Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan

Detalhes bibliográficos
Autor(a) principal: Veiga, Silvio Sanches [UNIFESP]
Data de Publicação: 1997
Outros Autores: Elias, MCQB, Gremski, W., Porcionatto, Marimélia Aparecida [UNIFESP], Silva, Roseli da [UNIFESP], Nader, Helena Bonciani [UNIFESP], Brentani, Ricardo Renzo [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1074/jbc.272.19.12529
http://repositorio.unifesp.br/handle/11600/25726
Resumo: Cell-fibronectin interactions, mediated through several different receptors, have been implicated in a wide variety of cellular properties. Among the cell surface receptors for fibronectin, integrins are the best characterized, particularly the prototype alpha(5) beta(1) integrin. Using [I-125]iodine cell surface labeling or metabolic radiolabeling with sodium [S-35]sulfate, we identified alpha(5) beta(1) integrin as the only sulfated integrin among beta(1) integrin heterodimers expressed by the human melanoma cell line Mel-85. This facultative sulfation was confirmed not only by immunoprecipitation reactions using specific monoclonal antibodies but also by fibronectin affinity chromatography, two dimensional electrophoresis, and chemical reduction, the covalent nature of alpha(5) beta(1) integrin sulfation was evidenced by its resistance to treatments with high ionic, chaotrophic, and denaturing agents such as 4 nz NaCl, 4 hn MgCl2, 8 M urea, and 6 ar guanidine HCl. Based on deglycosylation procedures as chemical beta-elimination, proteinase K digestion, and susceptibility to glycosaminoglycan lyases (chondroitinase ABC and heparitinases I and II), it was demonstrated that the alpha(5) beta(1) heterodimer and alpha(5) and beta(1) integrin subunits were proteoglycans. the importance of alpha(5) beta(1) sulfation was strengthened by the finding that this molecule is also sulfated in MG-63 (human osteosarcoma) and HCT-8 (human colon adenocarcinoma) cells.
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spelling Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycanCell-fibronectin interactions, mediated through several different receptors, have been implicated in a wide variety of cellular properties. Among the cell surface receptors for fibronectin, integrins are the best characterized, particularly the prototype alpha(5) beta(1) integrin. Using [I-125]iodine cell surface labeling or metabolic radiolabeling with sodium [S-35]sulfate, we identified alpha(5) beta(1) integrin as the only sulfated integrin among beta(1) integrin heterodimers expressed by the human melanoma cell line Mel-85. This facultative sulfation was confirmed not only by immunoprecipitation reactions using specific monoclonal antibodies but also by fibronectin affinity chromatography, two dimensional electrophoresis, and chemical reduction, the covalent nature of alpha(5) beta(1) integrin sulfation was evidenced by its resistance to treatments with high ionic, chaotrophic, and denaturing agents such as 4 nz NaCl, 4 hn MgCl2, 8 M urea, and 6 ar guanidine HCl. Based on deglycosylation procedures as chemical beta-elimination, proteinase K digestion, and susceptibility to glycosaminoglycan lyases (chondroitinase ABC and heparitinases I and II), it was demonstrated that the alpha(5) beta(1) heterodimer and alpha(5) and beta(1) integrin subunits were proteoglycans. the importance of alpha(5) beta(1) sulfation was strengthened by the finding that this molecule is also sulfated in MG-63 (human osteosarcoma) and HCT-8 (human colon adenocarcinoma) cells.UNIV FED PARANA,CTR POLITECN,DEPT CELL BIOL,SETER CIENCIAS BIOL,BR-81531990 CURITIBA,PARANA,BRAZILUniversidade Federal de São Paulo,ESCOLA PAULISTA MED,DEPT BIOCHEM,BR-04044020 São Paulo,BRAZILUniversidade Federal de São Paulo,ESCOLA PAULISTA MED,DEPT BIOCHEM,BR-04044020 São Paulo,BRAZILWeb of ScienceAmer Soc Biochemistry Molecular Biology IncUNIV FED PARANAUniversidade Federal de São Paulo (UNIFESP)Veiga, Silvio Sanches [UNIFESP]Elias, MCQBGremski, W.Porcionatto, Marimélia Aparecida [UNIFESP]Silva, Roseli da [UNIFESP]Nader, Helena Bonciani [UNIFESP]Brentani, Ricardo Renzo [UNIFESP]2016-01-24T12:30:21Z2016-01-24T12:30:21Z1997-05-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion12529-12535http://dx.doi.org/10.1074/jbc.272.19.12529Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997.10.1074/jbc.272.19.125290021-9258http://repositorio.unifesp.br/handle/11600/25726WOS:A1997WY82900041engJournal of Biological Chemistryinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2022-06-02T09:34:51Zoai:repositorio.unifesp.br/:11600/25726Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652022-06-02T09:34:51Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
title Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
spellingShingle Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
Veiga, Silvio Sanches [UNIFESP]
title_short Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
title_full Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
title_fullStr Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
title_full_unstemmed Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
title_sort Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
author Veiga, Silvio Sanches [UNIFESP]
author_facet Veiga, Silvio Sanches [UNIFESP]
Elias, MCQB
Gremski, W.
Porcionatto, Marimélia Aparecida [UNIFESP]
Silva, Roseli da [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author_role author
author2 Elias, MCQB
Gremski, W.
Porcionatto, Marimélia Aparecida [UNIFESP]
Silva, Roseli da [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv UNIV FED PARANA
Universidade Federal de São Paulo (UNIFESP)
dc.contributor.author.fl_str_mv Veiga, Silvio Sanches [UNIFESP]
Elias, MCQB
Gremski, W.
Porcionatto, Marimélia Aparecida [UNIFESP]
Silva, Roseli da [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Brentani, Ricardo Renzo [UNIFESP]
description Cell-fibronectin interactions, mediated through several different receptors, have been implicated in a wide variety of cellular properties. Among the cell surface receptors for fibronectin, integrins are the best characterized, particularly the prototype alpha(5) beta(1) integrin. Using [I-125]iodine cell surface labeling or metabolic radiolabeling with sodium [S-35]sulfate, we identified alpha(5) beta(1) integrin as the only sulfated integrin among beta(1) integrin heterodimers expressed by the human melanoma cell line Mel-85. This facultative sulfation was confirmed not only by immunoprecipitation reactions using specific monoclonal antibodies but also by fibronectin affinity chromatography, two dimensional electrophoresis, and chemical reduction, the covalent nature of alpha(5) beta(1) integrin sulfation was evidenced by its resistance to treatments with high ionic, chaotrophic, and denaturing agents such as 4 nz NaCl, 4 hn MgCl2, 8 M urea, and 6 ar guanidine HCl. Based on deglycosylation procedures as chemical beta-elimination, proteinase K digestion, and susceptibility to glycosaminoglycan lyases (chondroitinase ABC and heparitinases I and II), it was demonstrated that the alpha(5) beta(1) heterodimer and alpha(5) and beta(1) integrin subunits were proteoglycans. the importance of alpha(5) beta(1) sulfation was strengthened by the finding that this molecule is also sulfated in MG-63 (human osteosarcoma) and HCT-8 (human colon adenocarcinoma) cells.
publishDate 1997
dc.date.none.fl_str_mv 1997-05-09
2016-01-24T12:30:21Z
2016-01-24T12:30:21Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1074/jbc.272.19.12529
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997.
10.1074/jbc.272.19.12529
0021-9258
http://repositorio.unifesp.br/handle/11600/25726
WOS:A1997WY82900041
url http://dx.doi.org/10.1074/jbc.272.19.12529
http://repositorio.unifesp.br/handle/11600/25726
identifier_str_mv Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997.
10.1074/jbc.272.19.12529
0021-9258
WOS:A1997WY82900041
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of Biological Chemistry
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 12529-12535
dc.publisher.none.fl_str_mv Amer Soc Biochemistry Molecular Biology Inc
publisher.none.fl_str_mv Amer Soc Biochemistry Molecular Biology Inc
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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