Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study

Detalhes bibliográficos
Autor(a) principal: Caseli, Luciano [UNIFESP]
Data de Publicação: 2012
Outros Autores: Cavalheiro, Renan Pelluzzi [UNIFESP], Nader, Helena Bonciani [UNIFESP], Lopes, Carla Cristina [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://repositorio.unifesp.br/handle/11600/34810
http://dx.doi.org/10.1016/j.bbamem.2012.01.012
Resumo: Investigating the role of proteoglycans associated to cell membranes is fundamental to comprehend biochemical process that occurs at the level of membrane surfaces. in this paper, we exploit syndecan-4, a heparan sulfate proteoglycan obtained from cell cultures, in lipid Langmuir monolayers at the air-water interface. the monolayer served as a model for half a membrane, and the molecular interactions involved could be evaluated with tensiometry and vibrational spectroscopy techniques. Polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS) employed in a constant surface pressure regime showed that the main chemical groups for syndecan-4 were present at the air-water interface. Subsequent monolayer decompression and compression showed surface pressure-area isotherms with a large expansion for the lipid monolayers interacting with the cell culture reported to over-express syndecan-4, which was also an indication that the proteoglycan was inserted in the lipid monolayer. the introduction of biological molecules with affinity for syndecam-4, such as growth factors, which present a key role in biochemical process of cell signaling, changed the surface properties of the hybrid film, leading to a model, by which the growth factor binds to the sulfate groups present in the heparan sulfate chains. the polypeptide moiety of syndecan-4 responds to this interaction changing its conformation, which leads to lipid film relaxation and further monolayer condensation. (C) 2012 Elsevier B.V. All rights reserved.
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spelling Caseli, Luciano [UNIFESP]Cavalheiro, Renan Pelluzzi [UNIFESP]Nader, Helena Bonciani [UNIFESP]Lopes, Carla Cristina [UNIFESP]Universidade Federal de São Paulo (UNIFESP)2016-01-24T14:27:08Z2016-01-24T14:27:08Z2012-05-01Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1818, n. 5, p. 1211-1217, 2012.0005-2736http://repositorio.unifesp.br/handle/11600/34810http://dx.doi.org/10.1016/j.bbamem.2012.01.012WOS000302971100011.pdf10.1016/j.bbamem.2012.01.012WOS:000302971100011Investigating the role of proteoglycans associated to cell membranes is fundamental to comprehend biochemical process that occurs at the level of membrane surfaces. in this paper, we exploit syndecan-4, a heparan sulfate proteoglycan obtained from cell cultures, in lipid Langmuir monolayers at the air-water interface. the monolayer served as a model for half a membrane, and the molecular interactions involved could be evaluated with tensiometry and vibrational spectroscopy techniques. Polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS) employed in a constant surface pressure regime showed that the main chemical groups for syndecan-4 were present at the air-water interface. Subsequent monolayer decompression and compression showed surface pressure-area isotherms with a large expansion for the lipid monolayers interacting with the cell culture reported to over-express syndecan-4, which was also an indication that the proteoglycan was inserted in the lipid monolayer. the introduction of biological molecules with affinity for syndecam-4, such as growth factors, which present a key role in biochemical process of cell signaling, changed the surface properties of the hybrid film, leading to a model, by which the growth factor binds to the sulfate groups present in the heparan sulfate chains. the polypeptide moiety of syndecan-4 responds to this interaction changing its conformation, which leads to lipid film relaxation and further monolayer condensation. (C) 2012 Elsevier B.V. All rights reserved.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Universidade Federal de São Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, São Paulo, SP, BrazilUniversidade Federal de São Paulo, Inst Ciencias Ambientais Quim & Farmaceut, Diadema, SP, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, São Paulo, SP, BrazilWeb of Science1211-1217engElsevier B.V.Biochimica Et Biophysica Acta-biomembraneshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyinfo:eu-repo/semantics/openAccessHeparan sulfate proteoglycanSyndecan-4Molecular recognizingLangmuir monolayerProbing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film studyinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlereponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000302971100011.pdfapplication/pdf1070186${dspace.ui.url}/bitstream/11600/34810/1/WOS000302971100011.pdfac0964e535834f233c962744017c9a13MD51open accessTEXTWOS000302971100011.pdf.txtWOS000302971100011.pdf.txtExtracted texttext/plain42392${dspace.ui.url}/bitstream/11600/34810/9/WOS000302971100011.pdf.txt5aee41aa8e2cfde798a49ef6bb32ce96MD59open accessTHUMBNAILWOS000302971100011.pdf.jpgWOS000302971100011.pdf.jpgIM Thumbnailimage/jpeg7819${dspace.ui.url}/bitstream/11600/34810/11/WOS000302971100011.pdf.jpga13f18e608e97a4e1c46b0f3ff626f95MD511open access11600/348102023-06-05 19:26:24.182open accessoai:repositorio.unifesp.br:11600/34810Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-06-05T22:26:24Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.en.fl_str_mv Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
title Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
spellingShingle Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
Caseli, Luciano [UNIFESP]
Heparan sulfate proteoglycan
Syndecan-4
Molecular recognizing
Langmuir monolayer
title_short Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
title_full Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
title_fullStr Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
title_full_unstemmed Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
title_sort Probing the interaction between heparan sulfate proteoglycan with biologically relevant molecules in mimetic models for cell membranes: A Langmuir film study
author Caseli, Luciano [UNIFESP]
author_facet Caseli, Luciano [UNIFESP]
Cavalheiro, Renan Pelluzzi [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Lopes, Carla Cristina [UNIFESP]
author_role author
author2 Cavalheiro, Renan Pelluzzi [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Lopes, Carla Cristina [UNIFESP]
author2_role author
author
author
dc.contributor.institution.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
dc.contributor.author.fl_str_mv Caseli, Luciano [UNIFESP]
Cavalheiro, Renan Pelluzzi [UNIFESP]
Nader, Helena Bonciani [UNIFESP]
Lopes, Carla Cristina [UNIFESP]
dc.subject.eng.fl_str_mv Heparan sulfate proteoglycan
Syndecan-4
Molecular recognizing
Langmuir monolayer
topic Heparan sulfate proteoglycan
Syndecan-4
Molecular recognizing
Langmuir monolayer
description Investigating the role of proteoglycans associated to cell membranes is fundamental to comprehend biochemical process that occurs at the level of membrane surfaces. in this paper, we exploit syndecan-4, a heparan sulfate proteoglycan obtained from cell cultures, in lipid Langmuir monolayers at the air-water interface. the monolayer served as a model for half a membrane, and the molecular interactions involved could be evaluated with tensiometry and vibrational spectroscopy techniques. Polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS) employed in a constant surface pressure regime showed that the main chemical groups for syndecan-4 were present at the air-water interface. Subsequent monolayer decompression and compression showed surface pressure-area isotherms with a large expansion for the lipid monolayers interacting with the cell culture reported to over-express syndecan-4, which was also an indication that the proteoglycan was inserted in the lipid monolayer. the introduction of biological molecules with affinity for syndecam-4, such as growth factors, which present a key role in biochemical process of cell signaling, changed the surface properties of the hybrid film, leading to a model, by which the growth factor binds to the sulfate groups present in the heparan sulfate chains. the polypeptide moiety of syndecan-4 responds to this interaction changing its conformation, which leads to lipid film relaxation and further monolayer condensation. (C) 2012 Elsevier B.V. All rights reserved.
publishDate 2012
dc.date.issued.fl_str_mv 2012-05-01
dc.date.accessioned.fl_str_mv 2016-01-24T14:27:08Z
dc.date.available.fl_str_mv 2016-01-24T14:27:08Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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status_str publishedVersion
dc.identifier.citation.fl_str_mv Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1818, n. 5, p. 1211-1217, 2012.
dc.identifier.uri.fl_str_mv http://repositorio.unifesp.br/handle/11600/34810
http://dx.doi.org/10.1016/j.bbamem.2012.01.012
dc.identifier.issn.none.fl_str_mv 0005-2736
dc.identifier.file.none.fl_str_mv WOS000302971100011.pdf
dc.identifier.doi.none.fl_str_mv 10.1016/j.bbamem.2012.01.012
dc.identifier.wos.none.fl_str_mv WOS:000302971100011
identifier_str_mv Biochimica Et Biophysica Acta-biomembranes. Amsterdam: Elsevier B.V., v. 1818, n. 5, p. 1211-1217, 2012.
0005-2736
WOS000302971100011.pdf
10.1016/j.bbamem.2012.01.012
WOS:000302971100011
url http://repositorio.unifesp.br/handle/11600/34810
http://dx.doi.org/10.1016/j.bbamem.2012.01.012
dc.language.iso.fl_str_mv eng
language eng
dc.relation.ispartof.none.fl_str_mv Biochimica Et Biophysica Acta-biomembranes
dc.rights.driver.fl_str_mv http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
info:eu-repo/semantics/openAccess
rights_invalid_str_mv http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 1211-1217
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
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