Thrombin-induced secretion of serotonin from platelets can occur in seconds.

نویسندگان

  • A R Gear
  • D Burke
چکیده

The platelet release reaction was studied by a new quenched-flow approach. Platelets labeled with 14C-serotonin were reacted for short times (up to 5 sec) with thrombin and then quenched with glutaraldehyde or paraformaldehyde. Serotonin secretion began within 1 sec and was nearly complete by 4 sec. Aggregation recorded by a resistive-particle counter was similarly fast. Therefore, the quenched-flow system reveals that serotonin secretion can occur more rapidly than estimated in earlier studies.

منابع مشابه

Thrombin Causes Subsecond Changes in Protein Phosphorylation of Platelets

We have developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20and 40-kd proteins has been analyzed during the first five seconds of platelet response to thrombin from 0.1 to 5.0 U/mi and compared with the progress of aggregation and serotonin secretion. The onset time for aggregation and phosphorylation of both prot...

متن کامل

Thrombin causes subsecond changes in protein phosphorylation of platelets.

We have developed a general quenched-flow approach to study platelet function as early as 0.3 seconds after stimulation. Phosphorylation of 20- and 40-kd proteins has been analyzed during the first five seconds of platelet response to thrombin from 0.1 to 5.0 U/mL and compared with the progress of aggregation and serotonin secretion. The onset time for aggregation and phosphorylation of both pr...

متن کامل

Thrombin-induced platelet secretion. Further evidence for a specific pathway.

We have studied the interaction between thrombin and washed, human platelets using prostacyclin, a reversible inhibitor of platelet secretion. The effect of thrombin is limited to those reactions that are not inhibited by an increased concentration of platelet cyclic adenosine 3',5'-monophosphate, because prostacyclin is a potent inducer of the latter. Prostacyclin-treated platelets were briefl...

متن کامل

Thrombin induces serotonin secretion and aggregation independently of inositol phospholipids hydrolysis and protein phosphorylation in human platelets permeabilized with saponin.

We have observed that the addition of Ca2+ to platelets, permeabilized with saponin, promotes a drastic dephosphorylation of proteins and polyphosphoinositides without inducing platelet responses. Subsequent addition of thrombin could promote secretion of serotonin and aggregation in the absence of phospholipase C-induced breakdown of the inositol phospholipids and protein phosphorylation. This...

متن کامل

Interaction of Ca2+ and protein phosphorylation in the rabbit platelet release reaction.

Ca2+ flux and protein phosphorylation have been implicated as playing an important role in the induction of the platelet release reaction. However, the interactions between Ca2+, protein phosphorylation, and the release reaction have been difficult to study because secretion in human platelets is independent of extracellular Ca2+. Thus, we studied rabbit platelets, which, unlike human platelets...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

متن کامل
عنوان ژورنال:
  • Blood

دوره 60 5  شماره 

صفحات  -

تاریخ انتشار 1982