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Two highly purified neutral proteases from human leukocytes i.e. elastase-like protease (ELP) and chymotrypsin-like protease (CLP) do not destroy human platelets since no difference was found in 51Cr liberation from control and enzyme-treated platelets. As with pancreatic chymotrypsin (alpha-CT) ELP does not induce the release of 3H-serotonin while CLP provokes 3H-serotonin secretion, in an enzyme concentration and time dependent fashion. The rate and degree of 3H-serotonin release by CLP is similar to that produced by thrombin. Incubation of platelets at 37 degrees C for 30 min with alpha-CT or ELP renders them resistant to thrombin-releasing activity. Thrombin did not liberate any additional label from platelets which lost over 60% of serotonin during the preceding incubation with CLP. alpha-CT and ELP do not aggregate platelets either in the presence or absence of apyrase. CLP does aggregate platelets suspended in Tyrode buffer without apyrase but not in the presence of apyrase (100 mg/l). The action of alpha-CT, ELP and CLP on washed platelets induces a progressive prolongation of lag phase and a decrease in changes of light transmission during aggregation by thrombin. Similarly to alpha-CT-treated platelets, those subjected to CLP action aggregate in the presence of human fibrinogen. It is concluded that: (1) neutral proteases possibly contribute to development of defects in platelet function in pathological states associated with liberation of leukocyte content into the circulation, (2) CLP similarly to alpha-CT, exposes fibrinogen receptors but in contrast to alpha-CT, CLP aggregates platelets and stimulates serotonin secretion.
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J Kaczanowska, and
M Karpowicz, and
J Stachurska, and
M Kopeć
March 1984,
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K Bykowska, and
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M Karpowicz, and
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M Kopeć
April 1980,
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K Bykowska, and
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K Bykowska, and
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K Bykowska, and
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Blut,
K Bykowska, and
J Kaczanowska, and
M Karpowicz, and
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M Kopeć
July 2003,
Intensive care medicine,
K Bykowska, and
J Kaczanowska, and
M Karpowicz, and
J Stachurska, and
M Kopeć
October 1975,
Infection and immunity,
