Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages

Research output: Contribution to journal › Journal article › peer-review

Standard

Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages. / Brown, Bronwyn E; Nobecourt, Estelle; Zeng, Jingmin; Jenkins, Alicia J; Rye, Kerry-Anne; Davies, Michael Jonathan.

In: PLOS ONE, Vol. 8, No. 5, 2013, p. e65430.

Research output: Contribution to journal › Journal article › peer-review

Harvard

Brown, BE, Nobecourt, E, Zeng, J, Jenkins, AJ, Rye, K-A & Davies, MJ 2013, 'Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages', PLOS ONE, vol. 8, no. 5, pp. e65430. https://doi.org/10.1371/journal.pone.0065430

APA

Brown, B. E., Nobecourt, E., Zeng, J., Jenkins, A. J., Rye, K-A., & Davies, M. J. (2013). Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages. PLOS ONE, 8(5), e65430. https://doi.org/10.1371/journal.pone.0065430

Vancouver

Brown BE, Nobecourt E, Zeng J, Jenkins AJ, Rye K-A, Davies MJ. Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages. PLOS ONE. 2013;8(5):e65430. https://doi.org/10.1371/journal.pone.0065430

Author

Brown, Bronwyn E ; Nobecourt, Estelle ; Zeng, Jingmin ; Jenkins, Alicia J ; Rye, Kerry-Anne ; Davies, Michael Jonathan. / Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages. In: PLOS ONE. 2013 ; Vol. 8, No. 5. pp. e65430.

Bibtex

@article{a8c97f7a833447a1a43c9d345a87d09f,
title = "Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages",
abstract = "Increased protein glycation in people with diabetes may promote atherosclerosis. This study examined the effects of non-enzymatic glycation on the association of lipid-free apolipoproteinA-I (apoA-I) with phospholipid, and cholesterol efflux from lipid-loaded macrophages to lipid-free and lipid-associated apoA-I. Glycation of lipid-free apoA-I by methylglyoxal and glycolaldehyde resulted in Arg, Lys and Trp loss, advanced glycation end-product formation and protein cross-linking. The association of apoA-I glycated by glucose, methylglyoxal or glycolaldehyde with phospholipid multilamellar vesicles was impaired in a glycating agent dose-dependent manner, with exposure of apoA-I to both 30 mM glucose (42% decrease in kslow) and 3 mM glycolaldehyde (50% decrease in kfast, 60% decrease in kslow) resulting is significantly reduced affinity. Cholesterol efflux to control or glycated lipid-free apoA-I, or discoidal reconstituted HDL containing glycated apoA-I (drHDL), was examined using cholesterol-loaded murine (J774A.1) macrophages treated to increase expression of ATP binding cassette transporters A1 (ABCA1) or G1 (ABCG1). Cholesterol efflux from J774A.1 macrophages to glycated lipid-free apoA-I via ABCA1 or glycated drHDL via an ABCG1-dependent mechanism was unaltered, as was efflux to minimally modified apoA-I from people with Type 1 diabetes, or controls. Changes to protein structure and function were prevented by the reactive carbonyl scavenger aminoguanidine. Overall these studies demonstrate that glycation of lipid-free apoA-I, particularly late glycation, modifies its structure, its capacity to bind phospholipids and but not ABCA1- or ABCG1-dependent cholesterol efflux from macrophages.",
keywords = "ATP-Binding Cassette Transporters, Adult, Aldehydes, Animals, Apolipoprotein A-I, Biological Transport, Case-Control Studies, Cell Line, Cholesterol, Diabetes Mellitus, Type 1, Female, Glucose, Glycosylation, Humans, Lipid Metabolism, Lipoproteins, HDL, Macrophages, Male, Mice, Phospholipids, Young Adult",
author = "Brown, {Bronwyn E} and Estelle Nobecourt and Jingmin Zeng and Jenkins, {Alicia J} and Kerry-Anne Rye and Davies, {Michael Jonathan}",
year = "2013",
doi = "10.1371/journal.pone.0065430",
language = "English",
volume = "8",
pages = "e65430",
journal = "PLoS ONE",
issn = "1932-6203",
publisher = "Public Library of Science",
number = "5",

}

RIS

TY - JOUR

T1 - Apolipoprotein A-I glycation by glucose and reactive aldehydes alters phospholipid affinity but not cholesterol export from lipid-laden macrophages

AU - Brown, Bronwyn E

AU - Nobecourt, Estelle

AU - Zeng, Jingmin

AU - Jenkins, Alicia J

AU - Rye, Kerry-Anne

AU - Davies, Michael Jonathan

PY - 2013

Y1 - 2013

N2 - Increased protein glycation in people with diabetes may promote atherosclerosis. This study examined the effects of non-enzymatic glycation on the association of lipid-free apolipoproteinA-I (apoA-I) with phospholipid, and cholesterol efflux from lipid-loaded macrophages to lipid-free and lipid-associated apoA-I. Glycation of lipid-free apoA-I by methylglyoxal and glycolaldehyde resulted in Arg, Lys and Trp loss, advanced glycation end-product formation and protein cross-linking. The association of apoA-I glycated by glucose, methylglyoxal or glycolaldehyde with phospholipid multilamellar vesicles was impaired in a glycating agent dose-dependent manner, with exposure of apoA-I to both 30 mM glucose (42% decrease in kslow) and 3 mM glycolaldehyde (50% decrease in kfast, 60% decrease in kslow) resulting is significantly reduced affinity. Cholesterol efflux to control or glycated lipid-free apoA-I, or discoidal reconstituted HDL containing glycated apoA-I (drHDL), was examined using cholesterol-loaded murine (J774A.1) macrophages treated to increase expression of ATP binding cassette transporters A1 (ABCA1) or G1 (ABCG1). Cholesterol efflux from J774A.1 macrophages to glycated lipid-free apoA-I via ABCA1 or glycated drHDL via an ABCG1-dependent mechanism was unaltered, as was efflux to minimally modified apoA-I from people with Type 1 diabetes, or controls. Changes to protein structure and function were prevented by the reactive carbonyl scavenger aminoguanidine. Overall these studies demonstrate that glycation of lipid-free apoA-I, particularly late glycation, modifies its structure, its capacity to bind phospholipids and but not ABCA1- or ABCG1-dependent cholesterol efflux from macrophages.

AB - Increased protein glycation in people with diabetes may promote atherosclerosis. This study examined the effects of non-enzymatic glycation on the association of lipid-free apolipoproteinA-I (apoA-I) with phospholipid, and cholesterol efflux from lipid-loaded macrophages to lipid-free and lipid-associated apoA-I. Glycation of lipid-free apoA-I by methylglyoxal and glycolaldehyde resulted in Arg, Lys and Trp loss, advanced glycation end-product formation and protein cross-linking. The association of apoA-I glycated by glucose, methylglyoxal or glycolaldehyde with phospholipid multilamellar vesicles was impaired in a glycating agent dose-dependent manner, with exposure of apoA-I to both 30 mM glucose (42% decrease in kslow) and 3 mM glycolaldehyde (50% decrease in kfast, 60% decrease in kslow) resulting is significantly reduced affinity. Cholesterol efflux to control or glycated lipid-free apoA-I, or discoidal reconstituted HDL containing glycated apoA-I (drHDL), was examined using cholesterol-loaded murine (J774A.1) macrophages treated to increase expression of ATP binding cassette transporters A1 (ABCA1) or G1 (ABCG1). Cholesterol efflux from J774A.1 macrophages to glycated lipid-free apoA-I via ABCA1 or glycated drHDL via an ABCG1-dependent mechanism was unaltered, as was efflux to minimally modified apoA-I from people with Type 1 diabetes, or controls. Changes to protein structure and function were prevented by the reactive carbonyl scavenger aminoguanidine. Overall these studies demonstrate that glycation of lipid-free apoA-I, particularly late glycation, modifies its structure, its capacity to bind phospholipids and but not ABCA1- or ABCG1-dependent cholesterol efflux from macrophages.

KW - ATP-Binding Cassette Transporters

KW - Adult

KW - Aldehydes

KW - Animals

KW - Apolipoprotein A-I

KW - Biological Transport

KW - Case-Control Studies

KW - Cell Line

KW - Cholesterol

KW - Diabetes Mellitus, Type 1

KW - Female

KW - Glucose

KW - Glycosylation

KW - Humans

KW - Lipid Metabolism

KW - Lipoproteins, HDL

KW - Macrophages

KW - Male

KW - Mice

KW - Phospholipids

KW - Young Adult

U2 - 10.1371/journal.pone.0065430

DO - 10.1371/journal.pone.0065430

M3 - Journal article

C2 - 23741493

VL - 8

SP - e65430

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 5

ER -

ID: 128974281