Expression and localization of caveolin-1, and the presence of membrane rafts, in mouse and guinea pig spermatozoa

被引:109
作者
Travis, AJ
Merdiushev, T
Vargas, LA
Jones, BH
Purdon, MA
Nipper, RW
Galatioto, J
Moss, SB
Hunnicutt, GR
Kopf, GS [1 ]
机构
[1] Univ Penn, Med Ctr, Ctr Res Reprod & Womens Hlth, Philadelphia, PA 19104 USA
[2] Rockefeller Univ, Populat Council, New York, NY 10021 USA
关键词
spermatozoa; caveolin-1; membrane rafts; signaling; acrosome; germ cells;
D O I
10.1006/dbio.2001.0475
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In somatic cells, caveolin-1 plays several roles in membrane dynamics, including organization of detergent-insoluble lipid rafts, trafficking of cholesterol, and anchoring of signaling molecules. Events in sperm capacitation and fertilization require similar cellular functions, suggesting a possible role for caveolin-1 in spermatozoa. Immunoblot analysis demonstrated that caveolin-1 was indeed present in developing mouse male germ cells and both mouse and guinea pig spermatozoa. In mature spermatozoa, caveolin-1 was enriched in a Triton X-100-insoluble membrane fraction, as well as in membrane subdomains separable by means of their light buoyant densities through sucrose density gradient centrifugation. These data indicated the presence of membrane rafts enriched in caveolin-1 in spermatozoa. Indirect immunofluorescence analysis revealed caveolin-1 in the regions of the acrosome and flagellum in sperm of both species. Confocal immunofluorescence analysis of developing mouse male germ cells demonstrated partial co-localization with a marker for the acrosome. Furthermore, syntaxin-2, a protein involved in acrosomal exocytosis, was present in both raft and nonraft fractions in mature sperm. Together, these data indicated that sperm membranes possess distinct raft subdomains, and that caveolin-1 localized to regions appropriate for involvement with acrosomal biogenesis and exocytosis, as well as signaling pathways regulating such processes as capacitation and flagellar Motility. (C) 2001 Elsevier Science.
引用
收藏
页码:599 / 610
页数:12
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