title: Lens protein expression in mammals: taxon-specificity and the recruitment of crystallins.
abstract: Vertebrate lenses show remarkably taxon-specific patterns of protein composition, most obviously in the recruitment of enzymes as major crystallins. Phylogenetic relationships are particularly apparent in mammals. Here we describe eta-crystallin, which is probably identical to cytosolic aldehyde dehydrogenase, lens-specifically expressed at high abundance in the elephant shrews, primitive eutherians of the family Macroscelidae, and mu-crystallin, a novel lens protein expressed in some marsupials. We have also observed that enzymes that have been recruited as crystallins in some species are also moderately abundant in the lenses of other species. This hints that the origins of enzyme-crystallins may lie in a pool of enzymes widely expressed in lenses at fairly high levels, perhaps because they have important developmental or functional roles in the tissue.
authors.affiliation: Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892.
authors.forename: G
authors.initials: G
authors.lastname: Wistow
authors.forename: H
authors.initials: H
authors.lastname: Kim
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D015153:Blotting, Western; D003459:Crystallins / Q000737:chemistry*; D003720:Densitometry; D004591:Electrophoresis, Polyacrylamide Gel; D008322:Mammals / Q000378:metabolism*; D008394:Marsupialia / Q000378:metabolism; D008969:Molecular Sequence Data; D012788:Shrews / Q000378:metabolism
chemical_list: D003459:Crystallins; D000426:Alcohol Dehydrogenase