Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞
Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary arteries and explored potential roles for SAP...
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doaj-4be7ffc24e654f12aad6a602e6012d942021-04-28T06:06:47ZengElsevierJournal of Lipid Research0022-22752007-10-01481021622171Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞Cameron R. Stewart0Antonio Haw, III1Roland Lopez2Thomas O. McDonald3Judy M. Callaghan4Malcolm J. McConville5Kathryn J. Moore6Geoffrey J. Howlett7Kevin D. O'Brien8Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, AustraliaUniversity of Washington Medical Center, Seattle, WA 98195University of Washington Medical Center, Seattle, WA 98195University of Washington Medical Center, Seattle, WA 98195Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, AustraliaDepartment of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, AustraliaLipid Metabolism Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, AustraliaUniversity of Washington Medical Center, Seattle, WA 98195Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary arteries and explored potential roles for SAP in these regions, specifically the effect of SAP on the rate of formation and macrophage recognition of amyloid fibrils composed of apoC-II. Analysis of 42 human arterial sections by immunohistochemistry and double label fluorescence microscopy demonstrated that SAP and apoA-I, apoB, apoC-II, and apoE were increased significantly in atherosclerotic lesions compared with nonatherosclerotic segments. SAP colocalized with all four apolipoproteins to a similar extent, whereas plaque macrophages were found to correlate most strongly with apoC-II and apoB. In vitro studies showed that SAP accelerated the formation of amyloid fibrils by purified apoC-II. Furthermore, SAP strongly inhibited the phagocytosis of apoC-II amyloid fibrils by primary macrophages and macrophage cell lines and blocked the resultant production of reactive oxygen species. The ability of SAP to accelerate apoC-II amyloid fibril formation and inhibit macrophage recognition of apoC-II fibrils suggests that SAP may modulate the inflammatory response to amyloid fibrils in atherosclerosis.http://www.sciencedirect.com/science/article/pii/S0022227520424617atherosclerosismacrophageimmunohistochemistryamyloid |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Cameron R. Stewart Antonio Haw, III Roland Lopez Thomas O. McDonald Judy M. Callaghan Malcolm J. McConville Kathryn J. Moore Geoffrey J. Howlett Kevin D. O'Brien |
spellingShingle |
Cameron R. Stewart Antonio Haw, III Roland Lopez Thomas O. McDonald Judy M. Callaghan Malcolm J. McConville Kathryn J. Moore Geoffrey J. Howlett Kevin D. O'Brien Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ Journal of Lipid Research atherosclerosis macrophage immunohistochemistry amyloid |
author_facet |
Cameron R. Stewart Antonio Haw, III Roland Lopez Thomas O. McDonald Judy M. Callaghan Malcolm J. McConville Kathryn J. Moore Geoffrey J. Howlett Kevin D. O'Brien |
author_sort |
Cameron R. Stewart |
title |
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
title_short |
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
title_full |
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
title_fullStr |
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
title_full_unstemmed |
Serum amyloid P colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
title_sort |
serum amyloid p colocalizes with apolipoproteins in human atheroma: functional implicationss⃞ |
publisher |
Elsevier |
series |
Journal of Lipid Research |
issn |
0022-2275 |
publishDate |
2007-10-01 |
description |
Serum amyloid P (SAP) is a common component of human amyloid deposits and has been identified in atherosclerotic lesions. We investigated the extent of the colocalization of SAP with apolipoprotein A-I (apoA-I), apoB, apoC-II, and apoE in human coronary arteries and explored potential roles for SAP in these regions, specifically the effect of SAP on the rate of formation and macrophage recognition of amyloid fibrils composed of apoC-II. Analysis of 42 human arterial sections by immunohistochemistry and double label fluorescence microscopy demonstrated that SAP and apoA-I, apoB, apoC-II, and apoE were increased significantly in atherosclerotic lesions compared with nonatherosclerotic segments. SAP colocalized with all four apolipoproteins to a similar extent, whereas plaque macrophages were found to correlate most strongly with apoC-II and apoB. In vitro studies showed that SAP accelerated the formation of amyloid fibrils by purified apoC-II. Furthermore, SAP strongly inhibited the phagocytosis of apoC-II amyloid fibrils by primary macrophages and macrophage cell lines and blocked the resultant production of reactive oxygen species. The ability of SAP to accelerate apoC-II amyloid fibril formation and inhibit macrophage recognition of apoC-II fibrils suggests that SAP may modulate the inflammatory response to amyloid fibrils in atherosclerosis. |
topic |
atherosclerosis macrophage immunohistochemistry amyloid |
url |
http://www.sciencedirect.com/science/article/pii/S0022227520424617 |
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