Heparin interactions with apoA1 and SAA in inflammation-associated HDL

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Heparin interactions with apoA1 and SAA in inflammation-associated HDL. / Digre, Andreas; Nan, Jie; Frank, Martin; Li, Jin-Ping.

In: Biochemical and Biophysical Research Communications, Vol. 474, No. 2, 27.05.2016, p. 309-14.

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Digre, Andreas ; Nan, Jie ; Frank, Martin ; Li, Jin-Ping. / Heparin interactions with apoA1 and SAA in inflammation-associated HDL. In: Biochemical and Biophysical Research Communications. 2016 ; Vol. 474, No. 2. pp. 309-14.

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TY - JOUR

T1 - Heparin interactions with apoA1 and SAA in inflammation-associated HDL

AU - Digre, Andreas

AU - Nan, Jie

AU - Frank, Martin

AU - Li, Jin-Ping

N1 - Copyright © 2016 Elsevier Inc. All rights reserved.

PY - 2016/5/27

Y1 - 2016/5/27

N2 - Apolipoprotein A1 (apoA1) is the main protein component responsible for transportation of cholesterol on high-density lipoprotein (HDL). Serum amyloid A (SAA) is an acute phase protein associated with HDL. Apart from their physiological functions, both apoA1 and SAA have been identified as 'amyloidogenic peptides'. We report herein that the polysaccharide heparin interacts with both apoA1 and SAA in HDL isolated from plasma of inflamed mice. The reaction is rapid, forming complex aggregates composed of heparin, apoA1 and SAA as revealed by gel electrophoresis. This interaction is dependent on the size and concentration of added heparin. Mass spectrometry analysis of peptides derived from chemically crosslinked HDL-SAA particles detected multiple crosslinks between apoA1 and SAA, indicating close proximity (within 25 Å) of these two proteins on the HDL surface, providing a molecular and structural mechanism for the simultaneous binding of heparin to apoA1 and SAA.

AB - Apolipoprotein A1 (apoA1) is the main protein component responsible for transportation of cholesterol on high-density lipoprotein (HDL). Serum amyloid A (SAA) is an acute phase protein associated with HDL. Apart from their physiological functions, both apoA1 and SAA have been identified as 'amyloidogenic peptides'. We report herein that the polysaccharide heparin interacts with both apoA1 and SAA in HDL isolated from plasma of inflamed mice. The reaction is rapid, forming complex aggregates composed of heparin, apoA1 and SAA as revealed by gel electrophoresis. This interaction is dependent on the size and concentration of added heparin. Mass spectrometry analysis of peptides derived from chemically crosslinked HDL-SAA particles detected multiple crosslinks between apoA1 and SAA, indicating close proximity (within 25 Å) of these two proteins on the HDL surface, providing a molecular and structural mechanism for the simultaneous binding of heparin to apoA1 and SAA.

U2 - 10.1016/j.bbrc.2016.04.092

DO - 10.1016/j.bbrc.2016.04.092

M3 - Article

VL - 474

SP - 309

EP - 314

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 1090-2104

IS - 2

ER -