PLATELET INTERACTION WITH COLLAGEN FIBRILS IN FLOWING BLOOD .1. REACTION OF HUMAN PLATELETS WITH ALPHA CHYMOTRYPSIN-DIGESTED SUBENDOTHELIUM
- 1 January 1977
- journal article
- research article
- Vol. 37 (1), 1-16
Abstract
The subendothelial surface of rabbit aorta and .alpha. chymotrypsin-digested subendothelium were exposed to anticoagulated human blood in an annular flow chamber. The wall shear rate was similar to that observed in large arteries (830 s-1) and exposure times varied from 2 1/2-40 min. The platelet reactive substrate of .alpha. chymotrypsin-digested subendothelium consists of a 3-dimensional meshwork of collagen fibrils which form islands of variable size and height in a matrix of virtually unreactive elastin. Collagen-induced aggregation in the aggregometer was similar with or without prior .alpha. chymotrypsin-digestion of a highly dispersed preparation of fibrillar collagen. The rate of platelet adhesion was decreased on the fibrillar collagen of .alpha. chymotrypsin-digested subendothelium as compared to intact subendothelium. The rate of aggregation was increased once platelets adhered to the fibrillar collagen. Mural thrombi (aggregates) disappeared on subendothelium, whereas they grew progressively on the fibrillar collagen. The fibrillar collagen of .alpha. chymotrypsin-digested subendothelium appears to be a more thrombogenic surface. Physical (loose 3-dimensional meshwork vs. a comparatively solid surface) and/or chemical (number of platelet reactive sites per unit surface area) differences between the 2 surfaces may explain the platelet-surface-interaction patterns which are characteristic for each surface.This publication has 2 references indexed in Scilit:
- PLATELET INTERACTION WITH COLLAGEN FIBRILS IN FLOWING BLOOD .2. IMPAIRED ADHESION-AGGREGATION IN BLEEDING DISORDERS - COMPARISON WITH SUBENDOTHELIUM1977
- The determination of hydroxyproline in tissue and protein samples containing small proportions of this imino acidArchives of Biochemistry and Biophysics, 1961