High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women

Autores
Zago, Valeria; Miksztowicz, Verónica Julieta; Cacciagiú, Leonardo D.; Basilio, Francisco; Berg, Gabriela Alicia; Schreier, Laura Ester
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background HDL antiatherogenic effects would not only depend on its concentration but also on its biological quality. Hepatic lipase (HL) action on HDL acts in one of the last steps of reverse cholesterol transport. Cardiovascular risk increases after menopause, however HDL does not decrease even when HL is increased. We evaluated HDL capacity as a substrate of HL in healthy postmenopausal women (PMW). Methods We studied 20 PMW (51–60 y) and 20 premenopausal (PreMW) (26–40 y). In fasting serum, lipid–lipoprotein profile and HDL composition were assessed. Optimal assay conditions for HDL/HL ex vivo incubation were established. Increasing HDL–triglyceride concentrations (0.015 to 0.20 mmol/l) were incubated with post-heparin plasma obtained from a single healthy donor as a source of HL. Free fatty acids were measured and kinetic parameters calculated: Km(app), inverse to enzyme affinity, and Vmax. Results HDL composition in PMW exhibits triglyceride enrichment (p < 0.001). Kinetic analysis revealed higher Km(app) in PMW [130 (40–380) vs 45 (20–91) mmol/l, p < 0.0001)] correlating directly with HDL–triglycerides (r = 0.7, p = 0.0001). Catalytic efficiency, Vmax/Km(app) was reduced when compared to controls (p = 0.0001). Conclusion Triglyceride-enriched HDL from PMW constitutes a poor substrate for HL suggesting that this particle may not exert efficiently its antiatherogenic function, regardless of plasma concentration.
Fil: Zago, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Miksztowicz, Verónica Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Cacciagiú, Leonardo D.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Basilio, Francisco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Berg, Gabriela Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Schreier, Laura Ester. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Materia
Hdl Functionality
Hepatic Lipase
High Density Lipoprotein
Kinetics
Postmenopause
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:11336/67266
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/67266
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal womenZago, ValeriaMiksztowicz, Verónica JulietaCacciagiú, Leonardo D.Basilio, FranciscoBerg, Gabriela AliciaSchreier, Laura EsterHdl FunctionalityHepatic LipaseHigh Density LipoproteinKineticsPostmenopausehttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Background HDL antiatherogenic effects would not only depend on its concentration but also on its biological quality. Hepatic lipase (HL) action on HDL acts in one of the last steps of reverse cholesterol transport. Cardiovascular risk increases after menopause, however HDL does not decrease even when HL is increased. We evaluated HDL capacity as a substrate of HL in healthy postmenopausal women (PMW). Methods We studied 20 PMW (51–60 y) and 20 premenopausal (PreMW) (26–40 y). In fasting serum, lipid–lipoprotein profile and HDL composition were assessed. Optimal assay conditions for HDL/HL ex vivo incubation were established. Increasing HDL–triglyceride concentrations (0.015 to 0.20 mmol/l) were incubated with post-heparin plasma obtained from a single healthy donor as a source of HL. Free fatty acids were measured and kinetic parameters calculated: Km(app), inverse to enzyme affinity, and Vmax. Results HDL composition in PMW exhibits triglyceride enrichment (p < 0.001). Kinetic analysis revealed higher Km(app) in PMW [130 (40–380) vs 45 (20–91) mmol/l, p < 0.0001)] correlating directly with HDL–triglycerides (r = 0.7, p = 0.0001). Catalytic efficiency, Vmax/Km(app) was reduced when compared to controls (p = 0.0001). Conclusion Triglyceride-enriched HDL from PMW constitutes a poor substrate for HL suggesting that this particle may not exert efficiently its antiatherogenic function, regardless of plasma concentration.Fil: Zago, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaFil: Miksztowicz, Verónica Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaFil: Cacciagiú, Leonardo D.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaFil: Basilio, Francisco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaFil: Berg, Gabriela Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaFil: Schreier, Laura Ester. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; ArgentinaElsevier Science2012-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/67266Zago, Valeria; Miksztowicz, Verónica Julieta; Cacciagiú, Leonardo D.; Basilio, Francisco; Berg, Gabriela Alicia; et al.; High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women; Elsevier Science; Clinica Chimica Acta; 414; 9-2012; 142-1450009-8981CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.cca.2012.08.026info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0009898112004317info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:37Zoai:ri.conicet.gov.ar:11336/67266instacron: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:34982025-09-03 10:08:38.122CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
title High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
spellingShingle High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
Zago, Valeria
Hdl Functionality
Hepatic Lipase
High Density Lipoprotein
Kinetics
Postmenopause
title_short High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
title_full High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
title_fullStr High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
title_full_unstemmed High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
title_sort High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women
dc.creator.none.fl_str_mv Zago, Valeria
Miksztowicz, Verónica Julieta
Cacciagiú, Leonardo D.
Basilio, Francisco
Berg, Gabriela Alicia
Schreier, Laura Ester
author Zago, Valeria
author_facet Zago, Valeria
Miksztowicz, Verónica Julieta
Cacciagiú, Leonardo D.
Basilio, Francisco
Berg, Gabriela Alicia
Schreier, Laura Ester
author_role author
author2 Miksztowicz, Verónica Julieta
Cacciagiú, Leonardo D.
Basilio, Francisco
Berg, Gabriela Alicia
Schreier, Laura Ester
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Hdl Functionality
Hepatic Lipase
High Density Lipoprotein
Kinetics
Postmenopause
topic Hdl Functionality
Hepatic Lipase
High Density Lipoprotein
Kinetics
Postmenopause
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Background HDL antiatherogenic effects would not only depend on its concentration but also on its biological quality. Hepatic lipase (HL) action on HDL acts in one of the last steps of reverse cholesterol transport. Cardiovascular risk increases after menopause, however HDL does not decrease even when HL is increased. We evaluated HDL capacity as a substrate of HL in healthy postmenopausal women (PMW). Methods We studied 20 PMW (51–60 y) and 20 premenopausal (PreMW) (26–40 y). In fasting serum, lipid–lipoprotein profile and HDL composition were assessed. Optimal assay conditions for HDL/HL ex vivo incubation were established. Increasing HDL–triglyceride concentrations (0.015 to 0.20 mmol/l) were incubated with post-heparin plasma obtained from a single healthy donor as a source of HL. Free fatty acids were measured and kinetic parameters calculated: Km(app), inverse to enzyme affinity, and Vmax. Results HDL composition in PMW exhibits triglyceride enrichment (p < 0.001). Kinetic analysis revealed higher Km(app) in PMW [130 (40–380) vs 45 (20–91) mmol/l, p < 0.0001)] correlating directly with HDL–triglycerides (r = 0.7, p = 0.0001). Catalytic efficiency, Vmax/Km(app) was reduced when compared to controls (p = 0.0001). Conclusion Triglyceride-enriched HDL from PMW constitutes a poor substrate for HL suggesting that this particle may not exert efficiently its antiatherogenic function, regardless of plasma concentration.
Fil: Zago, Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Miksztowicz, Verónica Julieta. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Cacciagiú, Leonardo D.. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Basilio, Francisco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Berg, Gabriela Alicia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
Fil: Schreier, Laura Ester. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Departamento de Bioquímica Clínica; Argentina
description Background HDL antiatherogenic effects would not only depend on its concentration but also on its biological quality. Hepatic lipase (HL) action on HDL acts in one of the last steps of reverse cholesterol transport. Cardiovascular risk increases after menopause, however HDL does not decrease even when HL is increased. We evaluated HDL capacity as a substrate of HL in healthy postmenopausal women (PMW). Methods We studied 20 PMW (51–60 y) and 20 premenopausal (PreMW) (26–40 y). In fasting serum, lipid–lipoprotein profile and HDL composition were assessed. Optimal assay conditions for HDL/HL ex vivo incubation were established. Increasing HDL–triglyceride concentrations (0.015 to 0.20 mmol/l) were incubated with post-heparin plasma obtained from a single healthy donor as a source of HL. Free fatty acids were measured and kinetic parameters calculated: Km(app), inverse to enzyme affinity, and Vmax. Results HDL composition in PMW exhibits triglyceride enrichment (p < 0.001). Kinetic analysis revealed higher Km(app) in PMW [130 (40–380) vs 45 (20–91) mmol/l, p < 0.0001)] correlating directly with HDL–triglycerides (r = 0.7, p = 0.0001). Catalytic efficiency, Vmax/Km(app) was reduced when compared to controls (p = 0.0001). Conclusion Triglyceride-enriched HDL from PMW constitutes a poor substrate for HL suggesting that this particle may not exert efficiently its antiatherogenic function, regardless of plasma concentration.
publishDate 2012
dc.date.none.fl_str_mv 2012-09
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/67266
Zago, Valeria; Miksztowicz, Verónica Julieta; Cacciagiú, Leonardo D.; Basilio, Francisco; Berg, Gabriela Alicia; et al.; High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women; Elsevier Science; Clinica Chimica Acta; 414; 9-2012; 142-145
0009-8981
CONICET Digital
CONICET
url http://hdl.handle.net/11336/67266
identifier_str_mv Zago, Valeria; Miksztowicz, Verónica Julieta; Cacciagiú, Leonardo D.; Basilio, Francisco; Berg, Gabriela Alicia; et al.; High density lipoprotein is an inappropiate substrate for hepatic lipase in postmenopausal women; Elsevier Science; Clinica Chimica Acta; 414; 9-2012; 142-145
0009-8981
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cca.2012.08.026
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0009898112004317
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
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.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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