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Localization of thrombospondin in clots formed in situ
JE Murphy-Ullrich and DF Mosher
Thrombospondin is a principal glycoprotein secreted by thrombin- stimulated
platelets and has known affinities for fibrinogen and fibrin. We studied
the distribution of thrombospondin in clots formed in situ on
Formvar-coated coverslips at 37 degrees C for intervals up to 17 hours. The
distributions of three other major platelet granular proteins--fibrinogen,
fibronectin, and von Willebrand factor (vWF)-- were also determined. The
portions of the clots adhering to the coverslips after stripping, washing,
and fixation with formaldehyde were stained for the four proteins by the
peroxidase-antiperoxidase technique. Monoclonal antibodies were used to
localize thrombospondin, fibronectin, and vWF; affinity-purified polyclonal
antibodies were used to localize fibrinogen. Platelets stained positively
for all four proteins. Thrombospondin was maximally present in the fibrin
meshwork from 1 1/2 to 2 hours, after which the intensity of staining
decreased until only trace amounts of thrombospondin were detectable
between four and 17 hours. Antifibrinogen and, to a lesser extent,
antifibronectin stained the fibrin meshwork at all time points. The vWF was
not detectable in the fibrin meshwork at any time point. Staining of
polymorphonuclear leukocytes (PMNLs) in a fine granular pattern was found
with antithrombospondin. The fraction of PMNLs staining positively was 6%
to 14% at 1/2 to 4 hours and increased at eight hours to 27%. At 17 hours,
52% of the PMNLs stained for thrombospondin. More than 48% of the PMNLs
stained with antifibrinogen at all time points. PMNLs did not stain for
either fibronectin or vWF. These studies indicate that thrombospondin is a
transient component of the temporary fibrin meshwork and has a unique
spatial and temporal distribution in the hemostatic plug.
Volume 66,
Issue 5,
pp. 1098-1104,
11/01/1985
Copyright © 1985 by The American Society of Hematology
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