(Circulation. 2000;101:1229.)
© 2000 American Heart Association, Inc.
Brief Rapid Communications |
Heat Shock Protein 47 Is Expressed in Fibrous Regions of Human Atheroma and Is Regulated by Growth Factors and Oxidized Low-Density Lipoprotein
From the John P. Robarts Research Institute (Vascular Biology Group), London Health Sciences Centre, and University of Western Ontario, Departments of Medicine (Cardiology) (E.R., L.H.C., J.G.P.), Biochemistry, and Medical Biophysics (J.G.P.), London, Canada
Correspondence to J. Geoffrey Pickering, MD, PhD, FRCP(C), London Health Science Centre, 339 Windermere Road, London, Ontario N6A 5A5, Canada. E-mail gpickering{at}rri.on.ca
Background—Heat shock protein 47 (Hsp47) is a stress protein that may act as a chaperone for procollagen. Its involvement in atherosclerosis is unknown.
Methods and Results—Hsp47 expression in human coronary
arteries was assessed by immunostaining. Strong focal
expression was evident in atherosclerotic, but not normal, arteries and
was prevalent in the collagenous regions. Double
immunostaining revealed that all cells expressing type
I procollagen also expressed Hsp47. Moreover, parallel regulation of
pro
1(I)collagen and Hsp47 mRNA expression occurred with cultured
human smooth muscle cells stimulated with transforming growth
factor-ß1 or fibroblast growth factor-2. However, a proportion of
Hsp47-expressing cells in plaque did not express type I procollagen,
and this pattern could be reproduced in culture. Heat shock and
oxidized LDL stimulated the expression of Hsp47 mRNA by smooth muscle
cells, without a concomitant rise in pro1(I)collagen expression.
Conclusions—These findings identify Hsp47 as a novel constituent of human coronary atheroma. Its localization to the fibrous cap, regulation by growth factors in parallel with type I procollagen, and selective upregulation by stress raise the possibility that Hsp47 is a determinant of plaque stability.
Key Words: atherosclerosis • muscle, smooth • collagen • stress
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