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RSP29, a protein secreted by rat round spermatids, stimulates the secretory function of Sertoli cells in the testis. By making use of the N-terminal sequence homology of RSP29 and a human protein hDP1 that we had previously isolated, we cloned the full length cDNA sequence that encodes RSP29. The entire amino acid sequence of RSP29 showed significant homology with that of hDP1, which was later identified as glyoxalase II. Southern analysis showed that the RSP29 protein sequence is highly conserved in eukaryotes and possibly in prokaryotes. The RSP29 mRNA is expressed in many tissues but has an extremely high abundance in testis. These data suggest that RSP29 may have an important function in most tissues of enkaryotic organisms. The high expression of RSP29 in testis and its stimulatory effects on Sertoli cells suggest that RSP29 could be especially important in the regulation of spermatogenesis.

Original publication

DOI

10.1006/bbrc.1997.7880

Type

Journal article

Journal

Biochem biophys res commun

Publication Date

29/12/1997

Volume

241

Pages

714 - 719

Keywords

Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Conserved Sequence, DNA, Complementary, Humans, Male, Molecular Sequence Data, Organ Specificity, Rats, Sequence Homology, Amino Acid, Species Specificity, Spermatids, Spermatogenesis, Thiolester Hydrolases