Lens protein expression in mammals: Taxon-specificity and the recruitment of crystallins
- 1 March 1991
- journal article
- Published by Springer Nature in Journal of Molecular Evolution
- Vol. 32 (3) , 262-269
- https://doi.org/10.1007/bf02342749
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.Keywords
This publication has 30 references indexed in Scilit:
- A superfamily of NADPH-dependent reductases in eukaryotes and prokaryotesExperimental Eye Research, 1989
- Zeta-crystallin, a novel lens protein from the guinea pigCurrent Eye Research, 1987
- Gamma-crystallin family of the mouse lens: structural and evolutionary relationships.Proceedings of the National Academy of Sciences, 1984
- Complete Nucleotide Sequence of a cDNA Derived from Calf Lens γ-Crystallin mRNA: Presence of Alu I-Like DNA SequencesDNA, 1984
- Aldehyde dehydrogenase from human liverEuropean Journal of Biochemistry, 1984
- The Lens: Development, Proteins, Metabolism and CataractPublished by Elsevier ,1984
- Amino acid sequence homology among the 2-hydroxy acid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenase.Proceedings of the National Academy of Sciences, 1982
- Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.Proceedings of the National Academy of Sciences, 1982
- Primary Structure of the Bovine β‐Crystallin Bp ChainEuropean Journal of Biochemistry, 1981
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976