Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape

Autores
Díaz Ludovico, Ivo; Garda, Horacio Alberto; Gonzalez, Marina Cecilia
Año de publicación
2018
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Human apolipoprotein A-I (ApoA-I) is the major protein component of high density lipoproteins (HDL) playing a pivotal role in reverse cholesterol transport. A natural mutant of ApoA-I having a deletion of the single residue Lys107 (K) induces severe atherosclerosis. The structural and functional effects due mutation are studied to elucidate the pro-atherogenicity of this protein. In this study we investigate the structural effects of K107 deletion in a comparative approach with wild type (W) protein. Attending to structural alterations caused by deletion we have crosslinked with BS3 the lysine residues of both proteins in the native monomeric state (KBS3 and WBS3). Tryptophan fluorescence is red shifted in the deletion mutant (K or KBS3) compared with the wild type protein (W or WBS3) but it is not affected by crosslinking. The micellization of multilamellar DMPC liposomes (145:1 molar ratio) was evaluated with crosslinked (WBS3 and KBS3) and un-crosslinked proteins. The rate of the micellization process was decreased by the crosslinking although the efficiency of the process at final point was not affected. The size of HDL complexes formed by DMPC micellization were determined by polyacrylamide native electrophoresis and shape was visualized by TEM. Crosslinked proteins do not form the small sized populations of lipoprotein complexes observed with uncrosslinked proteins. TEM observation indicates that generation of discoidal complexes is decreased by crosslinking of the wild type protein but is less affected in the case of the deletion mutant. Thus, we can conclude that the ability to generate discoidal HDL complexes is reduced exclusively by crosslinking of lysine 107.
Fil: Díaz Ludovico, Ivo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Garda, Horacio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Gonzalez, Marina Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
XLVII Reunión Anual de la Sociedad Argentina de Biofísica
La Plata
Argentina
Sociedad Argentina de Biofísica
Materia
APOLIPOPROTEIN-AI
DELETION MUTANT
CROSSLINKING
HIGH DENSITY LIPOPROTEINS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/278024
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/278024
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shapeDíaz Ludovico, IvoGarda, Horacio AlbertoGonzalez, Marina CeciliaAPOLIPOPROTEIN-AIDELETION MUTANTCROSSLINKINGHIGH DENSITY LIPOPROTEINShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Human apolipoprotein A-I (ApoA-I) is the major protein component of high density lipoproteins (HDL) playing a pivotal role in reverse cholesterol transport. A natural mutant of ApoA-I having a deletion of the single residue Lys107 (K) induces severe atherosclerosis. The structural and functional effects due mutation are studied to elucidate the pro-atherogenicity of this protein. In this study we investigate the structural effects of K107 deletion in a comparative approach with wild type (W) protein. Attending to structural alterations caused by deletion we have crosslinked with BS3 the lysine residues of both proteins in the native monomeric state (KBS3 and WBS3). Tryptophan fluorescence is red shifted in the deletion mutant (K or KBS3) compared with the wild type protein (W or WBS3) but it is not affected by crosslinking. The micellization of multilamellar DMPC liposomes (145:1 molar ratio) was evaluated with crosslinked (WBS3 and KBS3) and un-crosslinked proteins. The rate of the micellization process was decreased by the crosslinking although the efficiency of the process at final point was not affected. The size of HDL complexes formed by DMPC micellization were determined by polyacrylamide native electrophoresis and shape was visualized by TEM. Crosslinked proteins do not form the small sized populations of lipoprotein complexes observed with uncrosslinked proteins. TEM observation indicates that generation of discoidal complexes is decreased by crosslinking of the wild type protein but is less affected in the case of the deletion mutant. Thus, we can conclude that the ability to generate discoidal HDL complexes is reduced exclusively by crosslinking of lysine 107.Fil: Díaz Ludovico, Ivo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Garda, Horacio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Gonzalez, Marina Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaXLVII Reunión Anual de la Sociedad Argentina de BiofísicaLa PlataArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/278024Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 122-122978-987-27591-6-2CONICET DigitalCONICETengNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-23T13:51:08Zoai:ri.conicet.gov.ar:11336/278024instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-12-23 13:51:08.539CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
title Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
spellingShingle Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
Díaz Ludovico, Ivo
APOLIPOPROTEIN-AI
DELETION MUTANT
CROSSLINKING
HIGH DENSITY LIPOPROTEINS
title_short Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
title_full Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
title_fullStr Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
title_full_unstemmed Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
title_sort Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape
dc.creator.none.fl_str_mv Díaz Ludovico, Ivo
Garda, Horacio Alberto
Gonzalez, Marina Cecilia
author Díaz Ludovico, Ivo
author_facet Díaz Ludovico, Ivo
Garda, Horacio Alberto
Gonzalez, Marina Cecilia
author_role author
author2 Garda, Horacio Alberto
Gonzalez, Marina Cecilia
author2_role author
author
dc.subject.none.fl_str_mv APOLIPOPROTEIN-AI
DELETION MUTANT
CROSSLINKING
HIGH DENSITY LIPOPROTEINS
topic APOLIPOPROTEIN-AI
DELETION MUTANT
CROSSLINKING
HIGH DENSITY LIPOPROTEINS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Human apolipoprotein A-I (ApoA-I) is the major protein component of high density lipoproteins (HDL) playing a pivotal role in reverse cholesterol transport. A natural mutant of ApoA-I having a deletion of the single residue Lys107 (K) induces severe atherosclerosis. The structural and functional effects due mutation are studied to elucidate the pro-atherogenicity of this protein. In this study we investigate the structural effects of K107 deletion in a comparative approach with wild type (W) protein. Attending to structural alterations caused by deletion we have crosslinked with BS3 the lysine residues of both proteins in the native monomeric state (KBS3 and WBS3). Tryptophan fluorescence is red shifted in the deletion mutant (K or KBS3) compared with the wild type protein (W or WBS3) but it is not affected by crosslinking. The micellization of multilamellar DMPC liposomes (145:1 molar ratio) was evaluated with crosslinked (WBS3 and KBS3) and un-crosslinked proteins. The rate of the micellization process was decreased by the crosslinking although the efficiency of the process at final point was not affected. The size of HDL complexes formed by DMPC micellization were determined by polyacrylamide native electrophoresis and shape was visualized by TEM. Crosslinked proteins do not form the small sized populations of lipoprotein complexes observed with uncrosslinked proteins. TEM observation indicates that generation of discoidal complexes is decreased by crosslinking of the wild type protein but is less affected in the case of the deletion mutant. Thus, we can conclude that the ability to generate discoidal HDL complexes is reduced exclusively by crosslinking of lysine 107.
Fil: Díaz Ludovico, Ivo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Garda, Horacio Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Gonzalez, Marina Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
XLVII Reunión Anual de la Sociedad Argentina de Biofísica
La Plata
Argentina
Sociedad Argentina de Biofísica
description Human apolipoprotein A-I (ApoA-I) is the major protein component of high density lipoproteins (HDL) playing a pivotal role in reverse cholesterol transport. A natural mutant of ApoA-I having a deletion of the single residue Lys107 (K) induces severe atherosclerosis. The structural and functional effects due mutation are studied to elucidate the pro-atherogenicity of this protein. In this study we investigate the structural effects of K107 deletion in a comparative approach with wild type (W) protein. Attending to structural alterations caused by deletion we have crosslinked with BS3 the lysine residues of both proteins in the native monomeric state (KBS3 and WBS3). Tryptophan fluorescence is red shifted in the deletion mutant (K or KBS3) compared with the wild type protein (W or WBS3) but it is not affected by crosslinking. The micellization of multilamellar DMPC liposomes (145:1 molar ratio) was evaluated with crosslinked (WBS3 and KBS3) and un-crosslinked proteins. The rate of the micellization process was decreased by the crosslinking although the efficiency of the process at final point was not affected. The size of HDL complexes formed by DMPC micellization were determined by polyacrylamide native electrophoresis and shape was visualized by TEM. Crosslinked proteins do not form the small sized populations of lipoprotein complexes observed with uncrosslinked proteins. TEM observation indicates that generation of discoidal complexes is decreased by crosslinking of the wild type protein but is less affected in the case of the deletion mutant. Thus, we can conclude that the ability to generate discoidal HDL complexes is reduced exclusively by crosslinking of lysine 107.
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/278024
Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 122-122
978-987-27591-6-2
CONICET Digital
CONICET
url http://hdl.handle.net/11336/278024
identifier_str_mv Crosslinked domains of apoA-I but not of ΔK107, are involved in rHDL´s shape; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 122-122
978-987-27591-6-2
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad Argentina de Biofísica
publisher.none.fl_str_mv Sociedad Argentina de Biofísica
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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