Presence of a laminin-binding chondroitin sulfate proteoglycan at the cell surface of a human melanoma cell Mel-85

Presence of a laminin-binding chondroitin sulfate proteoglycan at the cell surface of a human melanoma cell Mel-85

Autor Elias, MCQB Google Scholar
Veiga, S. S. Google Scholar
Gremski, W. Google Scholar
Porcionatto, M. A. Google Scholar
Nader, H. B. Google Scholar
Brentani, R. R. Google Scholar
Instituição Univ Fed Parana
Ludwig Inst Canc Res
Universidade Federal de São Paulo (UNIFESP)
Resumo Working with Mel-85 (a human melanoma cell line), we have been able to detect a laminin-binding molecule with an apparent molecular mass of 100/110 kDa (Mel-85-LBM). Reduction with beta-mercaptoethanol decreases its molecular mass but does not affect its ability to bind laminin. This laminin interaction seems to be very specific since Mel-85-LBM binds laminin, but not fibronectin, vitronectin or type I collagen in affinity chromatography experiments. the molecule has a negative net charge at physiological pH and binds laminin in a divalent cation dependent way. Mel-85-LBM was metabolically radiolabeled with sodium [S-35]-sulfate and chemical beta-elimination of purified Mel-85-LBM releases chondroitin sulfate chains. Mel-85-LBM is also sensitive to chondroitinase ABC digestion. These findings show that this molecule is a chondroitin sulfate proteoglycan. the location of this proteoglycan at the cell surface is evidenced by experiments using a polyclonal antiserum raised against purified Mel-85LBM, that specifically reacts with just one molecule by western blotting among Mel-85 total cell extract as well as produces a positive signal by flow cytometry and a fluorescence profile of Mel-85 cells adhered on laminin.
Palavra-chave laminin receptors
proteoglycan
cell adhesion
Idioma Inglês
Data de publicação 1999-07-01
Publicado em Molecular and Cellular Biochemistry. Dordrecht: Kluwer Academic Publ, v. 197, n. 1-2, p. 39-48, 1999.
ISSN 0300-8177 (Sherpa/Romeo, fator de impacto)
Publicador Kluwer Academic Publ
Extensão 39-48
Fonte http://dx.doi.org/10.1023/A:1006952731037
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000082651700006
Endereço permanente http://repositorio.unifesp.br/handle/11600/26107

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