Regulated serine proteinase lytic system on mammalian sperm surface: There must be a role

被引:29
作者
Cesari, Andreina [1 ]
de los Angeles Monclus, Maria [2 ]
Tejon, Gabriela P. [1 ]
Clementi, Marisa [2 ]
Fornes, Miguel W. [2 ]
机构
[1] Univ Nacl Mar del Plata, Inst Invest Biol, CONICET, RA-7600 Mar Del Plata, Buenos Aires, Argentina
[2] Natl Univ Cuyo CCT Mendoza, CONICET, Sch Med, LIAM,IHEM, Mendoza, Argentina
关键词
Sperm; Serine proteases; Inhibitors; Semen; Seminal plasma; ZONA-PELLUCIDA-BINDING; BULL SEMINAL PLASMA; C INHIBITOR GENE; ACROSIN INHIBITOR; MOLECULAR-CLONING; PLASMINOGEN-ACTIVATOR; PROTEASE INHIBITOR; HUMAN-SPERMATOZOA; SEQUENCE-ANALYSIS; IN-VITRO;
D O I
10.1016/j.theriogenology.2010.03.029
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Serine proteases play key roles in many biological processes, regulating surface proteins that are key-points in signaling pathways. Several studies have reported the presence of members of this protease family in sperm from various species. The precise regulation of their activity is thought to be performed by specific endogenous or extrinsic inhibitors. The contribution of the sperm serine to proteases to fertilization has been demonstrated by synthetic inhibitors and several single knock out experiments, but to date, there is no evidence that links a single enzyme to a single step of fertilization. The explanation for the failure in the understanding of the "one-enzyme-one-process" hypothesis may be that sperm have multiple serine proteases as a mechanism to ensure the success of fertilization. In addition to the classical purification and expression studies, we summarized recent advances in proteomics and performed a bioinformatics search of proteases and inhibitors, providing support for the idea of redundancy. This review summarizes current knowledge about serine proteases and their inhibitors in sperm capacitation and maturation, identifies questions that need to be answered, and provides a reference for future research. (C) 2010 Elsevier Inc. All rights reserved.
引用
收藏
页码:699 / 711
页数:13
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