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Low temperature‐induced dimerization of the bovine sperm serine protease, BSp66
Author(s) -
Cesari Andreina,
Cacciato Claudio Santiago,
De Castro Rosana Esther,
Sánchez Jorge Julián
Publication year - 2003
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10430
Subject(s) - sperm , proteases , semen , trypsin , serine protease , cryopreservation , serine , andrology , chemistry , antibody , biology , protease , microbiology and biotechnology , biochemistry , enzyme , immunology , anatomy , embryo , medicine
BSp120 and BSp66 are trypsin‐like serine proteases from bovine spermatozoa. The former is active in cryopreserved sperm samples while the latter shows proteolytic activity in recently obtained fresh sperm. Both proteases are immunologically related and co‐localize in the apical portion of the sperm head. In Western blots with specific antibodies, sperm samples incubated with reducing agents showed a decrease in the amount of BSp120, while BSp66 was detected with both anti‐BSp120 and anti‐BSp66 antibodies. BSp120 was evident in frozen intact spermatozoa after 60 days of semen cryopreservation and the kinetic of appearance of this protein was coincident with the decrease in the amount of BSp66. Identical results were obtained by freezing sperm extracts from fresh semen at −20°C. Our results suggest that BSp120 results from disulfide bond‐dimerization of BSp66 and that this process may be induced by temperatures below zero in both intact spermatozoa and in sperm extracts. J. Cell. Biochem. 88: 1057–1065, 2003. © 2003 Wiley‐Liss, Inc.