FEBS Letters | |
Isolation and characterization of heparin‐ and phosphorylcholine‐binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1 | |
Töpfer-Petersen, Edda3  Sanz, Libia3  Urbanke, Claus2  Calvete, Juan J3  Raida, Manfred1  Gentzel, Marc3  | |
[1] Niedersächsisches Institut für Peptid-Forschung GmbH, Hannover, Germany;Biophysikalische Meßgeräteabteilung, Medizinische Hochschule, Hannover, Germany;Institut für Reproduktionsmedizin, Tierärztliche Hochschule Hannover, Bünteweg 15, 30559 Hannover-Kirchrode, Germany | |
关键词: Heparin-binding protein; Phosphorylcholine-binding protein; Stallion seminal plasma HSP-1 and HSP-2; Boar seminal plasma pB1 (pAIF-1); Spermadhesin AQN-1; Primary structure; O-Glycosylation; Fibronectin type II domain; | |
DOI : 10.1016/S0014-5793(97)00344-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
In the bovine, seminal plasma heparin-binding proteins bind to sperm lipids containing the phosphorylcholine group and mediate the capacitating effects of heparin-like glycosaminoglycans during sperm residence in the female genital tract. We report the characterization of heparin- and phosphorylcholine-binding proteins of stallion and boar seminal plasma.orseeminallasma proteins HSP-1 and HSP-2, and boar protein pB1, belong to the same family as the bull heparin- and phosphorylcholine-binding proteins BSP-A1/2, BSP-A3, and BSP-30K. We have determined the amino acid sequence and posttranslational modifications of boar glycoprotein pB1. It contains 105 amino acids arranged into a mosaic structure consisting of a N-terminal 18-residue O-glycosylated polypeptide followed by two tandemly organized 40–45-residue fibronectin type II domains. pB1 displays 60–65% amino acid sequence similarity with its equine and bovine homologues. However, in their respective seminal plasmas, the BSP and the HSP proteins associate into 90–150-kDa oligomeric complexes, whereas pB1 forms a 35–40-kDa complex with spermadhesin AQN-1. In addition, pB1 appears to be identical to the recently described leukocyte adhesion regulator of porcine seminal fluid pAIF-1. Our results tie in with the hypothesis that homologous proteins from different mammalian species may display distinct biological activities, which may be related to species-specific aspects of sperm physiology.
【 授权许可】
Unknown
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