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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.)

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

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Author(s):
Portes-Junior, Jose A. [1] ; Yamanouye, Norma [2] ; Carneiro, Sylvia M. [3] ; Knittel, Paloma S. [1] ; Sant'Anna, Savio S. [4] ; Nogueira, Fabio C. S. [5] ; Junqueira, Magno [5] ; Magalhaes, Gerald S. [1] ; Domont, Gilberto B. [5] ; Moura-da-Silva, Ana M. [1]
Total Authors: 10
Affiliation:
[1] Inst Butantan, Lab Imunopatol, BR-05503900 Sao Paulo - Brazil
[2] Inst Butantan, Lab Farmacol, BR-05503900 Sao Paulo - Brazil
[3] Inst Butantan, Lab Biol Celular, BR-05503900 Sao Paulo - Brazil
[4] Inst Butantan, Lab Herpetol, BR-05503900 Sao Paulo - Brazil
[5] Univ Fed Rio de Janeiro, Dept Bioquim, Unidade Proteom, BR-21941909 Rio De Janeiro - Brazil
Total Affiliations: 5
Document type: Journal article
Source: JOURNAL OF PROTEOME RESEARCH; v. 13, n. 7, p. 3338-3348, JUL 2014.
Web of Science Citations: 14
Abstract

Snake venom metalloproteinases (SVMPs) are zinc-dependent enzymes responsible for most symptoms of human envenoming. Like matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase (ADAM) proteins, SVMPs are synthesized as zymogens, and enzyme activation is regulated by hydrolysis of their prodomain, but the processing of SVMPs is still unclear. In this study, we attempted to identify the presence of prodomain in different compartments of snake venom glands as zymogens or in the free form to elucidate some mechanism involved in SVMP activation. Using antibodies obtained by immunization with a recombinant prodomain, bands of zymogen molecular mass and prodomain peptides were detected mostly in gland extracts all along the venom production cycle and in the venom collected from the lumen at the peak of venom production. Prodomain was detected in secretory cells mostly in the secretory vesicles near the Golgi. We hypothesize that the processing of SVMPs starts within secretory vesicles and continues in the lumen of the venom gland just after enzyme secretion and involves different steps compared to ADAMs and MMPs but can be used as a model for studying the relevance of peptides resulting from prodomain processing and degradation for controlling the activity of metalloproteinases. (AU)

FAPESP's process: 10/01134-2 - Processing of metalloproteinase from Bothrops venom: activation of the catalytic activity by removal of pro-domain
Grantee:José Antonio Portes Junior
Support Opportunities: Scholarships in Brazil - Doctorate