TAILIEUCHUNG - Báo cáo Y học: Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum

Bothrops snake venoms are known to induce local tissue damage suchas hemorrhage andmyonecrosis. Theopossum Didelphis marsupialisis resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim of this work was to clone and study the chemical, physicochemical andbiological properties ofDM64, an antimyotoxic protein from opossum serum. DM64 is an acidic protein showing 15% glycosylation andwith amolecular mass of 63 659 Da when analysed by MALDI-TOF MS. | Eur. J. Biochem. 269 6052-6062 2002 FEBS 2002 doi Functional analysis of DM64 an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum Surza L. G. Rocha1 Bruno Lomonte3 Ana G. C. Neves-Ferreira1 Monique R. O. Trugilho1 Inacio de L. M. Junqueira-de-Azevedo4 5 Paulo L. Ho4 5 Gilberto B. Domont2 Jose M. Gutierrez3 and Jonas Perales1 1 Departamento de Fisiologia e Farmacodinamica Instituto Oswaldo Cruz Fiocruz Rio de Janeiro Brazil 2Departamento de Bioquimica Instituto de Quimica Universidade Federal do Rio de Janeiro Rio de Janeiro Brazil 3Instituto Clodomiro Picado Facultad de Microbiologia Universidad de Costa Rica San Jose Costa Rica 4Centro de Biotecnologia Instituto Butantan and 5Instituto de Biociencias Universidade de Sao Paulo Sao Paulo Brazil Bothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim of this work was to clone and study the chemical physicochemical and biological properties of DM64 an antimyotoxic protein from opossum serum. DM64 is an acidic protein showing 15 glycosylation and with a molecular mass of 63 659 Da when analysed by MALDI-TOF MS. It was cloned and the amino acid sequence was found to be homologous to DM43 a metalloproteinase inhibitor from D. marsupialis serum and to human a1B-glycoprotein indicating the presence of five immunoglobulin-like domains. DM64 neutralized both the in vivo myotoxicity and the in vitro cytotoxicity of myotoxins I mt-I Asp49 and II mt-II Lys49 from Bothrops asper venom. The inhibitor formed noncovalent complexes with both toxins but did not inhibit the PLA2 activity of mt-I. Accordingly DM64 did not neutralize the anticoagulant effect of mt-I nor its intracerebroventricular lethality effects that depend on its enzymatic activity and which demonstrate the dissociation between .

• Báo cáo khoa học
• Report medicine
• traditional medicine
• scientific reports
• Crystal structure
• medical analysis
• biochemical studies
• medical knowledge
• medical research
• analysis of cytoplasmic
• oxidation
• bacteria
• hemoglobin
• medicine
• cell proliferation
• breast cancer
• chemical reaction
• gastric cancer
• hormone medicine
• tumor cells
• environmental medicine