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Dissertations / Theses on the topic 'Calcium-binding proteins'

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Published: 4 June 2021

Last updated: 29 July 2024

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1

Castiblanco, Alfonso Adriana Patricia. "Expression and purification of engineered calcium binding proteins." unrestricted, 2009. http://etd.gsu.edu/theses/available/etd-04212009-135436/.

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Thesis (M.S.)--Georgia State University, 2009.
Title from file title page. Jenny J. Yang, committee chair; Zhi-Ren Liu, Gangli Wang, Giovanni Gadda, committee members. Description based on contents viewed June 30, 2009. Includes bibliographical references (p. 116-119).

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2

Castiblanco, Alfonso Adriana Patricia. "Expression and purification of engineered calcium binding proteins /." unrestricted, 2006. http://etd.gsu.edu/theses/available/etd-04212009-135436/.

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Thesis (M.S.)--Georgia State University, 2009.
Jenny J. Yang, committee chair; Zhi-Ren Liu, Gangli Wang, Giovanni Gadda, committee members. Typescript. Includes bibliographical references (leaves 101-104). Also available via the World Wide Web.

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3

Prichard, Lisa. "The role of the IQ motif, a protein kinase C and calmodulin regulatory domain, in neuroplasticity, RNA processing, and RNA metabolism /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/6302.

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4

Castiblanco, Adriana P. "Expression and Purification of Engineered Calcium Binding Proteins." Digital Archive @ GSU, 2009. http://digitalarchive.gsu.edu/chemistry_theses/20.

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Previous studies in Dr. Yang’s laboratory have established a grafting, design, and subdomain approach in order to investigate the properties behind Ca2+-binding sites located in Ca2+-binding proteins by employing engineered proteins. These approaches have not only enabled us to isolate Ca2+-binding sites and obtain their Ca2+-binding affinities, but also to investigate conformational changes and cooperativity effects upon Ca2+ binding. The focus of my thesis pertains to optimizing the expression and purification of engineered proteins with tailored functions. Proteins were expressed in E. coli using different cell strains, vectors, temperatures, and inducer concentrations. After rigorous expression optimization procedures, proteins were further purified using chromatographic and/or refolding techniques. Expression and purification optimization of proteins is essential for further analyses, since the techniques used for these studies require high protein concentrations and purity. Evaluated proteins had yields between 5-70 mg/L and purities of 80-90% as confirmed by SDS-PAGE electrophoresis.

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5

Campbell, Joanne A. "Calcium-binding, low salt soluble human aortic proteins." Thesis, Queen's University Belfast, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.388054.

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6

Maddox, Katherine. "A characterization of the calcium- and integrin-binding protein family." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 112 p, 2009. http://proquest.umi.com/pqdweb?did=1654487501&sid=7&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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7

Gilchrist, James Stuart Charles. "Calcium regulation of calcium transport by sarcoplasmic reticulum." Thesis, University of British Columbia, 1990. http://hdl.handle.net/2429/30880.

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The sarcoplasmic reticulum (SR) of skeletal muscle is an intracellular membraneous network that, through the cyclical release and re-uptake of Ca²⁺ into and from, respectively, the cytoplasmic space, regulates myofilament shortening and, therefore, muscle contraction. SR derived from the terminal cisternae (HSR) demonstrates the property of Ca²⁺-induced Ca²⁺ release. Upon attainment of a threshold intralumenal Ca²⁺ load, application of a small pulse of extralumenal Ca²⁺ stimulates the release of a pool of intralumenal Ca²⁺ via the ligand gated Ca²⁺ permeable pore of the Ca²⁺ release channel/ryanodine receptor complex. It was hypothesised that intralumenal Ca²⁺ regulates the opening of the release channel. HSR vesicles were purified from skeletal and cardiac muscle by a novel technique. Structural characterisation of these membranes demonstrated an enrichment of harvested fractions in the Ca²⁺ release channel and the intralumenal Ca²⁺ binding protein, calsequestrin. In radiometric studies, skeletal HSR vesicles were shown to bind ryanodine with high capacity at both low and high affinity sites, with 2 fold stimulation of Ca²⁺ accumulation by the polyorganic cation Ca²⁺ channel blocker, ruthenium red. HSR vesicles passively loaded Ca²⁺. Passive loading of HSR vesicles with Ca²⁺ was found to be non-linearly dependent upon the concentration of Ca²⁺ within the loading medium. This suggested the presence of 2 intralumenal Ca²⁺ binding sites with different affinities for Ca²⁺. A spectroscopic dual-wavelength assay of Ca²⁺ release was developed that took advantage of peculiar spectral properties of the metallochromic sensitive dye Antipyrylazo III. In the presence of mM MgATP and mM Mg2+ the initial fast phase of HSR Ca²⁺ was well resolved. Evidence was presented that initial rapid uptake was associated with high affinity binding to an intralumenal compartment. Ca²⁺ -induced Caz+ release was shown to occur with a threshold loading of intralumenal Ca²⁺. The intralumenal Ca²⁺ threshold for Ca²⁺-induced Ca²⁺ release was decreased in the presence of ryanodine. Ryanodine induced Ca²⁺ release was also dependent upon the amount of intralumenal Ca²⁺. Ryanodine was also shown to inhibit sustained Ca²⁺-induced Ca²⁺ release by apparent inhibition of the binding of Ca²⁺ to intralumenal sites. These results suggested that junctional state transitions of the Ca²⁺ channel and calsequestrin were interdependent. Purified mM and mM Ca²⁺ activated neutral protease isoforms selectively cleaved the Ca²⁺ channel into 410 and 150kDa peptides with limited proteolysis. This was demonstrated in both HSR vesicles and the purified Ca²⁺ release channel. A novel 88kDa protein was also shown to be fragmented by both CANP isoforms. The identity of this prominent HSR associated protein remains obscure. CANP fragmentation of HSR protein elevated passive and active 4^Ca²⁺ loading in vesicles. This indicated that selective structural modification of the cytoplasmic portion of the release channel modified the comformational states of a intralumenal Ca²⁺ binding compartment in HSR vesicles. In spectroscopic studies, CANP proteolysis of HSR proteins increased the sensitivity to Ca²⁺ and ryanodine-induced Ca²⁺ release through decreases in the required intralumenal Ca²⁺ threshold for release. These functional alterations coincided with apparent single site cleavage of the release channel. Further proteolysis of the initial 410 and 150kDa peptides was without further significant effect upon function. Based upon the hypothesis that primary sequences rich in proline (P), glutamate (E), aspartate (D), serine (S) and threonine (T) (PEST regions) are recognition sites for CANP binding to substrates, a search for PEST regions within the Ca²⁺ channel was undertaken. It was tentatively proposed that two PEST regions near the N-terminal of the Caz release channel may represent sites close to the CANP cleavage site. The results of this work were discussed in relation to a possible role of Ca²⁺-induced Ca²⁺ release in regulating the patterning of Ca²⁺ cytosolic transients. The frequency and amplitude of cytosolic Ca²⁺ transients appear to be important in regulating protein expression. The requirement of intralumenal Ca²⁺-induced Ca²⁺ release may be a means by which the cyclical uptake and release of Ca²⁺ during muscle relaxation and contraction can be coordinated. This coordination may define the patterning of cytosolic Ca²⁺ transients. The increased sensitivity to Ca²⁺-induced Ca²⁺ release by HSR after CANP treatment may represent a means by which the patterning of cytosolic Ca²⁺ transients can be altered to effect changes in protein synthesis.
Graduate and Postdoctoral Studies
Graduate

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8

Agah, Sayeh. "Parvalbumin stability and calcium affinity : the impact of the n-terminal domain /." Free to MU Campus, others may purchase, 2004. http://wwwlib.umi.com/cr/mo/fullcit?3164486.

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9

Ayar, Ahmet. "An investigation of calcium-induced calcium-release (CICR) in cultured rat sensory neurones." Thesis, University of Aberdeen, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285521.

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In this study the mechanisms of Ca²⁺-induced-Ca²⁺-release, effects of membrane depolarizations and the actions of pharmacological intracellular Ca²⁺-modulators were examined in cultured rat dorsal root ganglion (DRG) neurones. The whole cell configuration of the patch clamp technique was used to record action potentials, action potential after-potentials and voltage-activated calcium currents, (I_Ca), calcium-activated chloride currents, (I_CI(Ca)), and non-selective cation currents, (I_CAN), under current and voltage clamp recording conditions, respectively. A sub population of DRG neurones expressed action potential after-depolarizations and I_CI(Ca)tail currents which were due to activation of Ca²⁺-activated Cl^- channels as a result of Ca²⁺ entry. I_CANwas dominantly activated due to Ca²⁺ release from intracellular stores evoked by pharmacological Ca²⁺-releasing agents such as caffeine, ryanodine and dihydrosphingosine. Calcium-activated conductances were identified by estimating reversal potentials of the activated currents, using selective pharmacological blockers and extracellular ionic replacement studies. Calcium-dependence of activated currents was also examined by using high concentration of intracellular Ca²⁺ buffer, EGTA, to prevent elevation of intracellular Ca²⁺-levels and by rapidly buffering raised intracellular Ca²⁺ using intracellular 'caged Ca²⁺ chelator', diazo-2. The involvement of intracellular Ca²⁺- stores was examined by performing experiments in Ca²⁺-free extracellular recording medium and pharmacologically inhibiting release of Ca²⁺ from intracellular stores, using dantrolene. Ryanodine had complex actions on DRG neurones, which reflected its ability to mobilize Ca²⁺, deplete Ca²⁺ stores, and inhibit Ca²⁺ release channels. Ryanodine inhibited action potential after-depolarizations and I_CI(Ca)tail currents by interacting with intracellular stores and preventing amplification of Ca²⁺ signalling by CICR. It was found that CICR observed under physiological conditions in rat DRG neurones involves intracellular Ca²⁺stores which were sensitive to ryanodine. In addition to ryanodine sensitivity these intracellular Ca²⁺ stores could be mobilized by caffeine and dihydrosphingosine.

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10

Skene, Robert J. "Crystallographic studies of calcium-binding proteins, aeromonas salmonicida surface array protein and calmodulin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ64978.pdf.

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11

Abougou, Jean-Claude. "Biochemical properties of caldesmon." Diss., The University of Arizona, 1988. http://hdl.handle.net/10150/184604.

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An attempt to develop a short and reliable method of caldesmon purification led to the development of three procedures of caldesmon purification. The first method was seldom used because of its low yield and the lack of caldesmon endogenous kinase activity. However, it allowed us to purify MLCK (myosin light chain kinase). The second and third methods gave respectively, a caldesmon sample with and without kinase activity. We were able to localize the endogenous kinase in the 0-30% ammonium sulfate precipitated DEAE pellet but we were unsuccessful at purifying the kinase to homogeneity. We found that caldesmon can also be phosphorylated by rat brain Ca²⁺-calmodulin-dependent kinase II at sites identical to those of caldesmon endogenous kinase but different to those of kinase C. In addition, caldesmon and its endogenous kinase are two different proteins. Furthermore, our study of caldesmon inhibition of actomyosin ATPase activity showed that further research needs to be done to refute F-actin bundling process as a possible cause of caldesmon inhibition of actomyosin ATPase activity. In addition, our studies of caldesmon inhibition of HMM and S-1 ATPase activity suggest that S-2 might be partially involved in the inhibition mechanism. Finally, caldesmon did not affect the 6S-10S transition of myosin conformation and since caldesmon cannot compete against higher affinity calmodulin-binding protein such as MLCK thus, the flip-flop theory is untenable.

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12

Blamey, Chad Joseph. "Calcium- and integrin-binding protein 1 structure and function /." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 3.06 Mb., p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3220732.

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Thesis (Ph.D.)--University of Delaware, 2006.
Principal faculty advisors: Ulhas P. Naik, Dept. of Biological Sciences and Brian J. Bahnson, Dept. of Chemistry and Biochemistry. Includes bibliographical references.

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13

Jones, Lisa Michelle. "Using Protein Design to Understand the Role of Electrostatic Interactions on Calcium Binding Affinity and Molecular Recognition." Digital Archive @ GSU, 2008. http://digitalarchive.gsu.edu/chemistry_diss/16.

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Calcium regulates many biological processes through interaction with proteins with different conformational, dynamic, and metal binding properties. Previous studies have shown that the electrostatic environment plays a key role in calcium binding affinity. In this research, we aim to dissect the contribution of the electrostatic environment to calcium binding affinity using protein design. Many natural calcium binding proteins undergo large conformational changes upon calcium binding which hampers the study of these proteins. In addition, cooperativity between multiple calcium binding sites makes it difficult to study site-specific binding affinity. The design of a single calcium binding site into a host system eliminates the difficulties that occur in the study of calcium binding affinity. Using a computer algorithm we have rationally designed several calcium binding sites with a pentagonal bipyramidal geometry in the non-calcium dependent cell adhesion protein CD2 (CD2-D1) to better investigate the key factors that affect calcium binding affinity. The first generation proteins are all in varying electrostatic environments. The conformational and metal binding properties of each of these designed proteins were analyzed. The second generation designed protein, CD2.6D79, was designed based on criteria learned from the first generation proteins. This protein contains a novel calcium binding site with ligands all from the â-strands of the non-calcium dependent cell adhesion protein CD2. The resulting protein maintains native secondary and tertiary packing and folding properties. In addition to its selectivity for calcium over other mono and divalent metal ions, it displays strong metal binding affinities for calcium and its analogues terbium and lanthanum. Furthermore, our designed protein binds CD48, the ligand binding partner of CD2, with an affinity three-fold stronger than CD2. The electrostatic potential of the calcium binding site was modified through mutation to facilitate the study of the effect of electrostatic interactions on calcium binding affinity. Several charge distribution mutants display varying metal binding affinities based on their charge, distance to the calcium binding site, and protein stability. This study will provide insight into the key site factors that control calcium binding affinity and calcium dependent biological function.

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14

Keating, Suzanne Dawn. "Effects of lipocortin 1 over- and under-expression in a monocyte cell line." Thesis, Queen Mary, University of London, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.251883.

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15

Sweeney, Patricia J. "NMR analysis of drug interactions with isotopically labelled calmodulin." Thesis, University of Hertfordshire, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.303390.

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16

DeFord, James H. (James Henry) 1956. "Analysis of the Trypanosoma brucei Genome and Identification and Characterization of a Gene Family Encoding Putative EF-Hand Calcium-Binding Proteins." Thesis, University of North Texas, 1998. https://digital.library.unt.edu/ark:/67531/metadc278592/.

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The flagellum of Trypanosoma brucei contains a family of antigenically related EF-hand calcium-binding proteins which are called the calflagins. Genomic Southern blots indicated that multiple copies of calflagin genes occur in T brucei. All of the copies were contained in a single 23 kb Xhol-Xhol fragment. Genomic fragments of 2.5 and 1.7 kb were cloned that encoded calflagin sequences. Two new members of the calflagin family were found from genomic clone sequences. The deduced amino acid sequences of the genomic clones showed the calflagin genes were arranged tandemly along the genomic fragments and were similar to previously described calflagins. The calflagin genes were related by two unrelated 3' flanking sequences. An open reading frame that was unrelated to any calflagin was found at the 5' end of the 2.5 kb genomic fragment. Each encoded protein (~24,000u) contained three EF-hand calcium-binding motifs and one degenerate EF-hand motif. In general, variability among the T. brucei calflagins is greater than related proteins in T. lewisii and T. cruzi. This variability results from amino acid substitutions at the amino and carboxy termini, and duplication of internal segments.

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Kirberger, Michael. "Defining a Molecular Mechanism for Lead Toxicity via Calcium-Binding Proteins." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/chemistry_diss/53.

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Essential metals like Ca2+ and Zn2+ play critical roles in biological processes through protein interactions. Conversely, non-essential metals (e.g., Gd3+ and Pb2+) also interact with proteins, often with toxic effects. Molecular metal toxicity is assumed to be due to ionic displacement, and studies have demonstrated that Pb2+ replaces Zn2+, Ca2+ and other essential metals in proteins. The focus of this work was to compare protein Ca2+ and Pb2+ -binding sites and to investigate a mechanism of Pb2+ toxicity in Ca2+-binding proteins, particularly the intracellular trigger protein calmodulin (CaM) which binds four Ca2+ ions and interacts with numerous molecular targets via Ca2+-induced conformational change. A statistical analysis of PDB structural data for Pb2+ and Ca2+-binding (EF-hand and non-EF-hand) proteins revealed fewer binding ligands in Pb2+ sites (4 ± 2), than non-EF-Hand (6 ± 2) and EF-Hand (7 ± 1) Ca2+-binding sites. Pb2+ binds predominantly with sidechain Glu (38.4%), which is less prevalent in both non-EF-Hand (10.4%) and EF-Hand (26.6%) sites. Interestingly, analyses of proteins where Pb2+ replaces Ca2+ (calmodulin) or Zn2+ (5-aminolaevulinic acid dehydratase) revealed structural changes presumably unrelated to ionic displacement. These results suggested that Pb2+ adopts diverse binding geometries and that opportunistic binding outside of known Ca2+-binding sites may play a role in molecular metal toxicity. Ca2+-binding affinities (Kd) using phenylalanine and tyrosine fluorescence were found to be 1.15 ± 0.68 X 10-5 M and 2.04 ± 0.02 X 10-6 M for the N- and C-terminal domains, respectively. The Kd for Pb2+-binding in the N-terminal domain, 1.40 ± 0.30 X 10-6 M, was 8-fold higher than Ca2+. Binding of Pb2+ in the C-terminal domain produced a biphasic response with Kd values 7.34 ± 0.95 X 10-7 M and 1.93 ± 0.32 X 10-6 M, suggesting a single higher affinity Pb2+-binding site in the C-terminal domain with nearly equivalent affinity for the remaining sites. Competitive effects of Pb2+ added to Ca2+-loaded CaM were examined using multiple NMR techniques. Pb2+ was found to displace Ca2+ only in the N-terminal domain, however structural/dynamic changes were observed in the central helix apparently due to Pb2+-binding in secondary sites. These data supported our hypothesis that CaM structure and function is altered by opportunistic Pb2+-binding.

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18

Taylor, Clare Teresa. "Complement-binding proteins and intracellular calcium in human sperm-oocyte interaction." Thesis, University of Liverpool, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337139.

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19

Schacht, Teresa [Verfasser]. "Neuronal calcium-binding protein 2 (NECAB2): Charakterisierung eines striatalen Ca 2+ -bindenden Proteins / Teresa Schacht." Mainz : Universitätsbibliothek Mainz, 2017. http://d-nb.info/1141937689/34.

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20

Rahimi, Ahmed Farid Medical Sciences Faculty of Medicine UNSW. "Regulation of inflammation-associated S100 proteins in fibroblasts and their expression in atherosclerosis." Awarded by:University of New South Wales. School of Medical Sciences, 2004. http://handle.unsw.edu.au/1959.4/20503.

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The multigene family of Ca2+-binding S100 proteins comprises 22 members that have various important intra- and extracellular roles. The three inflammation-associated members of this family???S100A8, S100A9 and S100A12 (collectively termed "calgranulins")???are constitutive neutrophil and monocyte proteins also expressed by macrophages within acute and chronic inflammatory lesions, but not in tissue macrophages. They are expressed in human/murine wounds and by appropriately activated macrophages, microvascular endothelial cells and keratinocytes in vitro. The " calgranulins" are implicated in leukocyte activation/deactivation, fatty acid transport, leukocyte/fibroblast chemotaxis, transmigration and adhesion, embryogenesis, wound healing, protection against oxidants and antibacterial defence. Chapter 3 of this thesis explores growth-factor- and cytokine-mediated regulation and expression of S100A8 and S100A9 in fibroblasts, and demonstrates spatio-temporal expression of S100A8 in rat dermal wounds. Fibroblasts are stromal resident cells with important regulatory immune-inflammatory functions in wound healing, tissue remodelling and fibrosis. Fibroblast migration, proliferation, differentiation and their synthetic repertoire are modulated by various factors including extracellular matrix components, growth factors, prostaglandins, reactive oxygen species and cytokines. Fibroblast growth factor-2 (FGF-2), interleukin-1?(IL-1? and platelet-derived growth factor (PDGF) are potent fibroblast mitogens; PDGF and transforming growth factor-? (TGF-? are fibroblast chemoattractants. FGF-2 and IL-1?promote fibroblast proliferation, whereas TGF-?promotes myofibroblast differentiation and collagen production. Lipopolysaccharide (LPS), interferon ?(IFN?, tumour-necrosis factor ? (TNF?, TGF-?and PDGF did not induce the S100A8 gene in fibroblasts whereas FGF-2 (25 ng/ml) maximally induced mRNA 12 hr. after stimulation and this declined over 36 hr. The FGF-2 response was strongly enhanced and prolonged by optimal levels of heparin (1-10 IU/ml), maximally at 18 hr. post-stimulation. FGF-2/heparin-induced responses depended on cell-cell contact in vitro. IL-1?(10 U/ml) alone, or in synergy with FGF-2/heparin strongly induced the gene in 3T3 and primary fibroblasts. Dexamethasone (10???6 M) enhanced LPS- and FGF-2/-IL-1?induced responses. S100A9 mRNA was not induced by any of these mediators. Induction of S100A8 in the absence of S100A9 was confirmed in primary fibroblast-like cells by real-time reverse-transcriptase polymerase chain-reaction. FGF-2-heparin- and IL-1?induced mRNA expression depended on de-novo protein synthesis and was partially mediated by the mitogenactivated protein kinase pathway of activation. Preliminary promoter deletion analyses indicated that FGF-2-responsive elements in the gene promoter were distinct from those responsive to IL-1? TGF-?(2 ng/ml) significantly suppressed gene induction mediated by FGF-2 ?heparin/LPS/dexamethasone, but not by IL-1? TGF-?may compromise mRNA stability. Protein levels in FGF-2-heparin-IL-1?stimulated fibroblasts correlated well with mRNA levels and expression was mainly cytoplasmic. Immunohistochemistry indicated S100A8 associated with keratinocytes, neutrophils, macrophage-like cells and some hair follicles in wounded rat skin. Rat wounds also contained numerous S100A8- positive fibroblast-like cells 2 and 4 days post-injury; numbers declined by 7 days. Upregulation of S100A8 by FGF-2/IL-1? down-regulation by TGF-? and time-dependent expression of S100A8 in wound fibroblasts suggest a role in fibroblast differentiation at sites of inflammation and repair. Intracellular fibroblast-derived S100A8 may also regulate intracellular redox equilibrium and antioxidant defence. Atherosclerosis is a progressive chronic disease with complex aetiology and pathogenesis. S100A1 and S100B are associated with dendritic cells and lymphocytes in experimental rodent and human atherosclerotic lesions. Monocytes and macrophages in plaques of ApoE???/??? mice express S100A9 but not S100A8. Myeloperoxidase and HOClmediated oxidative mechanisms are fundamental in the pathogenesis of atherosclerosis and S100A8 is exquisitely sensitive to HOCl oxidation which generates sulphinamide bonds, novel non-reducible cysteine-lysine covalent bonds. Chapter 4 of this thesis presents novel evidence that, in contrast to the murine ApoE???/??? model, the three human " calgranulins" were expressed in human atherosclerotic plaques, but not in normal arteries. High levels of S100A8, S100A9 and S100A12 were evident in macrophages and foam cells. Some neovessels were anti-S100A8-/anti-S100A9-immunoreactive; S100A9 staining was also evident on the extracellular matrix. Patterns of expression of S100A8, S100A9 and S100A12 were overlapping in serial sections, except that only smooth muscle cells were S100A12-positive. S100A8 and S100A9 mRNA were also expressed by macrophages, foam cells and endothelial cells, indicating gene up-regulation rather than passive protein uptake. Western blotting of plaque extracts revealed monomeric S100A8, S100A9 and S100A12 and larger complexes. Some were resistant to reduction, suggesting non-disulfide covalent cross-linking, possibly via sulphinamide bonds. Stable S100A8-S100A9 complexes were also detected after immunoaffinity purification. In an in-vitro system, molar ratios of HOCl of >1 generated stable complexes of S100A8 and S100A9 whereas ~800 and ~100-fold excess HOCl oxidises apolipoprotein B-100 and BSA, respectively. S100A8 and S100A9 protected low-density lipoprotein (LDL) against HOCl oxidation in a thiol-independent manner. Because HOCl-oxidised S100s did not contain epitopes recognised by an antibody used to detect HOCl-oxidised proteins in plaque, levels of oxidised proteins in plaque are likely to be significantly greater than described. S100A8 and S100A9 may protect LDL by functioning as HOCl-scavengers. However, chronic oxidative cross-linking of S100A8 and S100A9 with other proteins and extracellular matrix components may contribute to plaque pathogenesis. These studies support key roles for the " calgranulins" in chronic inflammation, wound healing and atherogenesis possibly by regulating cellular differentiation, activation and modulation of redox-dependent mechanisms.

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Kim, Eunjung. "Biochemical studies of cardiac calsequestrin : its interaction with pharmaceutical drugs and its deleterious mutations." Online access for everyone, 2007. http://www.dissertations.wsu.edu/Dissertations/Spring2007/ej_kim_050107.pdf.

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22

Fallah, Zahra. "Development and plasticity of markers for inhibitory neurotransmission in the spinal cord." Thesis, University of Newcastle Upon Tyne, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244467.

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23

Duquette, Robert Alfred. "The effects of pH on canine, guinea pig and rat gastric smooth muscle function." Thesis, University of Liverpool, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.366492.

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24

Niven, Jennifer A. "The role of S100B in retinal inflammation." Thesis, University of Aberdeen, 2013. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=202787.

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S100B is a member of the S100 calcium binding protein family and is highly expressed within astrocytes in the brain. Elevated levels of S100B are associated with brain and central nervous system disorders, due to the breakdown of the blood brain barrier. Therefore S100B is routinely used as a marker of disease. Traditionally S100B was thought only as a cell breakdown product but increasing evidence suggests that it may play a role in exacerbating inflammation, however this role is not clear. S100B is known to be present within the eye but its role in retinal inflammation has not been investigated. The aim of this project was therefore to examine the role of S100B using the animal model experimental autoimmune uveoretinitis (EAU). This is a well-established model for the sight-threatening human condition posterior endogenous uveoretinitis. In this disease model an autoimmune response is induced leading to retinal inflammation. Using S100B knockout mice, I have shown a significantly reduced level of disease, as determined by clinical and histological grading. Real-time PCR array analysis of diseased matched retinas indicated down regulation of cytokines and chemokines in S100B knockout mice. In vitro experiments on a macrophage cell line confirmed S100B to have a pro-inflammatory effect on macrophages, the main effector cell in EAU, with up-regulation of cytokine and chemokine expression. In particular IL-1β, CCR1 and CCL22 showed a marked increase in gene expression in response to S100B which was confirmed by real-time PCR. Increased protein production of IL-1β (pro-form), CCR1 and CCL22 was also confirmed. S100B inhibited activation of T cells separated from spleens, as shown by reduced CD25+ expression and IL-2 production. IFN-γ and IL-17 production however was not affected. CCL2 and IL-6 are main inflammatory mediators produced by retinal pigment epithelial cells which are known to be elevated during retinal inflammation. S100B promoted CCL2 and IL-6 production in retinal pigment epithelial cells at different concentrations. The work carried out in this thesis provides additional understanding of the actions of extracellular S100B on immune system cells and its potential role in posterior uveitis.

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Alp, Murat. "A kinetic model of calcium binding to calretinin : experimental measurements and predicted effects on calcium signaling at neuronal synapses /." view abstract or download file of text, 2005. http://wwwlib.umi.com/cr/uoregon/fullcit?p3190505.

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Thesis (Ph. D.)--University of Oregon, 2005.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 250 - 269). Also available for download via the World Wide Web; free to University of Oregon users.

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Vasilev, Filip. "New roles for actin-binding proteins and PIP2 in intracellular calcium homeostasis." Thesis, Open University, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.582807.

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Spatiotemporal increase of the intracellular Ca2+ is the most universal way to regulate the function of a eukaryotic cell. Owing to a host of actin-binding proteins and enzymes whose activities are modulated by the local concentration of Ca2+, free Ca2+ in cytosol serves as a pivotal second messenger in a variety of cell functions. The rise and fall of intracellular Ca2+ wave has been best illustrated in eggs at fertilization. However, the molecular mechanism by which intracellular Ca2+ is increased in the fertilized egg is largely unknown despite the discoveries of the distinct Ca2+-mobilizing second messengers in the past 30 years. In this thesis, I have used the starfish oocytes to study how Ca2+ signaling can be modulated by the actin cytoskeleton, which is known to be dynamically remodelled during meiotic maturation and fertilization of the egg. The principal issues of my experimental work are: (i) to establish the role of actin-binding proteins and PIP2 in the regulation of the Ca2+ signaling; (ii) to study the effect of the Ca2+ -store depletion on Ca2+ signaling and on the structure and function of the actin cytoskeleton, and (iii) to study the role of the actin-cytoskeleton in establishing the block to polyspermy. Microinjected into starfish eggs, actin-binding protein gelsolin, function- blocking antibody to depactin, and the PIP2-sequestering fusion protein that indirectly alters the actin cytoskeleton, all changed a certain aspect of Ca2+ signaling. Depletion of the Ca2+ store with ionomycin in turn drastically changed the cortical structure and the actin cytoskeleton of the eggs, eventually leading to a deleterious effect on egg activation and early development. Finally, the alteration of the actin cytoskeleton led to failure to establish a fast and slow block to polyspermy. Taken together, this study indicated that the actin cytoskeleton is an important factor that optimizes the Ca2+ response at egg activation and guides monospermic fertilization.

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27

Campbell, Veronica Ann. "Components of neuronal calcium channels and their interaction with GTP-binding proteins." Thesis, University College London (University of London), 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.363058.

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Tanner, Bertrand Clarke William. "Spatial coupling between sarcomeric proteins controls Ca2+-sensitive contraction muscle : a complementary research approach integrating theory with experiments /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/7995.

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Craske, Madeleine Lisa. "Monitoring the distribution of calmodulin and the calcium-calmodulin binding reaction in isolated pancreatic acinar cells." Thesis, University of Liverpool, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.368870.

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Nguyen, Quynh Dung Sarah. "Calcium oxalate crystal formation in human urine and identification of mineral-binding proteins." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33815.

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Urolithiasis occurs in 20% of males and 5--10% of females, and 75% of kidney stones contain calcium oxalate (CO) mineral. To analyze mineral-binding proteins and to make gender comparisons, using the model of Doyle et al. (Clin Chem, 37: 1589--1594, 1991), CO crystals were generated in whole and centrifuged urine samples and then washed with water or sodium hydroxide. Crystals and mineral-binding proteins were analyzed by SDS-PAGE, Western blotting and electron microscopy (SEM). Regardless of urine or crystal treatment, osteopontin and UPTF1 proteins were consistently present in the samples, whereas THP and albumin were partially removed. SEM showed larger crystals precipitated from female than from male urine. Western blotting demonstrated more albumin bound to crystals from females. In other experiments, CO crystals were grown in the presence of poly-L-aspartic acid (PA) and albumin. SEM demonstrated that these proteins affected CO crystallization. Competitive protein-binding assays and fluorescence activated cell sorter analysis after binding of PA and albumin to hydroxyapatite indicated that PA binds hydroxyapatite with a stronger affinity than albumin.

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Yan, Kai. "Calcium binding proteins and GAD immunoreactivity in the auditory system of Gekko Gecko." College Park, Md.: University of Maryland, 2008. http://hdl.handle.net/1903/8193.

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Thesis (M.S.) -- University of Maryland, College Park, 2008.
Thesis research directed by: Dept. of Biology. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.

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Jones, Lisa Michelle. "Using protein design to understand the role of electrostatic interactions on calcium binding affinity and molecular recognition." unrestricted, 2006. http://etd.gsu.edu/theses/available/etd-07282006-143357/.

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Thesis (Ph.D.)--Georgia State University, 2006.
Title from file title page. Jenny J. Yang, committee chair; Alfons Baumstark, Giovanni Gadda, committee members. Electronic text (405 p. : ill. (some col.)) : digital, PDF file. Description based on contents viewed Aug. 20, 2008. Includes bibliographical references (p. 380-405).

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Casey, Diane M. "DC3, a Calcium-Binding Protein Important for Assembly of the Chlamydomonas Outer Dynein Arm: a Dissertation." eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/156.

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The outer dynein arm-docking complex (ODA-DC) specifies the outer dynein arm-binding site on the flagellar axoneme. The ODA-DC of Chlamydomonas contains equimolar amounts of three proteins termed DC1, DC2, and DC3 (Takada et al., 2002). DC1 and DC2 are predicted to be coiled-coil proteins, and are encoded by ODA3 and ODA1, respectively (Koutoulis et al., 1997; Takada et al., 2002). Prior to this work, nothing was known about DC3. To fully understand the function(s) of the ODA-DC, a detailed analysis of each of its component parts is necessary. To that end, this dissertation describes the characterization of the smallest subunit, DC3. In Chapter II, I report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 D protein with four EF hands that is a member of the CTER (Calmodulin, Troponin C, Essential and Regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming due to loss of some but not all, outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly. As mentioned above, DC3 has four EF-hands: two fit the consensus pattern for calcium binding and one contains two cysteine residues within its binding loop. To determine if the consensus EF-hands are functional, I purified bacterially expressed wild-type DC3 and analyzed its calcium-binding potential in the presence and absence of DTT and Mg2+. As reported in Chapter III, the protein bound one calcium ion with an affinity (Kd) of ~1 x 10-5 M. Calcium binding was observed only in the presence of DTT and thus is redox sensitive. DC3 also bound Mg2+ at physiological concentrations, but with a much lower affinity. Changing the essential glutamate to glutamine in both EF-hands eliminated the calcium-binding activity of the bacterially expressed protein. To investigate the role of the EF hands in vivo, I transformed the modified DC3 gene into a Chlamydomonas insertional mutant lacking DC3. The transformed strain swam normally, assembled a normal number of outer arms, and had a normal photoshock response, indicating that the E to Q mutations did not affect ODA-DC assembly, outer arm assembly, or Ca2+-mediated outer arm activity. Thus, DC3 is a true calcium-binding protein, but the function of this activity remains obscure. In Chapter IV, I report the initial characterization of a DC3 insertional mutant having a phenotype intermediate between that of the DC3-deletion strain and wild type. Furthermore, I suggest future experiments that may help elucidate the specific role of DC3 in outer arm assembly and ODA-DC function. Lastly, I speculate that the ODA-DC may play a role in flagellar regeneration.

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Casey, Diane M. "DC3, a Calcium-Binding Protein Important for Assembly of the Chlamydomonas Outer Dynein Arm: a Dissertation." eScholarship@UMMS, 2003. https://escholarship.umassmed.edu/gsbs_diss/156.

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The outer dynein arm-docking complex (ODA-DC) specifies the outer dynein arm-binding site on the flagellar axoneme. The ODA-DC of Chlamydomonas contains equimolar amounts of three proteins termed DC1, DC2, and DC3 (Takada et al., 2002). DC1 and DC2 are predicted to be coiled-coil proteins, and are encoded by ODA3 and ODA1, respectively (Koutoulis et al., 1997; Takada et al., 2002). Prior to this work, nothing was known about DC3. To fully understand the function(s) of the ODA-DC, a detailed analysis of each of its component parts is necessary. To that end, this dissertation describes the characterization of the smallest subunit, DC3. In Chapter II, I report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 D protein with four EF hands that is a member of the CTER (Calmodulin, Troponin C, Essential and Regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming due to loss of some but not all, outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly. As mentioned above, DC3 has four EF-hands: two fit the consensus pattern for calcium binding and one contains two cysteine residues within its binding loop. To determine if the consensus EF-hands are functional, I purified bacterially expressed wild-type DC3 and analyzed its calcium-binding potential in the presence and absence of DTT and Mg2+. As reported in Chapter III, the protein bound one calcium ion with an affinity (Kd) of ~1 x 10-5 M. Calcium binding was observed only in the presence of DTT and thus is redox sensitive. DC3 also bound Mg2+ at physiological concentrations, but with a much lower affinity. Changing the essential glutamate to glutamine in both EF-hands eliminated the calcium-binding activity of the bacterially expressed protein. To investigate the role of the EF hands in vivo, I transformed the modified DC3 gene into a Chlamydomonas insertional mutant lacking DC3. The transformed strain swam normally, assembled a normal number of outer arms, and had a normal photoshock response, indicating that the E to Q mutations did not affect ODA-DC assembly, outer arm assembly, or Ca2+-mediated outer arm activity. Thus, DC3 is a true calcium-binding protein, but the function of this activity remains obscure. In Chapter IV, I report the initial characterization of a DC3 insertional mutant having a phenotype intermediate between that of the DC3-deletion strain and wild type. Furthermore, I suggest future experiments that may help elucidate the specific role of DC3 in outer arm assembly and ODA-DC function. Lastly, I speculate that the ODA-DC may play a role in flagellar regeneration.

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35

Larner, Stephen Frank. "Up-regulation and activation of caspase-12 and caspase-7 following traumatic brain injury in rats." [Gainesville, Fla.] : University of Florida, 2004. http://purl.fcla.edu/fcla/etd/UFE0006609.

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Thesis (Ph.D.)--University of Florida, 2004.
Typescript. Title from title page of source document. Document formatted into pages; contains 139 pages. Includes Vita. Includes bibliographical references.

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36

Dressen, Cindy. "Caractérisation et rôles potentiels des "Calcium-Binding Proteins" dans l’acquisition du pouvoir fécondant des spermatozoïdes." Doctoral thesis, Universite Libre de Bruxelles, 2020. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/311948.

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La fécondation dépend de la capacité de deux cellules uniques à s’unir :l’ovocyte et le spermatozoïde. Alors que le stock d’ovocytes est établi dès la puberté, les spermatozoïdes sont produits de façon continue à partir d’une réserve de cellules germinales souches (spermatogonies). Immobile et inapte à la fécondation, le spermatozoïde testiculaire doit subir un processus de maturation qui débute dans l’épididyme et se poursuit dans les voies génitales femelles. Bien qu’une première forme de mobilité soit acquise au contact du fluide épididymaire, le spermatozoïde subit, tout au long de son parcours dans le tractus femelle, de nombreuses modifications structurelles et biochimiques appelées « capacitation » et qui s’avèrent indispensables à l’acquisition de son pouvoir fécondant. La production de spermatozoïdes fertiles est un processus hautement régulé, notamment via l’ion calcium ;second messager crucial de nombreux processus de signalisation intracellulaire. Les modifications de la concentration intracellulaire de calcium sont indispensables pour le développement du potentiel de fécondation du sperme via la modification du profil de mobilité vers l’hyperactivation ou encore la réalisation de la réaction acrosomiale. Différents mécanismes de régulation de la concentration intracellulaire calcique ont déjà été mis en évidence dans les spermatozoïdes :canaux calciques, réserves intracellulaires de calcium… Toutefois, peu d’informations relatent la présence et/ou l’implication de protéines liant le calcium (Calcium-Binding Proteins - CaBP) au sein de ce type cellulaire.Notre étude a pour but de caractériser la présence et l’implication potentielle de EF-Hand CaBP dans l’acquisition du pouvoir fécondant des spermatozoïdes murins. Nous nous sommes principalement focalisés sur l’étude de trois membres de cette famille protéique :la calrétinine, la calbindine D-28k et la parvalbumine. Nos investigations ont été menées de manière comparative entre des spermatozoïdes de type Wild-type (WT) et des spermatozoïdes n’exprimant pas une ou plusieurs CaBP (calrétinine knock-out - CR-/-, calbindine D-28k - knock-out CB-/-, triple knock-out pour la calrétinine, la calbindine D-28k et la parvalbumine - CR-/-CB-/-PV-/-). La première partie de notre projet décrit la localisation et l’expression de la calrétinine, la calbindine D-28k et la parvalbumine dans les spermatozoïdes de souris et de rats par immunofluorescence et Western blotting. Ces protéines ont été localisées au niveau de la pièce principale du flagelle et au niveau de la Redundant Nuclear Envelope dans le cas de la parvalbumine. Au cours de la seconde partie du projet, des études de mobilité ainsi que des quantifications du taux de réaction acrosomiale ont été menées en comparant les spermatozoïdes WT aux cellules CR-/- et CR-/-CB-/-PV-/-. Alors qu’aucune différence n’a été constatée entre les taux de réaction acrosomiale WT versus knock-out tant en condition basale qu’induite, l’absence d’une ou plusieurs protéines apparaît influencer certains paramètres de mobilité des spermatozoïdes. En effet, les spermatozoïdes CR-/- et CR-/-CB-/-PV-/- ont présenté une fréquence du battement de flagelle (BCF) plus élevée par rapport à la fréquence mesurée chez les spermatozoïdes WT, paramètre modifié notamment au cours de l’hyperactivation. Cette différence pourrait être liée à une modification du tamponnage calcique ou à une régulation différente du canal calcique CatSper, acteur majeur du développement de l’hyperactivation. Les résultats préliminaires des mesures électrophysiologiques suggèrent un rôle potentiel de la calrétinine dans la régulation de l’activité de ce canal. Par ailleurs, la comparaison entre le nombre de petits par portées WT par rapport aux portées CR-/- ou CR-/-CB-/-PV-/- a indiqué que l’absence d’expression d’une ou plusieurs EF-Hand CaBP réduisait le nombre de naissances par portée au sein des génotypes knock-out.En conclusion, l’ensemble de nos résultats expérimentaux ont démontré la présence de trois EF-Hand CaBP au niveau des spermatozoïdes murins et permis d’apporter de nouvelles informations quant à l’implication potentielle de celles-ci dans l’acquisition du pouvoir fécondant des spermatozoïdes.
Doctorat en Sciences biomédicales et pharmaceutiques (Médecine)
info:eu-repo/semantics/nonPublished

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37

Hasséssian, Harout. "A search for vitamin D dependent calcium binding proteins in the rat nervous system /." Thesis, McGill University, 1987. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66112.

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38

Elliott, Roslyn Marie Ann. "Studies involving calcium binding proteins associated with the outer acrosomal membrane of ram spermatozoa." Thesis, Royal Veterinary College (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322378.

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39

Andy, Divya. "Approach for Identification of Binding Proteins of Calcium Mobilizing Second Messengers: NAADP and cADPR." University of Toledo Health Science Campus / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=mco1525202591650673.

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40

Lo, Alexandra Siu Lok, and n/a. "Paradigms of inflammation : interactions between calcium-binding proteins and the receptor for advanced glycation end products (RAGE)." University of Otago. Department of Physiology, 2005. http://adt.otago.ac.nz./public/adt-NZDU20061016.163427.

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The receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily. The result of RAGE-ligand interactions augments the proinflammatory mechanisms acting in chronic inflammatory diseases. RAGE recognises a wide range of ligands that have no apparent structural similarities. It is unclear what controls this promiscuity of RAGE. The extracellular domain of RAGE has two potential glycosylation sites. It is speculated that N-linked glycosylation may have significant impact on ligand recognition, especially of S100 calcium binding protein ligands. Two objectives of this thesis were to establish whether S100A9 acts as a ligand for RAGE and to investigate whether glycosylation of RAGE has any influence on ligand recognition. These were achieved by generating two forms of RAGE. HEK 293 cells were transfected to express full-length, membrane-bound RAGE or a secreted form comprising the extracellular domain of RAGE. Site-directed mutagenesis of RAGE showed that asparagine at position 25 is the pre-dominant N-linked glycosylation site. The carbohydrate added to asparagine 25 was further modified to a non-sialylated carboxylated N-linked glycan, specifically recognised by monoclonal antibody GB 3.1. Binding studies showed that different RAGE ligands have individual requirements for glycosylation of the receptor. Binding of AGE-modified AGE-BSA or of S100B to RAGE occured independent of N-linked glycosylation of the receptor. RAGE also binds the S100 protein, MRP-14 (S100A9). In contrast to AGE-BSA or S100B, the non-sialylated carboxylated N-glycan expressed on RAGE is crucial for binding to MRP-14. However, RAGE produced in tunicamycin containing medium and thus lacking N-linked glycosylation, shows strong binding to MRP-14. It was concluded that two forms of binding are involved: the first mechanism relies on the non-sialylated carboxylated N-glycan attached to RAGE and acts in a "tethering" fashion. The second mechanism involves a conformational change of RAGE, which results in exposure of a binding site(s) and a more conventional receptor-ligand interaction. Another objective for this thesis is to study the expression of RAGE and its alternatively spliced variants. PCR analysis has revealed several variants of RAGE that result from alternative splicing mechanisms. The variant proteins are soluble due to a lack of membrane localising sequence. PCR results confirmed the presence of transcripts encoding for spliced variants of RAGE in several tumour cell lines. Among these were transcripts that should encode a soluble form of sRAGE 2. Furthermore, it was shown that sRAGE 2 transcript can be present in forms that contain the ligand-binding V-domain of RAGE or that are N-truncated and lack the V-domain. This is the first report of a soluble, N-truncated sRAGE 2 variant. The results in this thesis add to our knowledge of RAGE biology. MRP-14 (S100A9) is identified as a new ligand. The control of MRP-14/RAGE interaction relies on N-linked glycosylation of the receptor and further modification of the carbohydrate. "Tethering" or stronger receptor-ligand interactions are suggested as mechanisms for controlling RAGE recognition of multiple ligands. Soluble RAGE variants that lack or contain V-domain binding regions, and hence sites for glycosylation were produced. These have the capacity to compete with membrane-bound receptor for available ligand. The control of the expression of soluble RAGE variants, in concert with the control of various modification to carbohydrate expressed on the receptor, adds a level of complexity to ligand specificity. This may ultimately result in different paradigms of the inflammatory process.

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Vosnidou, Nancy Carol Hoffman. "Computational analysis of cadherins : sequence analysis of dimerization properties and quantum caculations of calcium coordination characteristics /." free to MU campus, to others for purchase, 2002. http://wwwlib.umi.com/cr/mo/fullcit?p3060154.

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42

Birkholz, Tyler M. "Exploring the Role of Calcium-Binding Protein Calreticulin in the Mouse Suprachiasmatic Nucleus." Bowling Green State University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1562689789471245.

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43

Flinn, Rory J. "Novel use of glycosylation scanning to map the intracellular trafficking of sarco(endo)plasmic reticulum calcium ATPase 1A." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 0.55 Mb., 80 p, 2005. http://wwwlib.umi.com/dissertations/fullcit/1428192.

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Xie, Yi. "Metastasis and angiogenesis in neuroblastoma involvement of visinin like protein-1 and dendritic cell /." Click to view the E-thesis via HKUTO, 2007. http://sunzi.lib.hku.hk/hkuto/record/B38588250.

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Xie, Yi, and 謝弋. "Metastasis and angiogenesis in neuroblastoma: involvement of visinin like protein-1 and dendritic cell." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2007. http://hub.hku.hk/bib/B38588250.

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46

Clark, Ruti H. "A model system for investigating biomineralization : elucidating protein G/calcium oxalate monohydrate interactions /." Thesis, Connect to this title online; UW restricted, 2000. http://hdl.handle.net/1773/8067.

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47

Conrad, Nailah. "Characterization of XVEF and XvCaM : two calcium-binding proteins isolated from the resurrection plant Xerophyta viscosa." Master's thesis, University of Cape Town, 2005. http://hdl.handle.net/11427/4251.

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Includes bibliographical references.
Xerophyta viscosa (Baker) is a resurrection plant with the ability to survive desiccation and rehydrate upon watering with minimal tissue damage. XVEF was isolated by differential screening of aX viscosa dehydration stress cDNA library. Reconstruction of the full length XVEF cDNA was conducted utilizing overlap extension PCR. XVEF codes for a putative calcium-binding protein and sequence analysis indicated that it has a 708 bp ORF corresponding to a protein with a molecular mass of26.95 kDa, has a conserved calcium-binding EF-hand motif, potential phosphorylation sites, a pI of 6.49 and a putative conserved transmembrane domain spanning residues 90-107. Northern blot analyses of total RNA indicated that XVEF transcript increased 48 hours after 100/-lM ABA application and was present between 12 and 48 hours in response to a low temperature stress (4°C). A second gene, XvCaM, was isolated from a low temperature (4°C) cDNA stress library. Sequence analysis indicates that it has a 450 bp ORF corresponding to a 16.39 kDa protein, a pI of 3.90 and potential phosphorylation sites. It apparently encodes a calcium-binding protein with putatively three EF-hands which showed the highest similarity to plant calmodulins. XVCAM was heterologously expressed in E. coli as a fusion protein with a 6X His-tag and it was shown to be a functional protein that binds Ca2+ by utilizing a 45CaCh overlay assay. Northern blot analyses of XvCaM using total RNA under low (4°C) and high temperature treatment (42°C) showed constitutive expression levels of the transcript. Under the dehydration/rehydration treatment transcript levels decreased between 40% R WC dehydration and 26% RWC rehydration. The northern blot conducted with polysomal RNA isolated from 150 mM NaCI treatment also showed constitutive expression. Western blot analyses using anti-XVCAM polyclonal antibodies showed that the protein accumulated at 24 hours during the NaCI stress and at 15% RWC (dry) to 40% RWC (rehydration) during the dehydration/rehydration stress. The northern and western analyses results suggest that XVCAM undergoes post-translational modifications and XvCaM mRNA is possibly stored for rapid recovery processes upon rehydration. These results indicate that XVEF and XvCaM are possibly calcium-binding proteins most likely involved in modulating stress-responsive calcium-signaling cascades.

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Wittenschlaeger, Thomas M. II. "Searching for the Rosetta Stones in the Multifunctional Proteins of the Phytophthora Sojae Genome." Bowling Green State University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1181012189.

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Ho, Peter D. "Regulation of morphology and intracellular calcium by Ras in rat neonatal cardiac myocytes /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2000. http://wwwlib.umi.com/cr/ucsd/fullcit?p9984293.

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Krylov, Dmitri M. "Guanylyl cyclase activating protein-1 and its regulation of retinal guanylyl cyclases : a study by molecular biological methods and a novel mass spectrometry based method /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/9259.

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