title: Autoantigen 1 of the guinea pig sperm acrosome is the homologue of mouse Tpx-1 and human TPX1 and is a member of the cysteine-rich secretory protein (CRISP) family.
abstract: We have cloned and sequenced cDNAs encoding autoantigen 1 (AA1), a testis-specific protein and the major autoantigen of the guinea pig sperm acrosome. The cDNA predicts a precursor protein of 244 amino acids including a 21 amino acid hydrophobic, secretory signal sequence. The mature polypeptide is predicted to have a molecular mass of 24,891 Daltons which agrees with the experimentally determined molecular weight of 25,000. Consistent with previous studies demonstrating that AA1 is not a glycoprotein, the predicted amino acid sequence contained no canonical sites for N-linked glycosylation. Comparison with other sequences showed that AA1 is the guinea pig homologue of the testis-specific protein Tpx-1 in mice and TPX1 in humans. AA1 also showed significant amino acid sequence homology with other cysteine-rich secretory proteins (CRISP's): rat and mouse acidic epididymal glycoproteins (AEG; also known as proteins D/E in rats) and helothermine, a toxin from the Mexican beaded lizard. In addition, AA1 had a lesser degree of homology with antigen 5 (vespid wasp venom), PR-1 (a plant pathogenesis related protein), and GliPR (a protein identified in human gliomas). Northern analysis of RNA from purified guinea pig spermatogenic cells showed that a 1.5 kb message was first detected in pachytene spermatocytes, was strongest in round spermatids, and was detected at a low level in condensing spermatids. Immunoblot analysis and metabolic labeling data of AA1 in spermatogenic cells showed that the protein was synthesized as early as the pachytene spermatocyte stage of spermatogenesis. Thus, the patterns of AA1 mRNA and protein expression during spermatogenesis are similar to the expression of other acrosomal mRNAs and proteins that are first detected meiotically.
authors.affiliation: Department of Obstetrics and Gynecology, University of Pennsylvania Medical Center, Philadelphia 19104-6080, USA.
authors.forename: J A
authors.initials: JA
authors.lastname: Foster
authors.forename: G L
authors.initials: GL
authors.lastname: Gerton
mesh_terms: D000177:Acrosome / Q000276:immunology*; D000595:Amino Acid Sequence; D000818:Animals; D001324:Autoantigens / Q000235:genetics*; D001483:Base Sequence; D015815:Cell Adhesion Molecules; D002478:Cells, Cultured; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006023:Glycoproteins / Q000737:chemistry; D006168:Guinea Pigs; D008297:Male; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D012333:RNA, Messenger; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013087:Spermatids / Q000378:metabolism; D013090:Spermatocytes / Q000378:metabolism; D013094:Spermatozoa / Q000276:immunology / Q000378:metabolism; D013737:Testis / Q000166:cytology / Q000378:metabolism
chemical_list: D001324:Autoantigens; D015815:Cell Adhesion Molecules; C483816:Crisp2 protein, mouse; D018076:DNA, Complementary; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D012333:RNA, Messenger; C105215:autoantigen 1, Cavia porcellus