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Heparin interactions with apoA1 and SAA in inflammation-associated HDL

Digre, Andreas; Nan, Jie LU ; Frank, Martin and Li, Jin-Ping (2016) In Biochemical and Biophysical Research Communications 474(2). p.14-309
Abstract

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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
474
issue
2
pages
6 pages
publisher
Elsevier
external identifiers
  • Scopus:84964575149
ISSN
1090-2104
DOI
10.1016/j.bbrc.2016.04.092
language
English
LU publication?
yes
id
42466248-8a18-4228-a021-13e765670ce9
date added to LUP
2016-09-07 22:49:14
date last changed
2016-10-13 05:13:16
@misc{42466248-8a18-4228-a021-13e765670ce9,
  abstract     = {<p>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.</p>},
  author       = {Digre, Andreas and Nan, Jie and Frank, Martin and Li, Jin-Ping},
  issn         = {1090-2104},
  language     = {eng},
  month        = {05},
  number       = {2},
  pages        = {14--309},
  publisher    = {ARRAY(0x911ad50)},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Heparin interactions with apoA1 and SAA in inflammation-associated HDL},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2016.04.092},
  volume       = {474},
  year         = {2016},
}