Laminin-derived peptide AG73 regulates migration, invasion, and protease activity of human oral squamous cell carcinoma cells through syndecan-1 and beta 1 integrin
| Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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| Data(s) |
20/10/2012
20/10/2012
2010
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| Resumo |
Squamous cell carcinoma is a prevalent head and neck tumor with high mortality. We studied the role played by laminin alpha 1 chain peptide AG73 on migration, invasion, and protease activity of cells (OSCC) from human oral squamous cell carcinoma. Immunohistochemistry and immunofluorescence analyzed expression of laminin alpha 1 chain and MMP9 in oral squamous cells carcinoma in vivo and in vitro. Migratory activity of AG73-treated OSCC cells was investigated by monolayer wound assays and in chemotaxis chambers. AG73-induced invasion was assessed in Boyden chambers. Invasion depends on MMPs. Conditioned media from cells grown on AG73 was subjected to zymography. We searched for AG73 receptors related to these activities in OSCC cells. Immunofluorescence analyzed AG73induced colocalization of syndecan-1 and beta 1 integrin. Cells had these receptors silenced by siRNA, followed by treatment with AG73 and analysis of migration, invasion, and protease activity. Oral squamous cell carcinoma expresses laminin alpha 1 chain and MMP9. OSCC cells treated with AG73 showed increased migration, invasion, and protease activity. AG73 induced colocalization of syndecan-1 and beta 1 integrin. Knockdown of these receptors decreased AG73-dependent migration, invasion, and protease activity. Syndecan-1 and beta 1 integrin signaling downstream of AG73 regulate migration, invasion, and MMP production by OSCC cells. Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) The State of Sao Paulo Research Foundation (FAPESP)[2006/57079-4] The State of Sao Paulo Research Foundation (FAPESP)[2008/57103-8] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Brazilian National Council for Scientific and Technological Development (CNPq)[471751/2003-0] Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Brazilian National Council for Scientific and Technological Development (CNPq)[304868/2006-0] Brazilian National Council for Scientific and Technological Development (CNPq)[470622/2007-5] Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) FAPESP[2007/51950-8] Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP) FAPESP[2005/55602-9] CNPq[504667/2008-4] Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) |
| Identificador |
TUMOR BIOLOGY, v.31, n.1, p.46-58, 2010 1010-4283 http://producao.usp.br/handle/BDPI/28089 10.1007/s13277-009-0008-x |
| Idioma(s) |
eng |
| Publicador |
SPRINGER |
| Relação |
Tumor Biology |
| Direitos |
restrictedAccess Copyright SPRINGER |
| Palavras-Chave | #Squamous cell carcinoma #Extracellular matrix #Laminin #Matrix metalloproteinases #Syndecan #Integrins #ADENOID CYSTIC CARCINOMA #BASEMENT-MEMBRANE #MATRIX METALLOPROTEINASES #PROGNOSTIC-SIGNIFICANCE #SYNTHETIC PEPTIDES #TUMOR INVASION #EXPRESSION #LINE #CANCER #SIKVAV #Oncology |
| Tipo |
article original article publishedVersion |
