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J Biol Chem, Vol. 274, Issue 5, 3033-3041, January 29, 1999
From the We have identified type VI collagen
(Col VI) as a primary subendothelial extracellular matrix component
responsible for von Willebrand factor (vWF)-dependent
platelet adhesion and aggregation under high tensile strength. Intact
tetrameric Col VI was the form of the collagen found to be capable of
promoting vWF-mediated platelet adhesion/aggregation under this shear
condition, whereas removal of the predominant portion of the terminal
globules by pepsin treatment abrogated its activity. The inability of
the pepsin-digested Col VI to support any platelet interaction at high
flow was because of the failure of the A3(vWF) domain to bind to this
form of collagen, suggesting a stringent requirement of a
tridimensional conformation or of intactness of its macromolecular structure. In contrast, the A1(vWF) domain bound to both intact and
pepsin-digested Col VI tetramers but, in accordance with the cooperating function of the two vWF domains, failed to support platelet
adhesion/aggregation under high shear onto Col VI by itself. The
putative A1(vWF) binding site resided within the A7(VI) module
(residues 413-613) of the globular amino-terminal portion of the
Identification of Domains Responsible for von Willebrand Factor
Type VI Collagen Interaction Mediating Platelet Adhesion under High
Flow
,,,,
,
Servizio Immunotrasfusionale e Analisi
Cliniche and § Divisione di Oncologia Sperimentale 2, Centro
di Riferimento Oncologico, Instituto Nazionale Tumori Centroeuropeo,
Aviano (PN) 33081 Italy, ¶ Department of Pediatrics Nara Medical
University, 840 Shijo-cho, Kashihara City Nara 634 Japan,
** Dipartimento di Scienze e Tecnologie Biomediche University of Udine,
Udine 33100 Italy, and Department of Evolutionary and
Functional Biology, University of Parma, Parma, 43100 Italy
3(VI) chain. Soluble recombinant A7(VI) polypeptide strongly perturbed the vWF-mediated platelet adhesion to Col VI under high shear
rates, without affecting the binding of the vWF platelet receptor
glycoprotein Ib to its cognate ligand A1(vWF). The findings provide
evidence for a concerted action of the A1(vWF) and A3(vWF) domains in
inducing platelet arrest on Col VI. This is accomplished via an
interaction of the A1(vWF) domain with a site contained in the 3
chain A7(VI) domain and via a conformation-dependent interaction of the A3(vWF) domain with the intact tetrameric collagen. The data further emphasize that Col VI microfilaments linking the
subendothelial basement membrane to the interstitial collagenous network may play a pivotal role in the hemostatic process triggered upon damage of the blood vessel wall.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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