TAILIEUCHUNG - Báo cáo khoa học: Alternagin-C, a nonRGD-disintegrin, induces neutrophil migration via integrin signaling

Recently, a new protein containing a disintegrin domain, alternagin-C (Alt-C), was purified fromBothrops alternatus venom. Unlike other disintegrins, in Alt-C an ECD amino acid motif takes the place of the RGD sequence. Most dis-integrins contain an RGD/KGD sequence and are very potent inhibitors of platelet aggregation, as well as other cell interactions with the extracellular matrix, including tumor cell metastasis and angiogenesis. The present study investi-gated the effects of Alt-C on human neutrophil chemotaxis in vitro and the activation of integrin-mediated pathways | Eur. J. Biochem. 270 4799-4808 2003 FEBS 2003 doi Alternagin-C a nonRGD-disintegrin induces neutrophil migration via integrin signaling Andrea Mariano-Oliveira1 Ana Lucia J. Coelho1 Cristina H. B. Terruggi2 Heloisa S. Selistre-de-Araujo2 Christina Barja-Fidalgo1 and Marta S. De Freitas1 1 Departamento de Farmacologia Instituto de Biologia Universidade do Estado do Rio de Janeiro Brazil 2Departamento de Ciencias Fisiologicas Universidade Federal de Sao Carlos Brazil Recently a new protein containing a disintegrin domain alternagin-C Alt-C was purified from Bothrops alternatus venom. Unlike other disintegrins in Alt-C an ECD amino acid motif takes the place of the RGD sequence. Most dis-integrins contain an RGD KGD sequence and are very potent inhibitors of platelet aggregation as well as other cell interactions with the extracellular matrix including tumor cell metastasis and angiogenesis. The present study investigated the effects of Alt-C on human neutrophil chemotaxis in vitro and the activation of integrin-mediated pathways. Alt-C showed a potent chemotactic effect for human neutrophils when compared to N-formyl-methionyl-leucyl-phenylalanine peptide fMLP a classic chemotactic agent. Moreover preincubation of neutrophils with Alt-C significantly inhibited chemotaxis toward fMLP and itself. In addition a peptide containing an ECD sequence presented a chemotactic activity and significantly inhibited chemotaxis induced by Alt-C and fMLP. A significant increase of F-actin content was observed in cells treated with Alt-C showing that the chemotactic activity of Alt-C on neutrophils is driven by actin cytoskeleton dynamic changes. Futhermore this protein was able to induce an increase of phosphotyrosine content triggering focal adhesion kinase activation and its association with phosphatidylinositol 3-kinase. Alt-C was also able to induce a significant increase in extracellular signal-regulated kinase 2 nuclear translocation. The .

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