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Blood, Vol. 94 No. 8 (October 15), 1999:
pp. 2704-2715
Influence of Fibrillar Collagen Structure on the Mechanisms of Platelet
Thrombus Formation Under Flow
Brian Savage,
Mark H. Ginsberg, and
Zaverio M. Ruggeri
From the Roon Research Center for Arteriosclerosis and Thrombosis,
Division of Experimental Hemostasis and Thrombosis, Departments of
Molecular and Experimental Medicine and of Vascular Biology, The
Scripps Research Institute, La Jolla, CA.
We have used real-time video microscopy to study the mechanisms of
platelet adhesion to type I collagen fibrils of distinct structure
exposed to flowing blood. Electron microscopy analysis by surface
replication demonstrated morphological differences between
acid-insoluble fibrils, displaying a regularly repeating striated
pattern (banded collagen), and acid-soluble fibrils generated by pepsin
treatment of insoluble collagen, smaller in size with a helical
configuration (nonbanded collagen). These structural differences proved
to be related to the role of platelet integrin  2 1 in stabilizing adhesion to collagen
under a variety of flow conditions. Blocking
21 function with a monoclonal antibody had no effect on platelet adhesion to insoluble type I collagen coated
at high density on a glass surface, whereas there was an absolute
dependence of 21 function for the initial
permanent arrest of platelets and subsequent thrombus formation on
pepsin-solubilized type I collagen under the same conditions. In
contrast, reconstituted, banded fibrils prepared from
pepsin-solubilized type I collagen supported platelet adhesion and
thrombus development even when platelet
21 function was blocked, a process that
was greatly accelerated by pre-exposure of this substrate to autologous
plasma under flow. These results implicate a collagen receptor(s) on platelets other than 21 that can
selectively engage domains in banded, but not nonbanded type I collagen
when 21 function is blocked. In addition,
collagen structure may regulate the extent and affinity of the binding
under flow of plasma components such as von Willebrand factor and/or
other IIb3 ligands.
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