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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.)

Molecular characterization of metalloproteases from Bothrops alternatus snake venom

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Pereira de Paula, Fernando Fonseca [1, 2] ; Ribeiro, Juliana Uema [3] ; Santos, Livia Mara [3] ; Ferreira de Souza, Dulce Helena [4] ; Leonardecz, Eduardo [1, 5] ; Henrique-Silva, Flavio [1] ; Selistre-de-Araujo, Heloisa Sobreiro [3]
Total Authors: 7
[1] Univ Fed Sao Carlos, Dept Genet & Evolucao, BR-13560 Sao Carlos, SP - Brazil
[2] Univ Brasilia, BR-70910900 Brasilia, DF - Brazil
[3] Univ Fed Sao Carlos, Dept Ciencias Fisiol, BR-13560 Sao Carlos, SP - Brazil
[4] Univ Fed Sao Carlos, Dept Quim, BR-13560 Sao Carlos, SP - Brazil
[5] EMBRAPA Genet Resources & Biotechnol, Brasilia, DF - Brazil
Total Affiliations: 5
Document type: Journal article
Source: Comparative Biochemistry and Physiology D-Genomics & Proteomics; v. 12, p. 74-83, DEC 2014.
Web of Science Citations: 2

We have previously demonstrated that alternagin-C (ALT-C), a disintegrin-like, Cys-rich protein isolated from Bothrops alternatus snake venom, induces human vascular endothelial cell (HUVEC) proliferation and angiogenesis in in vitro and in vivo assays. Therefore this protein could be interesting as a new approach for tissue regeneration studies. However, its primary sequence was not completely determined since the protein isolated from crude venom is usually a mixture of isoforms. Here we describe the transcriptome analysis of B. alternatus from the venom glands of a single male specimen. About 800 good-quality contigs were screened for snake venom metalloproteases/disintegrins, resulting in the following expression profile for these enzymes: 4% for P-I, 7% for P-II and 89% for P-III SVMPs. The PII-SVMP sequence code for RGD-disintegrins and all the expressed PIII-sequences have the ECD adhesive motif. A cDNA sequence coding for an ALT-C homolog was completely sequenced and characterized. Comparative sequence and structural analyses suggested new features that distinguish SVMP classes such as two prolyl endopetidase cleavage sites. All these data add new information on the expression pattern of metalloproteases of B. alternatus venom and may have practical applications for the production of recombinant disintegrins for cell adhesion studies. (C) 2014 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 98/14138-2 - Center for Structural Molecular Biotechnology
Grantee:Glaucius Oliva
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC