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Extralenticular Expression of the Rodent βB2-Crystallin Gene

1998; Elsevier BV; Volume: 66; Issue: 2 Linguagem: Inglês

10.1006/exer.1997.0439

1096-0007

Ron P. Dirks, Siebe T. van Genesen, Jacqueline Kruse, LEJA JORISSEN, Nicolette H. Lubsen,

Biochemical effects in animals

The vertebrate lens evolved to collect light and focus it onto the retina. In development, the lens grows through massive elongation of epithelial cells possibly recapitulating the evolutionary origins of the lens. The refractive index of the lens is largely dependent on high concentrations of soluble proteins called crystallins. All vertebrate lenses share a common set of crystallins from two superfamilies (although other lineage specific crystallins exist). The α-crystallins are small heat shock proteins while the β- and γ-crystallins belong to a superfamily that contains structural proteins of uncertain function. The crystallins are expressed at very high levels in lens but are also found at lower levels in other cells, particularly in retina and brain. All these proteins have plausible connections to maintenance of cytoplasmic order and chaperoning of the complex molecular machines involved in the architecture and function of cells, particularly elongated and post-mitotic cells. They may represent a suite of proteins that help maintain homeostasis in such cells that are at risk from stress or from the accumulated insults of aging.