High impact information on Bfsp1

• Remarkably, despite the inhibition of cell proliferation and apoptosis, the degeneration of lens fibers and aberrant expression of filensin were only marginally corrected in mgRb:Rb-/-:E2F1-/- fetuses at E15.5 but not at all at E18.5 or in mgRb:Rb-/-:p53-/mutant fetuses [1].
• 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 [2].
• It is well established that vertebrate lens fiber cells normally express a modified intermediate filament network consisting of the proteins filensin and CP49, and it was recently reported that the mouse strain 129 harbors mutations in CP49 that have the potential to confound the interpretation of gene knockout studies of the lens [3].
• Heterozygous animals exhibited an intermediate phenotype, showing a reduction in filensin transcript and moderate light-scattering at 5 months [4].
• Prenatal and postnatal mice were probed for the IF proteins phakosin, filensin, and vimentin, using light microscope immunocytochemical methodology [5].

Biological context of Bfsp1

• The results indicated that Bfsp1 maps at position 58 (+/- 6) on chromosome 2, in the vicinity of the blind-sterile (bs) locus [6].
• A minimal promoter region for mouse filensin of (-70 to +40) was identified [7].
• Comparison of the deduced amino acid sequences for rat and mouse filensin with those of cow and chick, and with other species of IF proteins, indicated the C-terminal non-alpha-helical tail domain of filensin to be one of the most divergent yet found in the vertebrate IF family [8].
• Localization of two conserved cis -acting enhancer regions for the filensin gene promoter that direct lens-specific expression [9].
• The results confirm previously reported phosphorylations of actin, phakinin, alphaA- and alphaB-crystallin, demonstrate previously unrecognized phosphorylations of filensin and betaB1-crystallin, and provide unequivocal evidence for phosphorylation of alphaA-crystallin at serine-148 [10].

Anatomical context of Bfsp1

• Gene structure and sequence comparisons of the eye lens specific protein, filensin, from rat and mouse: implications for protein classification and assembly [8].
• Filensin is a unique eye lens intermediate filament protein, and a major component of 'beaded filament' cytoskeletal network [9].

Other interactions of Bfsp1

• Filensin and phakinin are two lens-specific members of the intermediate filament (IF) superfamily of proteins [11].

Analytical, diagnostic and therapeutic context of Bfsp1

• Immunofluorescence demonstrated that FVB/N mice do not have detectable CP49 or filensin protein in the lens, whereas C57BL/6 mice have the expected protein distribution [3].
• Using RT-PCR and in situ hybridization analyses, we identified a subset of lens specific genes, most notably the late differentiation marker filensin, which were not properly induced during lens development in mgRb:Rb-/-fetuses [1].
• Here we report the molecular cloning, sequence and characterization of the mouse filensin gene [11].
• Translation and protein expression were characterized by Northern and Western blot analysis of both CP49 and its assembly partner filensin [12].

References