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J Biol Chem, Vol. 273, Issue 24, 14827-14837, June 12, 1998
From the Department of Protein Biochemistry, Institute of Life
Science, Kurume University, Kurume-shi,
Fukuoka-ken 839-8016, Japan
Platelet interaction with soluble and insoluble
collagens was characterized through binding studies. In contrast
to resting platelets, cells reacted with activators, TS2/16 (integrin
2
1-activating antibody), thrombin,
collagen-related peptide, or ADP, exhibited specific soluble collagen
binding that is Mg2+-dependent, but inhibited
by prostaglandin I2, Ca2+, and Gi9
(anti-integrin 21 antibody). Each
platelet has 1500-3500 soluble collagen binding sites, with a
dissociation constant of 3.5-9 × 10
8
M. This is the first study to show the specific binding of
soluble collagen to platelets; our data strongly suggest that the
receptor is integrin 21 after it becomes
activated upon platelet activation. These results suggest that
activation of platelets transforms integrin
21 to a state with higher affinity
binding sites for soluble collagen. The soluble collagen-platelet
interaction was compared with the platelet interaction with fibrillar
collagen, which has until now not been demonstrated to bind
specifically to platelets. Here, we demonstrated specific, biphasic
fibrillar collagen binding. One phase is rapid and metal
ion-independent, and accounts for most of the binding. The other phase
is slow and Mg2+-dependent. The characteristic
differences in the specific bindings of soluble and fibrous collagens
demonstrate the different contributions of two different collagen
receptors.
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