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Biology of Reproduction, Vol 51, 239-245, Copyright © 1994 by Society for the Study of Reproduction

ARTICLES

A novel, testis-specific member of the cellular lipophilic transport protein superfamily, deduced from a complimentary deoxyribonucleic acid clone

MC Schmitt, RS Jamison, MC Orgebin-Crist and DE Ong
Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232.

A novel member of the cellular lipophilic transport protein superfamily was identified after an antiserum raised against cellular retinoic acid- binding protein (CRABP) was found also to contain antibodies against another 15-kDa protein present in the cytosol of pubertal and adult rat testis. These antibodies were used to screen a rat testis cDNA expression library and isolate a 561-bp clone containing a full open reading frame from which the sequence of a novel 132 amino acid protein was deduced. The protein has 58% amino acid sequence identity to bovine myelin P2, 58% identity to murine adipocyte lipid-binding protein, and 40% identity to rat CRABP. Although the endogenous ligand has not yet been identified, conservation of residues involved in the binding of carboxylate groups suggests that the ligand is a fatty acid or an acidic retinoid. Tissue-specific expression was examined by Northern analysis and immunolocalization and appears to be restricted to late germ cells within the testis and epididymis. Immunostaining was first detectable in mid-pachytene spermatocytes and increased in intensity as these cells progressed to elongated spermatids, suggesting that this testis lipid-binding protein has a specific role in sperm development.


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P. R. Tovich and R. J. Oko
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J. Biol. Chem., August 22, 2003; 278(34): 32431 - 32438.
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