TY  - JOUR
PY  - 2014//
TI  - Unraveling the processing and activation of snake venom metalloproteinases
JO  - Journal of proteome research
A1  - Portes-Junior, José Antonio
A1  - Yamanouye, Norma
A1  - Carneiro, Sylvia Mendes
A1  - Knittel, Paloma Sirigatti
A1  - Sant'Anna, Sávio Stefanini
A1  - Nogueira, Fabio Cs
A1  - Junqueira, Magno
A1  - Magalhães, Geraldo Santana
A1  - Domont, Gilberto B.
A1  - Moura-da-Silva, Ana Maria
SP  - 3338
EP  - 3348
VL  - 13
IS  - 7
N2  - 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 pro-domain, but the processing of SVMPs is still unclear. In this study, we attempted to identify the presence of pro-domain 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 pro-domain, bands of zymogen molecular mass and pro-domain 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. Pro-domain 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 pro-domain processing and degradation for controlling the activity of metalloproteinases.<p />  <p>Language: en</p>
LA  - en
SN  - 1535-3893
UR  - http://dx.doi.org/10.1021/pr500185a
ID  - ref1
ER  -