Log in

Relevant bibliographies by topics / Filensin / Journal articles

Journal articles on the topic 'Filensin'

To see the other types of publications on this topic, follow the link: Filensin.

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 28 journal articles for your research on the topic 'Filensin.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Brunkener, M., and S. D. Georgatos. "Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells." Journal of Cell Science 103, no. 3 (November 1, 1992): 709–18. http://dx.doi.org/10.1242/jcs.103.3.709.

Full text

Abstract:

Filensin is a 100/110 kDa membrane-associated protein found in lens fiber cells. Previous studies have shown that this protein polymerizes in vitro and binds strongly to vimentin and to another 47 kDa lens membrane protein. Using cosedimentation assays, flotation assays and immunoelectron microscopy, we have examined the properties of purified filensin and measured its binding to lens membranes. Filensin behaves as a ureaextractable, hydrophilic protein which does not partition with Triton X-114 and is not affected by 1 M hydroxylamine at alkaline pH, an agent known to release fatty-acylated proteins from the membrane. Immunoblotting of urea-extracted lens membranes with two different affinity-purified antibodies reveals that, unlike intact filensin, a COOH-terminal filensin degradation product (51 kDa) remains tightly associated with the membranes. Purified filensin binds directly to urea-stripped lens membranes, but not to protein-free vesicles reconstituted from total lens lipids. The binding of filensin is not significantly influenced by the purified 47 kDa protein. Interestingly, the filensin-binding capacity of urea-extracted membranes is increased at least two-fold after trypsin treatment, which removes entirely the 51 kDa peptide from the membranes and presumably unmasks additional filensin-acceptor sites. Consistent with this, filensin binds to trypsinized and non-trypsinized membranes with similar affinities (2 × 10(−7) and 4 × 10(−7) M, respectively). Treatment of the membranes with thrombin, which also eliminates the 51 kDa peptide, does not increase their binding capacity, apparently because filensin-acceptor sites are also destroyed during proteolysis.(ABSTRACT TRUNCATED AT 250 WORDS)

APA, Harvard, Vancouver, ISO, and other styles

2

Remington, S. G. "Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins." Journal of Cell Science 105, no. 4 (August 1, 1993): 1057–68. http://dx.doi.org/10.1242/jcs.105.4.1057.

Full text

Abstract:

Filensin, a 100 kDa, membrane-associated, cytoskeletal protein, is uniquely expressed in the lens fiber cell (Merdes, A., Brunkener, M., Horstmann, H., and Georgatos, S. D. (1991) J. Cell Biol. 115, 397–410). I cloned and sequenced a full-length chicken lens cDNA encoding filensin, also known as CP95 (Ireland, M. and Maisel, H. (1989) Lens and Eye Toxicity Research 6, 623–638). The deduced amino acid sequence of 657 residues contained an internal 280 residue heptad repeat domain with sequence similarities to the rod domain of intermediate filament proteins. The putative filensin rod domain could be divided into three alpha-helical segments (1A, 1B and 2) separated by short, non-helical linkers. The sequence of the amino-terminal end of the filensin rod domain contained the highly conserved intermediate filament segment 1A motif (Conway, J. F. and Parry, D. A. D. (1988) Int. J. Biol. Macromol. 10, 79–98). Allowing conservative amino acid substitutions, the sequence of the carboxy-terminal end of the filensin rod domain was similar to that of the highly conserved intermediate filament rod carboxy terminus. The alpha-helical segments of the shorter filensin rod domain aligned with the corresponding segments of intermediate filament proteins by allowing a gap of four heptad repeats in the amino-terminal half of filensin segment 2. Filensin rod segment 2 contained the characteristic stutter in heptad repeat phasing, nine heptads from the end of the intermediate filament rod. The overall sequence identity between the rod domains of filensin and individual intermediate filament proteins was 20 to 25%, approximately the level of sequence identity observed between intermediate filament proteins of different types. The open reading frame of chicken filensin predicted a 657 amino acid protein with molecular mass of 76 kDa. Embryonic chicken filensin migrated in SDS-PAGE as a triplet of 102, 105 and 109 kDa, while rooster filensin migrated as a 105 and 109 kDa doublet. Antibodies to filensin labeled lens fiber cells but not lens epithelial cells. By immunofluorescence methods filensin was localized to the fiber cell plasma membranes, including the ends of elongated fiber cells.

APA, Harvard, Vancouver, ISO, and other styles

3

Goulielmos, G., S. Remington, F. Schwesinger, S. D. Georgatos, and F. Gounari. "Contributions of the structural domains of filensin in polymer formation and filament distribution." Journal of Cell Science 109, no. 2 (February 1, 1996): 447–56. http://dx.doi.org/10.1242/jcs.109.2.447.

Full text

Abstract:

Filensin and phakinin constitute the subunits of a heteropolymeric, lens-specific intermediate filament (IF) system known as the beaded-chain filaments (BFs). Since the rod of filensin is four heptads shorter than the rods of all other IF proteins, we decided to examine the specific contribution of this protein in filament assembly. For these purposes, we constructed chimeric proteins in which regions of filensin were exchanged with the equivalent ones of vimentin, a self-polymerizing IF protein. Our in vitro studies show that the filensin rod domain does not allow homopolymeric filament elongation. However, the filensin rod is necessary for co-polymerization of filensin with phakinin and seems to counteract the inherent tendency of the latter protein to homopolymerize into large, laterally associated filament bundles. Apart from the rod domain, the presence of an authentic or substituted tail domain in filensin is also essential for co-assembly with the naturally tail-less phakinin and formation of extended filaments in vitro. Finally, transfection experiments in CHO and MCF-7 cells show that the rod domain of filensin plays an important role in de novo filament formation and distribution. The same type of analysis further suggests that the end-domains of filensin interact with cell-specific, assembly-modulating factors.

APA, Harvard, Vancouver, ISO, and other styles

4

Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. "Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell." Journal of Cell Biology 115, no. 2 (October 15, 1991): 397–410. http://dx.doi.org/10.1083/jcb.115.2.397.

Full text

Abstract:

We have studied the molecular properties of a 100-kD protein, termed filensin, which we have isolated from porcine lens membranes. Filensin represents a membrane-associated element, resistant to salt and nonionic detergent treatment, and extractable only by alkali or high concentrations of urea. By indirect immunofluorescence and immunoelectron microscopy, this protein can be localized at the periphery of the lens fiber cells. Immunochemical analysis suggests that filensin originates from a larger 110-kD component which is abundantly expressed in lens but not in other tissues. Purified filensin polymerizes in a salt-dependent fashion and forms irregular fibrils (integral of 10 nm in diameter) when reconstituted into buffers of physiological ionic strength and neutral pH. Radiolabeled filensin binds specifically to lens vimentin under isotonic conditions, as demonstrated by affinity chromatography and ligand-blotting assays. By the latter approach, filensin also reacts with a 47-kD peripheral membrane protein of the lens cells. Purified filensin binds to PI, a synthetic peptide modelled after a segment of the COOH-terminal domain of peripherin (a type III intermediate filament protein highly homologous to vimentin), but not to various other peptides including the NH2-terminal headpiece of vimentin and derivatives of its middle (rod) domain. The filensin-PI binding is inhibited by purified lamin B, which is known to interact in vitro with PI (Djabali, K., M.-M. Portier, F. Gros, G. Blobel, and S. D. Georgatos. 1991. Cell. 64:109-121). Finally, limited proteolysis indicates that the filensin-vimentin interaction involves a 30-kD segment of the filensin molecule. Based on these observations, we postulate that the lens fiber cells express a polymerization-competent protein which is tightly associated with the plasma membrane and has the potential to serve as an anchorage site for vimentin intermediate filaments.

APA, Harvard, Vancouver, ISO, and other styles

5

Gounari, F., A. Merdes, R. Quinlan, J. Hess, P. G. FitzGerald, C. A. Ouzounis, and S. D. Georgatos. "Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins." Journal of Cell Biology 121, no. 4 (May 15, 1993): 847–53. http://dx.doi.org/10.1083/jcb.121.4.847.

Full text

Abstract:

The cDNA coding for calf filensin, a membrane-associated protein of the lens fiber cells, has been cloned and sequenced. The predicted 755-amino acid-long open reading frame shows primary and secondary structure similarity to intermediate filament (IF) proteins. Filensin can be divided into an NH2-terminal domain (head) of 38 amino acids, a middle domain (rod) of 279 amino acids, and a COOH-terminal domain (tail) of 438 amino acids. The head domain contains a di-arginine/aromatic amino acid motif which is also found in the head domains of various intermediate filament proteins and includes a potential protein kinase A phosphorylation site. By multiple alignment to all known IF protein sequences, the filensin rod, which is the shortest among IF proteins, can be subdivided into three subdomains (coils 1a, 1b, and 2). A 29 amino acid truncation in the coil 2 region accounts for the smaller size of this domain. The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neurofilament M and H proteins. We suggest that filensin is a novel IF protein which does not conform to any of the previously described classes. Purified filensin fails to form regular filaments in vitro (Merdes, A., M. Brunkener, H. Horstmann, and S. D. Georgatos. 1991. J. Cell Biol. 115:397-410), probably due to the missing segment in the coil 2 region. Participation of filensin in a filamentous network in vivo may be facilitated by an assembly partner.

APA, Harvard, Vancouver, ISO, and other styles

6

Merdes, A., F. Gounari, and S. D. Georgatos. "The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin." Journal of Cell Biology 123, no. 6 (December 15, 1993): 1507–16. http://dx.doi.org/10.1083/jcb.123.6.1507.

Full text

Abstract:

In previous studies we have characterized a lens-specific intermediate filament (IF) protein, termed filensin. Filensin does not self-assemble into regular IFs but is known to associate with another 47-kD lens-specific protein which has been suggested to represent its assembly partner. To address this possibility, we cloned and sequenced the cDNA coding for the bovine 47-kD protein which we have termed phakinin (from the greek phi alpha kappa omicron sigma = phakos = lens). The predicted sequence comprises 406 amino acids and shows significant similarity (31.3% identity over 358 residues) to type I cytokeratins. Phakinin possesses a 95-residue, non-helical domain (head) and a 311 amino acid long alpha-helical domain punctuated with heptad repeats (rod). Similar to cytokeratin 19, phakinin lacks a COOH-terminal tail domain and it therefore represents the second known example of a naturally tailless IF protein. Confocal microscopy on frozen lens sections reveals that phakinin colocalizes with filensin and is distributed along the periphery of the lens fiber cells. Quantitative immunoblotting with whole lens fiber cell preparations and fractions of washed lens membranes suggest that the natural stoichiometry of phakinin to filensin is approximately 3:1. Under in vitro conditions, phakinin self-assembles into metastable filamentous structures which tend to aggregate into thick bundles. However, mixing of phakinin and filensin at an optimal ratio of 3:1 yields stable 10-nm filaments which have a smooth surface and are ultrastructurally indistinguishable from "mainstream" IFs. Immunolabeling with specific antibodies shows that these filaments represent phakinin/filensin heteropolymers. Despite its homology to the cytokeratins, phakinin does not coassemble with acidic (type I), or basic (type II) cytokeratins. From these data we conclude that filensin and phakinin are obligate heteropolymers which constitute a new membrane-associated, lens-specific filament system related to, but distinct from the known classes of IFs.

APA, Harvard, Vancouver, ISO, and other styles

7

Goulielmos, G., F. Gounari, S. Remington, S. Müller, M. Häner, U. Aebi, and S. D. Georgatos. "Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells." Journal of Cell Biology 132, no. 4 (February 15, 1996): 643–55. http://dx.doi.org/10.1083/jcb.132.4.643.

Full text

Abstract:

The fiber cells of the eye lens possess a unique cytoskeletal system known as the "beaded-chain filaments" (BFs). BFs consist of filensin and phakinin, two recently characterized intermediate filament (IF) proteins. To examine the organization and the assembly of these heteropolymeric IFs, we have performed a series of in vitro polymerization studies and transfection experiments. Filaments assembled from purified filensin and phakinin exhibit the characteristic 19-21-nm periodicity seen in many types of IFs upon low angle rotary shadowing. However, quantitative mass-per-length (MPL) measurements indicate that filensin/phakinin filaments comprise two distinct and dissociable components: a core filament and a peripheral filament moiety. Consistent with a nonuniform organization, visualization of unfixed and unstained specimens by scanning transmission electron microscopy (STEM) reveals the the existence of a central filament which is decorated by regularly spaced 12-15-nm-diam beads. Our data suggest that the filamentous core is composed of phakinin, which exhibits a tendency to self-assemble into filament bundles, whereas the beads contain filensin/phakinin hetero-oligomers. Filensin and phakinin copolymerize and form filamentous structures when expressed transiently in cultured cells. Experiments in IF-free SW13 cells reveal that coassembly of the lens-specific proteins in vivo does not require a preexisting IF system. In epithelial MCF-7 cells de novo forming filaments appear to grow from distinct foci and organize as thick, fibrous laminae which line the plasma membrane and the nuclear envelope. However, filament assembly in CHO and SV40-transformed lens-epithelial cells (both of which are fibroblast-like) yields radial networks which codistribute with the endogenous vimentin IFs. These observations document that the filaments formed by lens-specific IF proteins are structurally distinct from ordinary cytoplasmic IFs. Furthermore, the results suggest that the spatial arrangement of filensin/phakinin filaments in vivo is subject to regulation by host-specific factors. These factors may involve cytoskeletal networks (e.g., vimentin IFs) and/or specific sites associated with the cellular membranes.

APA, Harvard, Vancouver, ISO, and other styles

8

Sandilands, A., A. R. Prescott, J. M. Carter, A. M. Hutcheson, R. A. Quinlan, J. Richards, and P. G. FitzGerald. "Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation." Journal of Cell Science 108, no. 4 (April 1, 1995): 1397–406. http://dx.doi.org/10.1242/jcs.108.4.1397.

Full text

Abstract:

The cells of the eye lens contain the type III intermediate filament protein vimentin, as well as two other intermediate filament proteins, CP49 and filensin. These two proteins appear to be unique to the differentiated lens fibre cell. Immunoblotting and confocal microscopy were used to describe changes which occur in these three intermediate filament proteins and the networks they form during fibre cell differentiation and maturation. The vimentin network was present in both epithelial cells and some fibre cells. Fibre cells were vimentin positive up to a specific point 2–3 mm in from the lens capsule where the vimentin signal was drastically reduced. The CP49/filensin network was not present in the undifferentiated epithelial cells but emerged in the differentiating fibre cells. This latter network exhibited a principally plasma membrane localization in younger fibre cells but became more cytoplasmic in older fibre cells. This change also occurred at a distinct point in fibre cell differentiation, much earlier than the observed loss of the vimentin network. The subcellular changes in the distributions of these cytoskeletal networks were correlated to the loss of the fibre cell nucleus, another feature of fibre cell differentiation. No correlation was found to changes in the vimentin network but nuclear loss did coincide with changes in the CP49/filensin network. Concomitant with nuclear pyknosis, there were also changes in the nuclear lamina as well as infringement of the nuclear compartment by CP49, as shown by confocal microscopy. This study demonstrates vimentin and the CP49/filensin network to be independent in the lens but both networks undergo dramatic changes in subcellular distribution during the differentiation/maturation of the fibre cell. Only changes in the CP49/filensin network can be correlated to nuclear loss. Thus in the lens, unlike mammalian erythropoiesis which is also characterized by nuclear loss, the vimentin network does not appear linked to nuclear retention.

APA, Harvard, Vancouver, ISO, and other styles

9

Fischer, R. S., R. A. Quinlan, and V. M. Fowler. "Tropomodulin binds to filensin intermediate filaments." FEBS Letters 547, no. 1-3 (June 26, 2003): 228–32. http://dx.doi.org/10.1016/s0014-5793(03)00711-7.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Georgatos, S. D., F. Gounari, G. Goulielmos, and U. Aebi. "To bead or not to bead? Lens-specific intermediate filaments revisited." Journal of Cell Science 110, no. 21 (November 1, 1997): 2629–34. http://dx.doi.org/10.1242/jcs.110.21.2629.

Full text

Abstract:

For nearly three decades cytoplasmic intermediate filaments (IFs) have been described as 10 nm thick, unbranched ropes radiating from the cell nucleus and extending to the plasma membrane. This stereotype is now being challenged by the discovery and molecular characterization of the beaded filaments (BFs), a novel class of IFs composed of the lens-specific proteins filensin and phakinin. In contrast to ‘mainstream’ IFs, BFs have a distinctly nodular appearance and form a meshwork underneath the plasma membrane of the lens fiber cells. In vitro assembly studies, expression of filensin and phakinin in cultured cells, and analysis of the corresponding genes reveal that these proteins have evolved from two different subfamilies of IF proteins, thus yielding a unique structure. The new information provides a basis for understanding how the various forms of tissue-specific IF proteins might have developed adopting to the constraints of a specialized environment.

APA, Harvard, Vancouver, ISO, and other styles

11

Masaki, Shigeo, Yusuke Kamachi, Roy A. Quinlan, Satoshi Yonezawa, and Hisato Kondoh. "Identification and functional analysis of the mouse lens filensin gene promoter." Gene 214, no. 1-2 (July 1998): 77–86. http://dx.doi.org/10.1016/s0378-1119(98)00230-3.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Carter, J. "Classification of CP49 and filensin: two lens specific intermediate filament proteins." Vision Research 35, no. 1 (October 1995): S196. http://dx.doi.org/10.1016/0042-6989(95)98757-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Wang, Zhen, Joy E. Obidike, and Kevin L. Schey. "Posttranslational Modifications of the Bovine Lens Beaded Filament Proteins Filensin and CP49." Investigative Opthalmology & Visual Science 51, no. 3 (March 1, 2010): 1565. http://dx.doi.org/10.1167/iovs.09-4565.

Full text

APA, Harvard, Vancouver, ISO, and other styles

14

Alizadeh, Azita, John Clark, Teri Seeberger, John Hess, Tom Blankenship, and Paul G. FitzGerald. "Targeted Deletion of the Lens Fiber Cell–Specific Intermediate Filament Protein Filensin." Investigative Opthalmology & Visual Science 44, no. 12 (December 1, 2003): 5252. http://dx.doi.org/10.1167/iovs.03-0224.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Gounari, Fotini, Niki Karagianni, Antoaneta Mincheva, Peter Lichter, Spyros D. Georgatos, and Volker Schirrmacher. "The mouse filensin gene: structure and evolutionary relation to other intermediate filament genes." FEBS Letters 413, no. 2 (August 18, 1997): 371–78. http://dx.doi.org/10.1016/s0014-5793(97)00937-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Carter, J. M., S. V. Duff, W. H. I. McLean, A. R. Prescott, P. S. Wallace, and R. A. Quinlan. "P 218 Classification of CP49 and filensin: Two lens specific intermediate filament proteins." Vision Research 35 (October 1995): S196. http://dx.doi.org/10.1016/0042-6989(95)90534-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Chaves, Jose M., Ratna Gupta, Kiran Srivastava, and Om Srivastava. "Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin." Biochemical and Biophysical Research Communications 494, no. 1-2 (December 2017): 402–8. http://dx.doi.org/10.1016/j.bbrc.2017.09.088.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Rose, Kristie M. Lindsey, Robert G. Gourdie, Alan R. Prescott, Roy A. Quinlan, Rosalie K. Crouch, and Kevin L. Schey. "The C Terminus of Lens Aquaporin 0 Interacts with the Cytoskeletal Proteins Filensin and CP49." Investigative Opthalmology & Visual Science 47, no. 4 (April 1, 2006): 1562. http://dx.doi.org/10.1167/iovs.05-1313.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Wang, Zhen, and Kevin L. Schey. "Identification of a direct Aquaporin-0 binding site in the lens-specific cytoskeletal protein filensin." Experimental Eye Research 159 (June 2017): 23–29. http://dx.doi.org/10.1016/j.exer.2017.02.012.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Masaki, Shigeo, Satoshi Yonezawa, and Roy A. Quinlan. "Localization of Two Conserved Cis -acting Enhancer Regions for the Filensin Gene Promoter That Direct Lens-specific Expression." Experimental Eye Research 75, no. 3 (September 2002): 295–305. http://dx.doi.org/10.1006/exer.2002.2016.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Masaki, S., and R. A. Quinlan. "Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: implications for protein classification and assembly." Gene 201, no. 1-2 (November 1997): 11–20. http://dx.doi.org/10.1016/s0378-1119(97)00419-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Liu, Ke, Lei Lyu, David Chin, Junyuan Gao, Xiurong Sun, Fu Shang, Andrea Caceres, et al. "Altered ubiquitin causes perturbed calcium homeostasis, hyperactivation of calpain, dysregulated differentiation, and cataract." Proceedings of the National Academy of Sciences 112, no. 4 (January 12, 2015): 1071–76. http://dx.doi.org/10.1073/pnas.1404059112.

Full text

Abstract:

Although the ocular lens shares many features with other tissues, it is unique in that it retains its cells throughout life, making it ideal for studies of differentiation/development. Precipitation of proteins results in lens opacification, or cataract, the major blinding disease. Lysines on ubiquitin (Ub) determine fates of Ub-protein substrates. Information regarding ubiquitin proteasome systems (UPSs), specifically of K6 in ubiquitin, is undeveloped. We expressed in the lens a mutant Ub containing a K6W substitution (K6W-Ub). Protein profiles of lenses that express wild-type ubiquitin (WT-Ub) or K6W-Ub differ by only ∼2%. Despite these quantitatively minor differences, in K6W-Ub lenses and multiple model systems we observed a fourfold Ca2+ elevation and hyperactivation of calpain in the core of the lens, as well as calpain-associated fragmentation of critical lens proteins including Filensin, Fodrin, Vimentin, β-Crystallin, Caprin family member 2, and tudor domain containing 7. Truncations can be cataractogenic. Additionally, we observed accumulation of gap junction Connexin43, and diminished Connexin46 levels in vivo and in vitro. These findings suggest that mutation of Ub K6 alters UPS function, perturbs gap junction function, resulting in Ca2+ elevation, hyperactivation of calpain, and associated cleavage of substrates, culminating in developmental defects and a cataractous lens. The data show previously unidentified connections between UPS and calpain-based degradative systems and advance our understanding of roles for Ub K6 in eye development. They also inform about new approaches to delay cataract and other protein precipitation diseases.

APA, Harvard, Vancouver, ISO, and other styles

23

HESS, JOHN F., JODI T. CASSELMAN, ALLEN P. KONG, and PAUL G. FITZGERALD. "Primary Sequence, Secondary Structure, Gene Structure, and Assembly Properties Suggests that the Lens-specific Cytoskeletal Protein Filensin Represents a Novel Class of Intermediate Filament Protein." Experimental Eye Research 66, no. 5 (May 1998): 625–44. http://dx.doi.org/10.1006/exer.1998.0478.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

de Iongh, Robbert U., Frank J. Lovicu, Paul A. Overbeek, Michael D. Schneider, Josephine Joya, Edna D. Hardeman, and John W. McAvoy. "Requirement for TGFβ receptor signaling during terminal lens fiber differentiation." Development 128, no. 20 (October 15, 2001): 3995–4010. http://dx.doi.org/10.1242/dev.128.20.3995.

Full text

Abstract:

Several families of growth factors have been identified as regulators of cell fate in the developing lens. Members of the fibroblast growth factor family are potent inducers of lens fiber differentiation. Members of the transforming growth factor β (TGFβ) family, particularly bone morphogenetic proteins, have also been implicated in various stages of lens and ocular development, including lens induction and lens placode formation. However, at later stages of lens development, TGFβ family members have been shown to induce pathological changes in lens epithelial cells similar to those seen in forms of human subcapsular cataract. Previous studies have shown that type I and type II TGFβ receptors, in addition to being expressed in the epithelium, are also expressed in patterns consistent with a role in lens fiber differentiation. In this study we have investigated the consequences of disrupting TGFβ signaling during lens fiber differentiation by using the mouse αΑ-crystallin promoter to overexpress mutant (kinase deficient), dominant-negative forms of either type I or type II TGFβ receptors in the lens fibers of transgenic mice. Mice expressing these transgenes had pronounced bilateral nuclear cataracts. The phenotype was characterized by attenuated lens fiber elongation in the cortex and disruption of fiber differentiation, culminating in fiber cell apoptosis and degeneration in the lens nucleus. Inhibition of TGFβ signaling resulted in altered expression patterns of the fiber-specific proteins, α-crystallin, filensin, phakinin and MIP. In addition, in an in vitro assay of cell migration, explanted lens cells from transgenic mice showed impaired migration on laminin and a lack of actin filament assembly, compared with cells from wild-type mice. These results indicate that TGFβ signaling is a key event during fiber differentiation and is required for completion of terminal differentiation.

APA, Harvard, Vancouver, ISO, and other styles

25

Nakamuta, Ryoichi, Hiroyuki Ainobu, Masaya Wada, Taketsune Matsuzaki, Yushi Oishi, Mikako Oka, Makoto Takehana, Yozo Takasaki, and Shoji Ando. "2P-050 Morphological analysis of the intermediate filaments formed by lens-specific proteins filensin and phakinin in vitro(The 46th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 48, supplement (2008): S82—S83. http://dx.doi.org/10.2142/biophys.48.s82_6.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Li, Yong, Dandan Qi, Baoli Zhu, and Xin Ye. "Analysis of m6A RNA Methylation-Related Genes in Liver Hepatocellular Carcinoma and Their Correlation with Survival." International Journal of Molecular Sciences 22, no. 3 (February 2, 2021): 1474. http://dx.doi.org/10.3390/ijms22031474.

Full text

Abstract:

N6-methyladenosine (m6A) modification on RNA plays an important role in tumorigenesis and metastasis, which could change gene expression and even function at multiple levels such as RNA splicing, stability, translocation, and translation. In this study, we aim to conduct a comprehensive analysis on m6A RNA methylation-related genes, including m6A RNA methylation regulators and m6A RNA methylation-modified genes, in liver hepatocellular carcinoma, and their relationship with survival and clinical features. Data, which consist of the expression of widely reported m6A RNA methylation-related genes in liver hepatocellular carcinoma from The Cancer Genome Atlas (TCGA), were analyzed by one-way ANOVA, Univariate Cox regression, a protein–protein interaction network, gene enrichment analysis, feature screening, a risk prognostic model, correlation analysis, and consensus clustering analysis. In total, 405 of the m6A RNA methylation-related genes were found based on one-way ANOVA. Among them, DNA topoisomerase 2-alpha (TOP2A), exodeoxyribonuclease 1 (EXO1), ser-ine/threonine-protein kinase Nek2 (NEK2), baculoviral IAP repeat-containing protein 5 (BIRC5), hyaluronan mediated motility receptor (HMMR), structural maintenance of chromosomes protein 4 (SMC4), bloom syndrome protein (BLM), ca-sein kinase I isoform epsilon (CSNK1E), cytoskeleton-associated protein 5 (CKAP5), and inner centromere protein (INCENP), which were m6A RNA methylation-modified genes, were recognized as the hub genes based on the protein–protein interaction analysis. The risk prognostic model showed that gender, AJCC stage, grade, T, and N were significantly different between the subgroup with the high and low risk groups. The AUC, the evaluation parameter of the prediction model which was built by RandomForest, was 0.7. Furthermore, two subgroups were divided by consensus clustering analysis, in which stage, grade, and T differed. We identified the important genes expressed significantly among two clusters, including uridine-cytidine kinase 2 (UCK2), filensin (BFSP1), tubulin-specific chaperone D (TBCD), histone-lysine N-methyltransferase PRDM16 (PRDM16), phosphorylase b ki-nase regulatory subunit alpha (PHKA2), serine/threonine-protein kinase BRSK2 (BRSK2), Arf-GAP with coiled-coil (ACAP3), general transcription factor 3C polypep-tide 2 (GTF3C2), and guanine nucleotide exchange factor MSS4 (RABIF). In our study, the m6A RNA methylation-related genes in liver hepatocellular carcinoma were analyzed systematically, including the expression, interaction, function, and prognostic values, which provided an important theoretical basis for m6A RNA methylation in liver cancer. The nine important m6A-related genes could be prognostic markers in the survival time of patients.

APA, Harvard, Vancouver, ISO, and other styles

27

Agbamu, Samuel. "The Arco dei Fileni: A fascist reading of Sallust’s Bellum Iugurthinum." Classical Receptions Journal 11, no. 2 (January 28, 2019): 157–77. http://dx.doi.org/10.1093/crj/cly023.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

PARFITT, ROSE. "Fascism, Imperialism and International Law: An Arch Met a Motorway and the Rest is History . . ." Leiden Journal of International Law 31, no. 3 (July 2, 2018): 509–38. http://dx.doi.org/10.1017/s0922156518000304.

Full text

Abstract:

AbstractWhat would happen to our understanding of international law and its relationship with violence if we collapsed the distinction between our supposedly post-colonial ‘present’ and its colonial ‘past’; between the sovereign spaces of the twenty-first century global order, and the integrated, hierarchical space of fascist imperialism? I respond to this question through an investigation into the physical contours of a precise ‘imperial location’: 30°31′00″N, 18°34′00″E. These co-ordinates refer to a point on the sea-edge of the Sirtica that is occupied today by the Ra's Lanuf oil refinery, one of Libya's three most important such facilities. In the late 1930s, however, during Libya's period of fascist colonial rule, this was the point at which a state-of-the-art motorway, the Via litoranea libica, was crossed by a giant triumphal arch, the Arco dei Fileni. Through a chronotopic reading of the temporal, spatial and interpellative aspects of this point, its architecture and its history, I suggest that fascist lawyers, officials and intellectuals accepted a horrifying truth about the relationship between international law and violence – a relationship that twenty-first century doctrinal international law is loath to confront, concerning the inherently expansionist logic of the sovereign state, and the inevitably hierarchical ordering of the ‘international community’ which stems from it.

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!