The function of filensin and phakinin in lens transparency

Mikako Oka, Hiroaki Kudo, Norio Sugama, Yuko Asami, Makoto Takehana

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Purpose: Beaded filaments are lens cell-specific intermediate filaments composed of two proteins: filensin and phakinin (CP49). Filensin and phakinin are believed to function in the maintenance of lens transparency. To elucidate the function of filensin and phakinin at the molecular level, we examined the degradation of these two proteins in normal and cataractous rat lenses. Methods: A hereditary cataract model, the Shumiya cataract rat (SCR), was used for these studies. Anti-filensin antibodies were raised against three different regions of the protein, the rod domain, the inner region of the tail domain, and the outer region of the tail domain. Anti-filensin and anti-phakinin antibodies were used to examine the conformation of degradation of filensin and phakinin by western blot analysis and fluorescent immunocytochemistry of cryosectioned lenses. Results: In the normal lens, filensin was processed from a 94 kDa protein to proteins of 50 kDa and 38 kDa. Similarly, phakinin was processed from a 49 kDa protein to one of 40 kDa. The concentrations of filensin and phakinin in the rat lens cortex fluctuated with age and decreased during cataractogenesis. The 50 kDa form of filensin decreased significantly before opacification. In the normal lens, phakinin, the filensin rod domain, and the filensin inner tail domain localized to membrane lining regions in the shallow cortex and to the central region of the cytoplasm in the deep cortex. The COOH-terminal domain of filensin localized to the membrane lining region in the deep cortex. In pre-cataractous lenses, phakinin and the filensin rod domain localized primarily to the membranes lining the shallow cortex region and were distributed throughout the cytoplasm of lens fiber cells in the deep cortex. Conclusions: The 50 kDa form of filensin is important for the localization of beaded filaments in lens fiber cells and for lens transparency.

Original languageEnglish
Pages (from-to)815-822
Number of pages8
JournalMolecular Vision
Volume14
Publication statusPublished - 2008 Apr 25

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Lenses
Tail
phakinin
filensin
Cataract
Membranes
Anti-Idiotypic Antibodies
Cytoplasm
Proteins
Intermediate Filaments
Proteolysis
Western Blotting
Immunohistochemistry
Maintenance

ASJC Scopus subject areas

  • Ophthalmology

Cite this

Oka, M., Kudo, H., Sugama, N., Asami, Y., & Takehana, M. (2008). The function of filensin and phakinin in lens transparency. Molecular Vision, 14, 815-822.

The function of filensin and phakinin in lens transparency. / Oka, Mikako; Kudo, Hiroaki; Sugama, Norio; Asami, Yuko; Takehana, Makoto.

In: Molecular Vision, Vol. 14, 25.04.2008, p. 815-822.

Research output: Contribution to journalArticle

Oka, M, Kudo, H, Sugama, N, Asami, Y & Takehana, M 2008, 'The function of filensin and phakinin in lens transparency', Molecular Vision, vol. 14, pp. 815-822.
Oka M, Kudo H, Sugama N, Asami Y, Takehana M. The function of filensin and phakinin in lens transparency. Molecular Vision. 2008 Apr 25;14:815-822.
Oka, Mikako ; Kudo, Hiroaki ; Sugama, Norio ; Asami, Yuko ; Takehana, Makoto. / The function of filensin and phakinin in lens transparency. In: Molecular Vision. 2008 ; Vol. 14. pp. 815-822.
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