Post-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycan
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/25726 http://dx.doi.org/10.1074/jbc.272.19.12529 |
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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Veiga, Silvio Sanches [UNIFESP]Elias, MCQBGremski, W.Porcionatto, Marimélia Aparecida [UNIFESP]Silva, Roseli da [UNIFESP]Nader, Helena Bonciani [UNIFESP]Brentani, Ricardo Renzo [UNIFESP]UNIV FED PARANAUniversidade Federal de São Paulo (UNIFESP)2016-01-24T12:30:21Z2016-01-24T12:30:21Z1997-05-09Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997.0021-9258http://repositorio.unifesp.br/handle/11600/25726http://dx.doi.org/10.1074/jbc.272.19.1252910.1074/jbc.272.19.12529WOS:A1997WY82900041Cell-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 Science12529-12535engAmer Soc Biochemistry Molecular Biology IncJournal of Biological ChemistryPost-translational modifications of alpha(5)beta(1) integrin by glycosaminoglycan chains - the alpha(5)beta(1) integrin is a facultative proteoglycaninfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP11600/257262022-06-02 09:34:51.642metadata only accessoai:repositorio.unifesp.br:11600/25726Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-06-02T12:34:51Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.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.institution.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.issued.fl_str_mv |
1997-05-09 |
dc.date.accessioned.fl_str_mv |
2016-01-24T12:30:21Z |
dc.date.available.fl_str_mv |
2016-01-24T12:30:21Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/25726 http://dx.doi.org/10.1074/jbc.272.19.12529 |
dc.identifier.issn.none.fl_str_mv |
0021-9258 |
dc.identifier.doi.none.fl_str_mv |
10.1074/jbc.272.19.12529 |
dc.identifier.wos.none.fl_str_mv |
WOS:A1997WY82900041 |
identifier_str_mv |
Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 272, n. 19, p. 12529-12535, 1997. 0021-9258 10.1074/jbc.272.19.12529 WOS:A1997WY82900041 |
url |
http://repositorio.unifesp.br/handle/11600/25726 http://dx.doi.org/10.1074/jbc.272.19.12529 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.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 |
|
_version_ |
1802764138272784384 |