Heparin interactions with apoA1 and SAA in inflammation-associated HDL
(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.
(Less)
- author
- Digre, Andreas ; Nan, Jie LU ; Frank, Martin and Li, Jin-Ping
- organization
- publishing date
- 2016-05-27
- 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
-
- pmid:27105909
- scopus:84964575149
- wos:000376221700013
- 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
- 2024-06-28 14:39:37
@article{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 = {{Elsevier}}, 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}}, doi = {{10.1016/j.bbrc.2016.04.092}}, volume = {{474}}, year = {{2016}}, }