Crowding modulates the glycation of plasma proteins: In vitro analysis of structural modifications to albumin and transferrin and identification of sites of modification

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dc.catalogadorgjm
dc.contributor.authorFuentes Lemus, Eduardo Felipe
dc.contributor.authorReyes Valenzuela, Juan Sebastián
dc.contributor.authorLópez Alarcón, Camilo Ignacio
dc.contributor.authorDavies, Michael J.
dc.date.accessioned2024-12-30T16:02:13Z
dc.date.available2024-12-30T16:02:13Z
dc.date.issued2022
dc.description.abstractProtein modification occurs in biological milieus that are characterized by high concentrations of (macro)mol-ecules (i.e. heterogeneous and packed environments). Recent data indicate that crowding can modulate the extent and rate of protein oxidation, however its effect on other post-translational modifications remains to be explored. In this work we hypothesized that crowding would affect the glycation of plasma proteins. Physiologically-relevant concentrations of albumin (35 mg mL-1) and transferrin (2 mg mL-1) were incubated with methylglyoxal and glyoxal (5 mu M-5 mM), two alpha-oxoaldehyde metabolites that are elevated in the plasma of people with diabetes. Crowding was induced by adding dextran or ficoll polymers. Electrophoresis, electron microscopy, fluorescence spectroscopy and mass spectrometry were employed to investigate the structural consequences of glycation under crowded conditions. Our data demonstrate that crowding modulates the extent of formation of transferrin cross-links, and also the modification pathways in both albumin and transferrin. Arginine was the most susceptible residue to modification, with lysine and cysteine also affected. Loss of 0.48 and 7.28 arginine residues per protein molecule were determined on incubation with 500 mu M methylglyoxal for albumin and transferrin, respectively. Crowding did not influence the extent of loss of arginine and lysine for either protein, but the sites of modification, detected by LC-MS, were different between dilute and crowded conditions. These data confirm the relevance of studying modification processes under conditions that closely mimic biological milieus. These data unveil additional factors that influence the pattern and extent of protein modification, and their structural consequences, in biological systems.
dc.format.extent16 páginas
dc.fuente.origenWOS
dc.identifier.doi10.1016/j.freeradbiomed.2022.10.319
dc.identifier.eissn1873-4596
dc.identifier.issn0891-5849
dc.identifier.urihttps://doi.org/10.1016/j.freeradbiomed.2022.10.319
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/89372
dc.identifier.wosidWOS:000896919100003
dc.information.autorucEscuela de Química; Fuentes Lemus, Eduardo Felipe; 0000-0002-1465-8466; 186720
dc.information.autorucEscuela de Química; Reyes Valenzuela, Juan Sebastián; S/I; 1268701
dc.information.autorucEscuela de Química; López Alarcón, Camilo Ignacio; S/I; 1004308
dc.issue.numeroPart 2
dc.language.isoen
dc.nota.accesosin adjunto
dc.pagina.final566
dc.pagina.inicio551
dc.revistaFree Radical Biology and Medicine
dc.rightsacceso abierto
dc.rights.licenseCC BY 4.0 Attribution 4.0 International Deed
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectProtein glycation
dc.subjectCrowding
dc.subjectAdvanced glycation products
dc.subjectAlbumin
dc.subjectTransferrin
dc.subjectMethylglyoxal
dc.subjectGlyoxal
dc.subject.ddc510
dc.subject.deweyMatemática física y químicaes_ES
dc.subject.ods03 Good health and well-being
dc.subject.odspa03 Salud y bienestar
dc.titleCrowding modulates the glycation of plasma proteins: In vitro analysis of structural modifications to albumin and transferrin and identification of sites of modification
dc.typeartículo
dc.volumen193
sipa.codpersvinculados186720
sipa.codpersvinculados1268701
sipa.codpersvinculados1004308
sipa.trazabilidadWOS;2023-01-17
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