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BFSP1  -  beaded filament structural protein 1,...

Bos taurus

 
 
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High impact information on BFSP1

  • Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins [1].
  • The filensin tail contains 6 1/2 tandem repeats which match analogous motifs of mammalian neurofilament M and H proteins [1].
  • 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 [1].
  • Lateral to the germinative zone were the cells of the transition zone (meridinal rows) where expression of the lens specific proteins beta-crystallin, gamma-crystallin, filensin and aquaporin 0 as well as the lens fiber-, adipocyte- and brain glia-specific Na, K-ATPase catalytic subunit, alpha2 are expressed [2].
  • Monoclonal and polyclonal antibodies to peptides and specific subdomains of filensin were used to follow changes in the subcellular distribution of filensin during bovine lens fiber cell differentiation [3].
 

Biological context of BFSP1

 

Associations of BFSP1 with chemical compounds

  • The urea-insoluble filensin immunoreactive peptides were only partially removed by alkali extraction, indicating a very avid association with the membrane [4].
 

Other interactions of BFSP1

 

Analytical, diagnostic and therapeutic context of BFSP1

  • Our results clarify previous confusion in the literature regarding the processing of filensin which arose because of the similar relative electrophoretic mobilities by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the different fragment sets [3].

References

  1. Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins. Gounari, F., Merdes, A., Quinlan, R., Hess, J., FitzGerald, P.G., Ouzounis, C.A., Georgatos, S.D. J. Cell Biol. (1993) [Pubmed]
  2. Differential protein expression in lens epithelial whole-mounts and lens epithelial cell cultures. Ong, M.D., Payne, D.M., Garner, M.H. Exp. Eye Res. (2003) [Pubmed]
  3. Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways. Sandilands, A., Prescott, A.R., Hutcheson, A.M., Quinlan, R.A., Casselman, J.T., FitzGerald, P.G. Eur. J. Cell Biol. (1995) [Pubmed]
  4. Intermediate filament cytoskeletal proteins associated with bovine lens native membrane fractions. Fleschner, C.R. Curr. Eye Res. (1998) [Pubmed]
 
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