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The transglutaminase in vascular cells and tissues could provide an
alternate pathway for fibrin stabilization
CS Greenberg, KE Achyuthan, MJ Borowitz and MA Shuman
A thrombin-independent transglutaminase (TG) has been identified in
vascular cells and tissues from human, rabbit, rat, porcine, and bovine
sources. The vascular TG had several properties that were similar but not
identical to guinea pig liver TG. Both enzymes had similar chromatographic
and electrophoretic properties, preferentially cross- linked the
alpha-chains of fibrinogen, and reacted with polyclonal and monoclonal
anti-guinea-pig liver TG antibodies. However, the TG from adult bovine
aortic endothelial (ABAE) cells exhibited a novel Ca2+/Mg2+ dependence for
enzymatic activity that was distinct from that of purified guinea pig liver
TG. The mol wt of the vascular TG (79 +/- 3 kd) determined by sodium
dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was slightly
lower than the purified guinea pig liver TG (85 +/- 9 kd). The TG antigen
was detected by immunohistochemical techniques in association with the
endothelial and smooth muscle cells of arteries, veins, venules, and
capillaries. The TG antigen also codistributed with the fibronectin antigen
along the hepatic sinusoids. The ABAE cell TG cross-linked alpha 2-plasmin
inhibitor to fibrinogen and caused the modified fibrinogen to be 40- fold
more resistant to plasminolysis. A thrombin-independent TG in vascular
cells of blood vessels could provide an alternate pathway to inhibit
fibrinolysis and promote fibrin stabilization.
Volume 70,
Issue 3,
pp. 702-709,
09/01/1987
Copyright © 1987 by The American Society of Hematology

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