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Glycoprotein Changes in the Bovine Sperm Plasma Membrane during Maturation in the Epididymis
Author(s) -
Buchanan Teresa L,
Mclean Eric,
Raychoudhury Samir,
Nagdas Subir K
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.581.6
Subject(s) - epididymis , capacitation , sperm , glycoprotein , acrosome , biology , flagellum , acrosome reaction , membrane , microbiology and biotechnology , chemistry , andrology , biochemistry , genetics , medicine , gene
The plasma membrane of spermatozoa is a mosaic of distinct domains corresponding to defined segments of the head and the flagellum. To attain fertilizing ability, sperm undergo several biochemical changes during transit in the epididymal duct. The objective of the present study is to analyze the maturation‐associated changes of bovine sperm surface glycoproteins during epididymal maturation. Among the several lectins tested, we found a 19kDa WGA binding polypeptide, termed as WGA19 polypeptide, only present in the plasma membranes of cauda sperm, not in the caput sperm plasma membrane. Both luminal fluid and spermatozoa of the cauda epididymis exhibited the presence of WGA19 polypeptide. No band was observed in epididymal fluid or spermatozoa of the caput epididymis. Phase separation analysis of cauda sperm plasma membrane fraction demonstrates that WGA19 polypeptide is an integral membrane protein. Proteomic identification of the WGA19 polypeptide yielded five peptides that matched the sequence of human calmodulin 3. The WGA19 polypeptide was retained within the hybrid membrane complex of bovine sperm following capacitation and the acrosome reaction. This study suggests that 19kDa WGA polypeptide secreted from the cauda epididymis, anchores or/ binds to the plasma membrane, and may have an important role in sperm‐egg interactions. Supported by NIH/NIGMS/1SC3GM096875‐01 and Graduate School Program.