Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/29775 http://dx.doi.org/10.1242/jcs.03459 |
Resumo: | The physiological functions of the cellular prion protein, PrPC, as a cell surface pleiotropic receptor are under debate. We report that PrPC interacts with vitronectin but not with fibronectin or collagen. the binding sites mediating this PrPC-vitronectin interaction were mapped to residues 105-119 of PrPC and the residues 307-320 of vitronectin. the two proteins were co-localized in embryonic dorsal root ganglia from wild-type mice. Vitronectin addition to cultured dorsal root ganglia induced axonal growth, which could be mimicked by vitronectin peptide 307-320 and abrogated by anti-PrPC antibodies. Full-length vitronectin, but not the vitronectin peptide 307-320, induced axonal growth of dorsal root neurons from two strains of PrPC-null mice. Functional assays demonstrated that relative to wild-type cells, PrPC-null dorsal root neurons were more responsive to the Arg-Gly-Asp peptide (an integrin-binding site), and exhibited greater alpha v beta 3 activity. Our findings indicate that PrPC plays an important role in axonal growth, and this function may be rescued in PrPC-knockout animals by integrin compensatory mechanisms. |
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Hajj, Glaucia N. M.Lopes, Marilene H.Mercadante, Adriana F.Veiga, Silvio Sanches [UNIFESP]Silveira, Rafael Bertoni da [UNIFESP]Santos, Tiago G.Ribeiro, Karina C. B.Juliano, Maria Aparecida [UNIFESP]Jacchieri, Saul G.Zanata, Silvio M.Martins, Vilma R.Hosp Alemao Oswaldo CruzUniversidade de São Paulo (USP)Hosp CancUniv Fed ParanaUniversidade Federal de São Paulo (UNIFESP)2016-01-24T13:48:45Z2016-01-24T13:48:45Z2007-06-01Journal of Cell Science. Cambridge: Company of Biologists Ltd, v. 120, n. 11, p. 1915-1926, 2007.0021-9533http://repositorio.unifesp.br/handle/11600/29775http://dx.doi.org/10.1242/jcs.03459WOS000246665300011.pdf10.1242/jcs.03459WOS:000246665300011The physiological functions of the cellular prion protein, PrPC, as a cell surface pleiotropic receptor are under debate. We report that PrPC interacts with vitronectin but not with fibronectin or collagen. the binding sites mediating this PrPC-vitronectin interaction were mapped to residues 105-119 of PrPC and the residues 307-320 of vitronectin. the two proteins were co-localized in embryonic dorsal root ganglia from wild-type mice. Vitronectin addition to cultured dorsal root ganglia induced axonal growth, which could be mimicked by vitronectin peptide 307-320 and abrogated by anti-PrPC antibodies. Full-length vitronectin, but not the vitronectin peptide 307-320, induced axonal growth of dorsal root neurons from two strains of PrPC-null mice. Functional assays demonstrated that relative to wild-type cells, PrPC-null dorsal root neurons were more responsive to the Arg-Gly-Asp peptide (an integrin-binding site), and exhibited greater alpha v beta 3 activity. Our findings indicate that PrPC plays an important role in axonal growth, and this function may be rescued in PrPC-knockout animals by integrin compensatory mechanisms.Hosp Alemao Oswaldo Cruz, Ludwig Inst Canc Res, São Paulo, BrazilUniv São Paulo, Inst Quim, Dept Bioquim, BR-05508 São Paulo, BrazilHosp Canc, Ctr Tratamento & Pesquisa, São Paulo, BrazilUniv Fed Parana, Dept Patol Basica, BR-80060000 Curitiba, Parana, BrazilUniv Fed Parana, Dept Biol Celular, BR-80060000 Curitiba, Parana, BrazilUniversidade Federal de São Paulo, INFAR, BR-04023062 São Paulo, BrazilUniversidade Federal de São Paulo, INFAR, BR-04023062 São Paulo, BrazilWeb of Science1915-1926engCompany of Biologists LtdJournal of Cell Sciencedorsal root gangliaextracellular matrixcellular prion proteinvitronectinaxon growthintegrinsCellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrinsinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000246665300011.pdfapplication/pdf2289974${dspace.ui.url}/bitstream/11600/29775/1/WOS000246665300011.pdff8aa67021dd7662436b68712d06fec5bMD51open accessTEXTWOS000246665300011.pdf.txtWOS000246665300011.pdf.txtExtracted texttext/plain69929${dspace.ui.url}/bitstream/11600/29775/2/WOS000246665300011.pdf.txtd8660a11ec59d3770bd4d6df129539c0MD52open access11600/297752022-07-08 10:58:20.079open accessoai:repositorio.unifesp.br:11600/29775Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-07-08T13:58:20Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
title |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
spellingShingle |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins Hajj, Glaucia N. M. dorsal root ganglia extracellular matrix cellular prion protein vitronectin axon growth integrins |
title_short |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
title_full |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
title_fullStr |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
title_full_unstemmed |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
title_sort |
Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins |
author |
Hajj, Glaucia N. M. |
author_facet |
Hajj, Glaucia N. M. Lopes, Marilene H. Mercadante, Adriana F. Veiga, Silvio Sanches [UNIFESP] Silveira, Rafael Bertoni da [UNIFESP] Santos, Tiago G. Ribeiro, Karina C. B. Juliano, Maria Aparecida [UNIFESP] Jacchieri, Saul G. Zanata, Silvio M. Martins, Vilma R. |
author_role |
author |
author2 |
Lopes, Marilene H. Mercadante, Adriana F. Veiga, Silvio Sanches [UNIFESP] Silveira, Rafael Bertoni da [UNIFESP] Santos, Tiago G. Ribeiro, Karina C. B. Juliano, Maria Aparecida [UNIFESP] Jacchieri, Saul G. Zanata, Silvio M. Martins, Vilma R. |
author2_role |
author author author author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Hosp Alemao Oswaldo Cruz Universidade de São Paulo (USP) Hosp Canc Univ Fed Parana Universidade Federal de São Paulo (UNIFESP) |
dc.contributor.author.fl_str_mv |
Hajj, Glaucia N. M. Lopes, Marilene H. Mercadante, Adriana F. Veiga, Silvio Sanches [UNIFESP] Silveira, Rafael Bertoni da [UNIFESP] Santos, Tiago G. Ribeiro, Karina C. B. Juliano, Maria Aparecida [UNIFESP] Jacchieri, Saul G. Zanata, Silvio M. Martins, Vilma R. |
dc.subject.eng.fl_str_mv |
dorsal root ganglia extracellular matrix cellular prion protein vitronectin axon growth integrins |
topic |
dorsal root ganglia extracellular matrix cellular prion protein vitronectin axon growth integrins |
description |
The physiological functions of the cellular prion protein, PrPC, as a cell surface pleiotropic receptor are under debate. We report that PrPC interacts with vitronectin but not with fibronectin or collagen. the binding sites mediating this PrPC-vitronectin interaction were mapped to residues 105-119 of PrPC and the residues 307-320 of vitronectin. the two proteins were co-localized in embryonic dorsal root ganglia from wild-type mice. Vitronectin addition to cultured dorsal root ganglia induced axonal growth, which could be mimicked by vitronectin peptide 307-320 and abrogated by anti-PrPC antibodies. Full-length vitronectin, but not the vitronectin peptide 307-320, induced axonal growth of dorsal root neurons from two strains of PrPC-null mice. Functional assays demonstrated that relative to wild-type cells, PrPC-null dorsal root neurons were more responsive to the Arg-Gly-Asp peptide (an integrin-binding site), and exhibited greater alpha v beta 3 activity. Our findings indicate that PrPC plays an important role in axonal growth, and this function may be rescued in PrPC-knockout animals by integrin compensatory mechanisms. |
publishDate |
2007 |
dc.date.issued.fl_str_mv |
2007-06-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T13:48:45Z |
dc.date.available.fl_str_mv |
2016-01-24T13:48:45Z |
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 Cell Science. Cambridge: Company of Biologists Ltd, v. 120, n. 11, p. 1915-1926, 2007. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/29775 http://dx.doi.org/10.1242/jcs.03459 |
dc.identifier.issn.none.fl_str_mv |
0021-9533 |
dc.identifier.file.none.fl_str_mv |
WOS000246665300011.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1242/jcs.03459 |
dc.identifier.wos.none.fl_str_mv |
WOS:000246665300011 |
identifier_str_mv |
Journal of Cell Science. Cambridge: Company of Biologists Ltd, v. 120, n. 11, p. 1915-1926, 2007. 0021-9533 WOS000246665300011.pdf 10.1242/jcs.03459 WOS:000246665300011 |
url |
http://repositorio.unifesp.br/handle/11600/29775 http://dx.doi.org/10.1242/jcs.03459 |
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eng |
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eng |
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Journal of Cell Science |
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1915-1926 |
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Company of Biologists Ltd |
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Company of Biologists Ltd |
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