title: Role of short-range protein interactions in lens opacifications.
abstract: At high protein concentrations found in the lens, short-range order of lens proteins results in a medium of relatively constant protein density and refractive index that minimizes scattering of light. During aging and cataractogenesis of the lens, formation of high molecular weight aggregates causes fluctuations in this protein density, resulting in light scattering and a concomitant decrease in transparency, with eventual lens opacification. This review summarizes what is known about the molecular nature of short-range order, both in the normal and cataractous lens, then hypothesizes that part of this order involves heterologous crystallin interactions that may be necessary for the maintenance of lens transparency. A summary of past and possible future experimental approaches will be reviewed that can be used to ascertain the existence of these interactions and their possible changes during lens opacification.
authors.affiliation: Division of Biology, Kansas State University, Manhattan, KS 66506, USA.
authors.forename: Aldo
authors.initials: A
authors.lastname: Ponce
authors.forename: Christopher
authors.initials: C
authors.lastname: Sorensen
authors.forename: Larry
authors.initials: L
authors.lastname: Takemoto
mesh_terms: D000818:Animals; D002386:Cataract / Q000235:genetics / Q000378:metabolism*; D003459:Crystallins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007908:Lens, Crystalline / Q000378:metabolism*; D008954:Models, Biological; D009154:Mutation; D011499:Protein Processing, Post-Translational
chemical_list: D003459:Crystallins