A novel, testis-specific member of the cellular lipophilic transport protein superfamily, deduced from a complimentary deoxyribonucleic acid clone.
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.[1]References
- A novel, testis-specific member of the cellular lipophilic transport protein superfamily, deduced from a complimentary deoxyribonucleic acid clone. Schmitt, M.C., Jamison, R.S., Orgebin-Crist, M.C., Ong, D.E. Biol. Reprod. (1994) [Pubmed]
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