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Gene Review

BFSP2  -  beaded filament structural protein 2,...

Bos taurus

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High impact information on BFSP2

  • By the use of 14C-labeled amines and SDS-denaturing PAGE, covalent adducts derived from primary amines and the PSII subunits, CP47, D2/D1, and the Mn-stabilizing protein, can be observed [1].
  • Filensin and phakinin constitute the subunits of a heteropolymeric, lens-specific intermediate filament (IF) system known as the beaded-chain filaments (BFs) [2].
  • The CP49/filensin network was not present in the undifferentiated epithelial cells but emerged in the differentiating fibre cells [3].
  • 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 [3].
  • Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation [3].

Biological context of BFSP2


Anatomical context of BFSP2

  • The cortical non-sedimenting membrane fraction and the nuclear membrane fraction of the 25%/45% sucrose density interface were notably deficient in CP49 [5].

Associations of BFSP2 with chemical compounds

  • RESULTS: LEC incubated with 7-keto presented higher levels of p57KIP2 and showed expression of fiber specific proteins such as MIP26 and CP49, compared to cells incubated with 25-OH or cholesterol [6].
  • CP49 immunoreactive peptides were found almost exclusively in the urea-soluble protein of all membrane fractions from both the cortex and nucleus [5].

Other interactions of BFSP2

  • We identified age-related changes in water-insoluble alpha-crystallin, the major membrane protein MP26 and the cytoskeletal proteins vimentin, phakinin and actin between control and UV-irradiated lenses [7].

Analytical, diagnostic and therapeutic context of BFSP2

  • A rapid one-step purification procedure for CP49, an intermediate filament protein found in the lens, is described using reverse-phase HPLC [4].
  • The expression of the differentiation marker p57KIP2, proliferation marker PCNA (Proliferating Cell Nuclear Antigen) and fibers specific proteins gamma-crystallin, CP49, MIP26 following treatment with oxysterols was determined by western blot [6].
  • In order to better understand the physiological role of CP49 in lens transparency we have purified CP49 from both compartments and compared the in vitro assembly characteristics of both by electron microscopy and sedimentation assays [4].


  1. Amine binding and oxidation at the catalytic site for photosynthetic water oxidation. Ouellette, A.J., Anderson, L.B., Barry, B.A. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Contributions of the structural domains of filensin in polymer formation and filament distribution. Goulielmos, G., Remington, S., Schwesinger, F., Georgatos, S.D., Gounari, F. J. Cell. Sci. (1996) [Pubmed]
  3. Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. Sandilands, A., Prescott, A.R., Carter, J.M., Hutcheson, A.M., Quinlan, R.A., Richards, J., FitzGerald, P.G. J. Cell. Sci. (1995) [Pubmed]
  4. In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with alpha-crystallin but not with vimentin. Carter, J.M., Hutcheson, A.M., Quinlan, R.A. Exp. Eye Res. (1995) [Pubmed]
  5. Intermediate filament cytoskeletal proteins associated with bovine lens native membrane fractions. Fleschner, C.R. Curr. Eye Res. (1998) [Pubmed]
  6. 7-ketocholesterol stimulates differentiation of lens epithelial cells. Girão, H., Shang, F., Pereira, P. Mol. Vis. (2003) [Pubmed]
  7. UV-A-related alterations of young and adult lens water-insoluble alpha-crystallin, plasma membranous and cytoskeletal proteins. Weinreb, O., Dovrat, A., Dunia, I., Benedetti, E.L., Bloemendal, H. Eur. J. Biochem. (2001) [Pubmed]
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