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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Peptidase activities in Crotalus durissus terrificus semen

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Author(s):
Marinho, Camila Eduardo [1, 2] ; Almeida-Santos, Selma Maria [3] ; Carneiro, Sylvia Mendes [4] ; Yamasaki, Simone Cristina [1] ; Silveira, Paulo Flavio [1]
Total Authors: 5
Affiliation:
[1] Inst Butantan, Pharmacol Lab, BR-05503900 Sao Paulo - Brazil
[2] Univ Sao Paulo, Inst Biociencias, Dept Physiol, BR-05508900 Sao Paulo - Brazil
[3] Inst Butantan, Lab Ecol & Evolut, BR-05503900 Sao Paulo - Brazil
[4] Inst Butantan, Lab Cellular Biol, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Reproduction; v. 136, n. 6, p. 767-776, DEC 2008.
Web of Science Citations: 2
Abstract

To understand the role of peptidases in seminal physiology of Crotalus durissus terrificus, activity levels of representative enzymes in semen and their sensitivities to inhibitors, cofactors, and peptide hormones were evaluated. The existence of seminal fractions and the association of peptidases with these fractions were also characterized for the first time in snakes. The prominent inhibitors of aminopeptidases (APs) were amastatin for acid, basic, and neutral; bestatin for basic; and diprotin A for dipeptidyl-IV. Cystyl and prolylimino AN were similarly susceptible to the majority of these inhibitors. The basic and neutral were characterized as metallo-peptidases, acid AP was activated by MnCl(2), and cystyl, prolyl-imino, and type I pyroglutamyl were characterized as sulphydryl-dependent APs. Angiotensin II, vasotocin, bradykinin, fertilization-promoting peptide, and TRH altered the majority of these peptidase activities; these peptides are possible substrates and/or modulators of these peptidases. Peptidase activities were found in all seminal fractions: seminal plasma (SP), prostasome-like (PR) structures, and soluble (S-) and membrane-bound fractions (MFs) of spermatozoa. The levels of activity of each peptidase varied among different seminal fractions. In SP, the higher activities were puromycin-insensitive neutral and basic APs. in PR, the higher activity was puromycin-insensitive neutral AP. In spermatozoa, the higher activity in subcellular SF was puromycin-sensitive neutral, while in MF both puromycin-sensitive and -insensitive neutral AN were equally higher than the other examined peptidases. Data suggested that these peptidases, mainly basic and neutral, have a high relevance in regulating seminal functions of C. d. terrificus. (AU)

FAPESP's process: 07/06829-6 - Effects of Apis mellifera venom on anti-type II collagen antibody, interleukin 6 and peptidases of synovia, synovium and circulating leukocytes in rats with type-II collagen-induced arthritis
Grantee:Simone Cristina Yamasaki
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 05/03745-0 - The rattlesnake Crotalus durissus terrificus (Viperidae: Crotalinae) as an experimental model to study the involvement of peptidases in the survival of spermatozoids
Grantee:Camila Eduardo Marinho
Support Opportunities: Scholarships in Brazil - Master