Molecular Characterization of the Glycated Plasma Membrane Calcium Pump

We have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell Ca2+ pump diminishes the Ca2+-ATPase activity of the enzyme up to 50%. Such effect is due to the reaction of glucose with lysine residues of the Ca2+ pump (Biochem. J. 293:369–375, 1993). The aim of t...

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Detalles Bibliográficos
Autores: González Flecha, F. L., Castello, Pablo R., Gagliardino, Juan José, Rossi, Juan Pablo F. C.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:1999
País:Argentina
Institución:Universidad Nacional de La Plata
Repositorio:SEDICI (UNLP)
Idioma:inglés
OAI Identifier:oai:sedici.unlp.edu.ar:10915/131051
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/131051
Access Level:acceso abierto
Palabra clave:Ciencias Naturales
Biología
PMCA
Glycation
Phosphatase
Lys residues
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spelling Molecular Characterization of the Glycated Plasma Membrane Calcium PumpGonzález Flecha, F. L.Castello, Pablo R.Gagliardino, Juan JoséRossi, Juan Pablo F. C.Ciencias NaturalesBiologíaPMCAGlycationPhosphataseLys residuesWe have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell Ca2+ pump diminishes the Ca2+-ATPase activity of the enzyme up to 50%. Such effect is due to the reaction of glucose with lysine residues of the Ca2+ pump (Biochem. J. 293:369–375, 1993). The aim of this work was to determine whether the effect of glucose is due to a full inactivation of a fraction of the total population of Ca2+ pump, or to a partial inactivation of all the molecules. Glycation decreased the Vmax; for the ATPase activity leaving unaffected the apparent affinities for Ca2+, calmodulin or ATP. The apparent turnover was identical in both, the glycated and the native enzyme. Glycation decreased the Vmax; for the ATP-dependent but not for the calmodulin-activated phosphatase activities. Concomitantly with the inhibition, up to 6.5% of the lysine residues were randomly glycated. The probabilistic analysis of the relation between the enzyme activity and the fraction of nonmodified residues indicates that only one Lys residue is responsible for the inhibition. We suggest that glucose decreases the Ca2+-ATPase activity by reacting with one essential Lys residue probably located in the vicinity of the catalytic site, which results in the full inactivation of the enzyme. Thus, Ca2+-ATPase activity measured in erythrocyte membranes or purified enzyme preparations preincubated with glucose depends on the remaining enzyme molecules in which the essential Lys residue stays unglycated.Centro de Endocrinología Experimental y Aplicada1999-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf25-34http://sedici.unlp.edu.ar/handle/10915/131051enginfo:eu-repo/semantics/altIdentifier/issn/0022-2631info:eu-repo/semantics/altIdentifier/issn/1432-1424info:eu-repo/semantics/altIdentifier/doi/10.1007/s002329900555info:eu-repo/semantics/altIdentifier/pmid/10485991info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2024-05-08T13:11:04Zoai:sedici.unlp.edu.ar:10915/131051Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292024-05-08 13:11:04.385SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
title Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
spellingShingle Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
González Flecha, F. L.
Ciencias Naturales
Biología
PMCA
Glycation
Phosphatase
Lys residues
title_short Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
title_full Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
title_fullStr Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
title_full_unstemmed Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
title_sort Molecular Characterization of the Glycated Plasma Membrane Calcium Pump
dc.creator.none.fl_str_mv González Flecha, F. L.
Castello, Pablo R.
Gagliardino, Juan José
Rossi, Juan Pablo F. C.
author González Flecha, F. L.
author_facet González Flecha, F. L.
Castello, Pablo R.
Gagliardino, Juan José
Rossi, Juan Pablo F. C.
author_role author
author2 Castello, Pablo R.
Gagliardino, Juan José
Rossi, Juan Pablo F. C.
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Naturales
Biología
PMCA
Glycation
Phosphatase
Lys residues
topic Ciencias Naturales
Biología
PMCA
Glycation
Phosphatase
Lys residues
description We have previously demonstrated (Diabetes 39:707–711, 1990) that in vitro glycation of the red cell Ca2+ pump diminishes the Ca2+-ATPase activity of the enzyme up to 50%. Such effect is due to the reaction of glucose with lysine residues of the Ca2+ pump (Biochem. J. 293:369–375, 1993). The aim of this work was to determine whether the effect of glucose is due to a full inactivation of a fraction of the total population of Ca2+ pump, or to a partial inactivation of all the molecules. Glycation decreased the Vmax; for the ATPase activity leaving unaffected the apparent affinities for Ca2+, calmodulin or ATP. The apparent turnover was identical in both, the glycated and the native enzyme. Glycation decreased the Vmax; for the ATP-dependent but not for the calmodulin-activated phosphatase activities. Concomitantly with the inhibition, up to 6.5% of the lysine residues were randomly glycated. The probabilistic analysis of the relation between the enzyme activity and the fraction of nonmodified residues indicates that only one Lys residue is responsible for the inhibition. We suggest that glucose decreases the Ca2+-ATPase activity by reacting with one essential Lys residue probably located in the vicinity of the catalytic site, which results in the full inactivation of the enzyme. Thus, Ca2+-ATPase activity measured in erythrocyte membranes or purified enzyme preparations preincubated with glucose depends on the remaining enzyme molecules in which the essential Lys residue stays unglycated.
publishDate 1999
dc.date.none.fl_str_mv 1999-09-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/131051
url http://sedici.unlp.edu.ar/handle/10915/131051
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/issn/1432-1424
info:eu-repo/semantics/altIdentifier/doi/10.1007/s002329900555
info:eu-repo/semantics/altIdentifier/pmid/10485991
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
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reponame_str SEDICI (UNLP)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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