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Volume 271, Number 26,
Issue of June 28, 1996
pp. 15623-15628
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
A Retinaldehyde Dehydrogenase as a Structural Protein in a
Mammalian Eye Lens
GENE RECRUITMENT OF -CRYSTALLIN
(Received for publication, February 14, 1996, and in revised form, April 2, 1996)
Caroline
Graham
,
Jason
Hodin
and
Graeme
Wistow
From the Section on Molecular Structure and Function, Laboratory of
Molecular and Developmental Biology, National Eye Institute, National
Institutes of Health, Bethesda, Maryland 20892-2730
-Crystallin is a taxon-specific crystallin, a
major component of the eye lens in elephant shrews (Macroscelidea).
Sequence analysis of -crystallin from two genera of elephant shrews
and expression of recombinant -crystallin show that the protein is a
cytoplasmic (class 1) aldehyde dehydrogenase (ALDH1, EC) with
activity for the oxidation of retinaldehyde to retinoic acid. Unlike
many other mammals, elephant shrews have two ALDH1 genes. One encodes
ALDH1/ -crystallin which, in addition to its very high expression in
lens, is also the predominant form of ALDH1 expressed in other parts of
the eye. The second gene encodes a ``non-lens'' ALDH1 (ALDH1-nl)
which is the predominant form expressed in liver. This pattern of
tissue preference contrasts with other mammals which make use of the
same major ALDH1 transcript in both ocular and non-ocular tissues. Thus
the gene recruitment of ALDH1/ -crystallin as a structural protein in
elephant shrew lenses is associated with its collateral recruitment as
the major form of ALDH1 expressed in other parts of the eye.

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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.
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