We have recently found @entity1476 ( @entity1476 ) in @entity1 platelets and reported that the release of this enzyme during platelet activation stimulates aggregation. We have now identified @entity1495 ( @entity1495 ) in @entity1 platelets and resistance-sized (approximately 200 microm) arteries. Resting platelets released small quantities of pro- @entity1495 . Maximal release of @entity1495 was detected during partial (appr. 30% maximum) aggregation with @entity556 . However, maximal release of @entity1476 was associated with @entity1423 . @entity1495 antibodies induced aggregation of resting platelets and potentiated aggregation of platelets induced by @entity556 and collagen. Moreover, @entity1495 microisolated from arteries as well as recombinant @entity1 @entity1495 (0.1-30 ng/ml) inhibited @entity556 and collagen-induced aggregation. We conclude that @entity1495 is an inhibitor of aggregation and in this action opposes the effects of @entity1476 . The @entity1476 / @entity1495 system may play an important role in the regulation of platelet-platelet and platelet-vessel wall interactions.

Differential regulation of XXXX by matrix metalloproteinases-9 and -2.

@entity1 :: ('9606', 'Species') :: ['human'] @entity556 :: ('2147', 'Gene') :: ['thrombin'] @entity1423 :: ('MESH:D001791', 'Disease') :: ['maximal aggregation'] @entity1476 :: ('4313', 'Gene') :: ['matrix metalloproteinase-2', 'MMP-2'] @entity1495 :: ('4318', 'Gene') :: ['MMP-9', 'matrix metalloproteinase-9']
@entity1423 :: (MESH:D001791,Disease) :: ['platelet aggregation']
