Identification of a Danger-Associated Peptide From Apolipoprotein B100 (ApoBDS-1) That Triggers Innate Proatherogenic Responses
(2011) In Circulation 124(22). p.2433-2433- Abstract
- Background-Subendothelial deposited low-density lipoprotein particles are a known inflammatory factor in atherosclerosis. However, the causal components derived from low-density lipoprotein are still poorly defined. Apolipoprotein B100 (ApoB100) is the unexchangeable protein component of low-density lipoprotein, and the progression of atherosclerosis is associated with immune responses to ApoB100-derived peptides. In this study, we analyzed the proinflammatory activity of ApoB100 peptides in atherosclerosis. Methods and Results-By screening a peptide library of ApoB100, we identified a distinct native peptide referred to as ApoB100 danger-associated signal 1 (ApoBDS-1), which shows sequence-specific bioactivity in stimulation of... (More)
- Background-Subendothelial deposited low-density lipoprotein particles are a known inflammatory factor in atherosclerosis. However, the causal components derived from low-density lipoprotein are still poorly defined. Apolipoprotein B100 (ApoB100) is the unexchangeable protein component of low-density lipoprotein, and the progression of atherosclerosis is associated with immune responses to ApoB100-derived peptides. In this study, we analyzed the proinflammatory activity of ApoB100 peptides in atherosclerosis. Methods and Results-By screening a peptide library of ApoB100, we identified a distinct native peptide referred to as ApoB100 danger-associated signal 1 (ApoBDS-1), which shows sequence-specific bioactivity in stimulation of interleukin-8, CCL2, and interleukin-6. ApoBDS-1 activates mitogen-activated protein kinase and calcium signaling, thereby effecting the expression of interleukin-8 in innate immune cells. Ex vivo stimulation of carotid plaques with ApoBDS-1 enhances interleukin-8 and prostaglandin E(2) release. Furthermore, we demonstrated that ApoBDS-1-positive peptide fragments are present in atherosclerotic lesions using immunoassays and that low-molecular-weight fractions isolated from plaque show ApoBDS-1 activity inducing interleukin-8 production. Conclusions-Our data show that ApoBDS-1 is a previously unrecognized peptide with robust proinflammatory activity, contributing to the disease-promoting effects of low-density lipoprotein in the pathogenesis of atherosclerosis. (Circulation. 2011; 124: 2433-2443.) (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2307030
- author
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- apolipoprotein B100, atherosclerosis, innate immunity, macrophage, oxidized LDL
- in
- Circulation
- volume
- 124
- issue
- 22
- pages
- 2433 - 2433
- publisher
- Lippincott Williams & Wilkins
- external identifiers
-
- wos:000298130700015
- scopus:82355175118
- ISSN
- 1524-4539
- DOI
- 10.1161/CIRCULATIONAHA.111.051599
- language
- English
- LU publication?
- yes
- id
- d01ebb68-2d10-4621-bcfa-5121f32d4669 (old id 2307030)
- date added to LUP
- 2016-04-01 14:44:28
- date last changed
- 2022-04-14 19:28:59
@article{d01ebb68-2d10-4621-bcfa-5121f32d4669, abstract = {{Background-Subendothelial deposited low-density lipoprotein particles are a known inflammatory factor in atherosclerosis. However, the causal components derived from low-density lipoprotein are still poorly defined. Apolipoprotein B100 (ApoB100) is the unexchangeable protein component of low-density lipoprotein, and the progression of atherosclerosis is associated with immune responses to ApoB100-derived peptides. In this study, we analyzed the proinflammatory activity of ApoB100 peptides in atherosclerosis. Methods and Results-By screening a peptide library of ApoB100, we identified a distinct native peptide referred to as ApoB100 danger-associated signal 1 (ApoBDS-1), which shows sequence-specific bioactivity in stimulation of interleukin-8, CCL2, and interleukin-6. ApoBDS-1 activates mitogen-activated protein kinase and calcium signaling, thereby effecting the expression of interleukin-8 in innate immune cells. Ex vivo stimulation of carotid plaques with ApoBDS-1 enhances interleukin-8 and prostaglandin E(2) release. Furthermore, we demonstrated that ApoBDS-1-positive peptide fragments are present in atherosclerotic lesions using immunoassays and that low-molecular-weight fractions isolated from plaque show ApoBDS-1 activity inducing interleukin-8 production. Conclusions-Our data show that ApoBDS-1 is a previously unrecognized peptide with robust proinflammatory activity, contributing to the disease-promoting effects of low-density lipoprotein in the pathogenesis of atherosclerosis. (Circulation. 2011; 124: 2433-2443.)}}, author = {{Ketelhuth, Daniel F. J. and Rios, Francisco J. O. and Wang, Yajuan and Liu, Huiqing and Johansson, Maria E. and Nordin Fredrikson, Gunilla and Hedin, Ulf and Gidlund, Magnus and Nilsson, Jan and Hansson, Goran K. and Yan, Zhong-qun}}, issn = {{1524-4539}}, keywords = {{apolipoprotein B100; atherosclerosis; innate immunity; macrophage; oxidized LDL}}, language = {{eng}}, number = {{22}}, pages = {{2433--2433}}, publisher = {{Lippincott Williams & Wilkins}}, series = {{Circulation}}, title = {{Identification of a Danger-Associated Peptide From Apolipoprotein B100 (ApoBDS-1) That Triggers Innate Proatherogenic Responses}}, url = {{http://dx.doi.org/10.1161/CIRCULATIONAHA.111.051599}}, doi = {{10.1161/CIRCULATIONAHA.111.051599}}, volume = {{124}}, year = {{2011}}, }