Matrix Metalloproteinase-13/Collagenase-3 Deletion Promotes Collagen Accumulation and Organization in Mouse Atherosclerotic Plaques
Author(s) -
Jun-o Deguchi,
Elena Aïkawa,
Peter Libby,
Jeffrey R. Vachon,
Masaki Inada,
Stephen M. Krane,
Peter Whittaker,
Masanori Aikawa
Publication year - 2005
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.105.562041
Subject(s) - collagenase , matrix metalloproteinase , interstitial collagenase , apolipoprotein e , medicine , apolipoprotein b , pathology , elastin , inflammation , mmp1 , matrix (chemical analysis) , endocrinology , chemistry , biochemistry , enzyme , gene expression , cholesterol , disease , gene , chromatography
Interstitial collagen plays a crucial structural role in arteries. Matrix metalloproteinases (MMPs), including MMP-13/collagenase-3, likely contribute to collagen catabolism in atherosclerotic plaques.
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