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Journal articles on the topic 'Filensin'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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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.

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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 p

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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.

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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 cou

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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.

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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 elong

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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.

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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 filensi

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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.

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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 p

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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.

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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 t

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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.

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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) measuremen

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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.

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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 le

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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.

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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.

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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 phaki

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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.

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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-

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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.

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24

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

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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 fo

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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.

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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.

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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 gene

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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.

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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.

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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,

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