Complete processing of type III collagen in atherosclerotic plaques

被引:33
作者
Bode, MK
Mosorin, M
Satta, J
Risteli, L
Juvonen, T
Risteli, J [1 ]
机构
[1] Oulu Univ, Dept Clin Chem, FIN-90220 Oulu, Finland
[2] Oulu Univ, Dept Surg, FIN-90220 Oulu, Finland
关键词
atherosclerosis; plaque; collagen; extracellular matrix;
D O I
10.1161/01.ATV.19.6.1506
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
The extent of processing of type LII collagen is assessed, and the proportions of type I and III collagens are estimated in atherosclerotic plaques obtained from the carotid artery, common femoral artery, and aorta. The fraction of type III collagen that had retained its amino-terminal propeptide (pN-collagen) was 42% in the soluble extract but only 0.0081% in the insoluble residue. Taken together, only 0.011% of the type III collagen in whole plaques was in the form of type In: pN-collagen. Together with the small amounts of the free propeptides of type I procollagen, this finding indicates a low rate of collagen turnover. The amounts of solubilized telopeptides of type I and III collagens were measured, after heat denaturation and trypsin digestion of the collagenous helix, by specific immunoassays for the corresponding trypsin-generated antigens. The mean proportion of type III collagen was 61% (95% confidence interval, 58% to 65%) in the carotid and femoral artery plaques and 56% (95% confidence interval, 44% to 68%) in the aortic specimens. The completely processed and cross-linked type III collagen seems to be the major collagen type in atherosclerotic plaques.
引用
收藏
页码:1506 / 1511
页数:6
相关论文
共 36 条
[1]  
BARNES MJ, 1985, COLLAGEN REL RES, V5, P65
[2]   3 CONFORMATIONALLY DISTINCT DOMAINS IN AMINO-TERMINAL SEGMENT OF TYPE-III PROCOLLAGEN AND ITS RAPID TRIPLE HELIX REVERSIBLE COIL TRANSITION [J].
BRUCKNER, P ;
BACHINGER, HP ;
TIMPL, R ;
ENGEL, J .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1978, 90 (03) :595-603
[3]  
Dabbagh K, 1998, THROMB HAEMOSTASIS, V79, P405
[4]   CROSS-LINKING IN COLLAGEN AND ELASTIN [J].
EYRE, DR ;
PAZ, MA ;
GALLOP, PM .
ANNUAL REVIEW OF BIOCHEMISTRY, 1984, 53 :717-748
[5]   COLLAGEN FIBRILLOGENESIS IN HUMAN-SKIN [J].
FLEISCHMAJER, R ;
PERLISH, JS ;
TIMPL, R .
ANNALS OF THE NEW YORK ACADEMY OF SCIENCES, 1985, 460 :246-257
[6]   In vitro interactions of oxidatively modified LDL with type I, II, III, IV and V collagen, laminin, fibronectin, and poly-D-lysine [J].
Greilberger, J ;
Schmut, O ;
Jurgens, G .
ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, 1997, 17 (11) :2721-2728
[7]   QUANTITATION OF TYPE-I TO TYPE-III COLLAGEN RATIOS IN SMALL SAMPLES OF HUMAN TENDON, BLOOD-VESSELS, AND ATHEROSCLEROTIC PLAQUE [J].
HANSON, AN ;
BENTLEY, JP .
ANALYTICAL BIOCHEMISTRY, 1983, 130 (01) :32-40
[8]   INCORPORATION OF SULFATE INTO TYPE-III PROCOLLAGEN BY CULTURED HUMAN-FIBROBLASTS - IDENTIFICATION OF TYROSINE O-SULFATE [J].
JUKKOLA, A ;
RISTELI, J ;
NIEMELA, O ;
RISTELI, L .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1986, 154 (01) :219-224
[9]   COLLAGENS IN HUMAN ATHEROSCLEROSIS - IMMUNOHISTOCHEMICAL ANALYSIS USING COLLAGEN TYPE-SPECIFIC ANTIBODIES [J].
KATSUDA, S ;
OKADA, Y ;
MINAMOTO, T ;
ODA, Y ;
MATSUI, Y ;
NAKANISHI, I .
ARTERIOSCLEROSIS AND THROMBOSIS, 1992, 12 (04) :494-502
[10]  
KAUPPILA S, IN PRESS BR J CANC