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Changes in lectin binding to bovine sperm during heparin‐induced capacitation
Author(s) -
Medeiros C.M.O,
Parrish J.J.
Publication year - 1996
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199608)44:4<525::aid-mrd12>3.0.co;2-x
Subject(s) - capacitation , sperm , acrosome , protamine , andrology , biology , heparin , propidium iodide , human fertilization , staining , acrosome reaction , wheat germ agglutinin , lectin , immunology , anatomy , biochemistry , medicine , apoptosis , genetics , programmed cell death
Changes in the plasma membrane of bovine sperm during heparin‐induced capacitation were detected by the binding of fluorescent labeled lectins to unfixed sperm. Of the seven lectins evaluated, only binding of wheat germ agglutinin (WGA) changed with capacitation. Sperm were classified into one of 5 patterns (p1–p5) based on staining with WGA, presence or absence of propidium iodide (PI) staining (dead or alive), and acrosomal integrity (acrosome intact or reacted). The major changes associated with capacitation occurred in p1 and p2. Sperm in p1 exhibited diffuse WGA binding over the anterior sperm head, were alive, and had intact acrosomes. In p2, sperm were also acrosome intact and alive, but lacked WGA binding. When sperm were incubated under capacitating conditions with heparin, there was a decrease over time in the percentage of sperm classified in p1 (p < 0.05) and an increase in the percentage of sperm in p2 (p < 0.05). When capacitation by heparin was delayed by the inclusion of glucose in the culture medium, the same heparin‐dependent changes in the percentage of sperm in p1 and p2 were delayed (p < 0.05). When capacitation by heparin was inhibited by including protamine in the culture medium, the percentage of sperm in p1 or p2 was not different from sperm incubated without heparin. Heparin‐induced capacitation was associated with a loss of WGA binding to the bovine sperm head. © 1996 Wiley‐Liss, Inc.