon, Sarah, Boram Shin, and Hyun Goo Woo. "Endoplasmic Reticulum Stress Induces CAP2 Expression Promoting Epithelial-Mesenchymal Transition in Liver Cancer Cells." Molecules and Cells 44, no. 8 (August 31, 2021): 569–79. http://dx.doi.org/10.14348/molcells.2021.0031.

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Erne, Paul, and Kent Hermsmeyer. "Intracellular Cap2+ Release in Vascular Muscle Cells by Caffeine, Ryanodine, Norepinephrine, and Neuropeptide Y." Journal of Cardiovascular Pharmacology 12, Supplement (1988): 85–91. http://dx.doi.org/10.1097/00005344-198800125-00015.

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Journal articles on the topic 'CAP2'

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