DIFFERENTIAL ENERGY-REQUIREMENTS FOR PLATELET RESPONSES - A SIMULTANEOUS STUDY OF AGGREGATION, 3 SECRETORY PROCESSES, ARACHIDONATE LIBERATION, PHOSPHATIDYLINOSITOL BREAKDOWN AND PHOSPHATIDATE PRODUCTION
DIFFERENTIAL ENERGY-REQUIREMENTS FOR PLATELET RESPONSES - A SIMULTANEOUS STUDY OF AGGREGATION, 3 SECRETORY PROCESSES, ARACHIDONATE LIBERATION, PHOSPHATIDYLINOSITOL BREAKDOWN AND PHOSPHATIDATE PRODUCTION
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DOI:
10.1042/bj2080009
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发表时间:
1982-01-01
影响因子:
4.1
通讯作者:
DANGELMAIER, CA
中科院分区:
文献类型:
--
作者:
HOLMSEN, H;KAPLAN, KL;DANGELMAIER, CA
Different energy requirements are indicated for some platelet responses; these differences could be due to inadequate methodology and differences in platelet preparation. The efect of decreasing ATP availability on 7 platelet responses measured in gel-filtered human platelets are described. The cells, prelabeled with 5-hydroxy[3H]tryptamine, [3H]- or [14C]adenine, [32P]Pi or [3H]arachidonate, were incubated with antimycin A and 2-deoxy-D-glucose. Platelet responses induced by thrombin and collagen (secretion only), level of metabolic ATP and the adenylate energy charge (AEC) were determined at various times during incubation. Platelet aggregation was rapidly inhibited after a lag of 5-15 min and with 50% inhibition at AEC = 0.55-0.60. Secretion of 5-hydroxy[14C]tryptamine and ATP + ADP from dense granules and of fibrinogen and .beta.-thromboglobulin from .alpha.-granules were inhibited in parallel, without a lag and with 50% inhibition at AEC = 0.65-0.70. The inhibition of secretion of platelet factor 4 from the .alpha.-granules followed another pattern with 50% inhibition AEC = 0.70-0.80. Breakdown of [3H]arachidonate and secretion of acid hydrolases were inhibited in parallel, and inhibition was present at the start of incubation with 50% inhibition at AEC = 0.80-0.87. The responses apparently have different energy requirements, which increase in the order aggregation < dense granule, .alpha.-granule secretion < acid hydrolase secretion, phosphatidylinositol breakdown, phosphatidate formation and arachidonate liberation. The powerful inhibition of phosphatidylinositol breakdown by metabolic inhibitors suggests that energy-requiring steps are involved in the activation of phospholipase C.