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Sikvav a laminin-1-derived peptide, binds alpha3 integrin and regulates protease activity of a human salivary gland adenoid cystic carcinoma cell line through erk pathway

V. M. Freitas Ruy Gastaldoni Jaeger; Congresso do Instituto de Ciências Biomédicas (4. 2005 São Paulo)

Resumos São Paulo: Comissão de Cultura e Extensão Universitária do ICB/USP, 2005

São Paulo Comissão de Cultura e Extensão Universitária do ICB/USP 2005

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  • Título:
    Sikvav a laminin-1-derived peptide, binds alpha3 integrin and regulates protease activity of a human salivary gland adenoid cystic carcinoma cell line through erk pathway
  • Autor: V. M. Freitas
  • Ruy Gastaldoni Jaeger; Congresso do Instituto de Ciências Biomédicas (4. 2005 São Paulo)
  • Assuntos: HISTOLOGIA
  • É parte de: Resumos São Paulo: Comissão de Cultura e Extensão Universitária do ICB/USP, 2005
  • Notas Locais: Disponível somente em CD-ROM
  • Descrição: Objectives: Adenoid cystic carcinoma is a frequently occurring malignant salivary gland neoplasm, with high level of recurrence and metastasis. We have demonstrated that laminin and its derived peptide SIKVAV regulates morphology and protease activity of a cell line (CAC2) derived from human adenoid cystic carcinoma. Here we studied the regulatory mechanisms underlying protease activity induced by SIKVAV in CAC2 cells. Methods and results: MMPs 2 and 9 were immunolocalized in adenoid cystic carcinoma cells in vivo and in vitro. CAC2 cells were cultured on SIKVAV, to analyze the role of this peptid regulating protease activity. Zymography of the conditioned medium showed that SIKVAV enhanced secretion of MMPs 2 and 9. We analyzed a putative receptor for SIKVAV in CAC2 cells. Function-blocking antibodies to integrins alpha3beta1 and alpha6beta1 decreased both the adhesion of CAC2 cells to SIKVAV and protease secretion. A similar result was observed when cells were treated with EDTA. RNA interference (RNAi) was also used to silence alpha3 integrin expression. CAC2 cells with decreased alpha3 integrin expression were cultured on SIKVAV, and showed both decreased adhesion and protease activity. Furthermore, we isolated cell surface ligands using SIKVAV affinity chromatography, which were identified as alpha3 integrin by immunoblot. This result was confirmed by solid phase binding assays. We also defined a cell signaling pathway for the effect of integrins in CAC2 cells.
    A MAPK kinase inhibitor (UO126) decreased the effect of SIKVAV in the secretion of MMP-2 in CAC-2 cells, suggesting that SIKVAV signal is transduced by integrins and the ERK pathway. Conclusion: We propose that SIKVAV regulates protease activity of CAC2 cells through integrins and ERK Support: FAPESP (02/04208-0, 03/02724-4, 02/12387-2, CNPq 471751/2003-3)
  • Editor: São Paulo Comissão de Cultura e Extensão Universitária do ICB/USP
  • Data de criação/publicação: 2005
  • Formato: res. 86.
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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