The mechanism of thrombin-induced platelet factor 4 secretion.

@article{Ginsberg1980TheMO,
  title={The mechanism of thrombin-induced platelet factor 4 secretion.},
  author={Mark H. Ginsberg and L. M. Taylor and Richard G. Painter},
  journal={Blood},
  year={1980},
  volume={55 4},
  pages={
          661-8
        }
}
We have measured thrombin-induced secretion of platelet factor 4 antigen (PF4) and simultaneously followed its intracellular translocation by immunofluorescence. In permeable resting platelets, speckled intracellular immunofluorescent staining for PF4 was observed. Addition of thrombin to washed platelets at 22 degrees C resulted in secretion of PF4 and formation of large (approximately 0.5 micrometer) immunofluorescent masses. These masses moved to the cell periphery during secretion and were… 
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Ultrastructural localization of coagulation factor V in human platelets.
TLDR
At the light level, Factor V and Fbg are localized in the same structure in resting and thrombin-stimulated cells, establishing at the ultrastructural level an alpha granule localization of human coagulation Factor V.
Centripetal myosin redistribution in thrombin-stimulated platelets. Relationship to platelet Factor 4 secretion.
Redistribution of alpha-granules and their contents in thrombin- stimulated platelets
TLDR
Thrombin stimulation of platelets causes at least some of the fibrinogen, beta TG, and PF4 stored in their alpha granules to be redistributed to their plasma membranes by way of surface-connected vacuoles formed by fusion of thealpha granules with elements of the surface- connected canalicular system.
Immunofluorescent localization of adhesive glycoproteins in resting and thrombin-stimulated platelets.
TLDR
In thrombin-stimulated cells, co-localization of all proteins in these masses was observed by double label immunofluorescence, indicating that TSP, Fbg, Fn, and beta TG are localized in the same structure in resting cells.
Further studies of the secretory pathway in thrombin-stimulated human platelets.
TLDR
The findings support the concept that secretion by stimulated human platelets results from development of direct communications between granules and channels of the OCS and subsequent extrusion of products through channel pores to the surrounding medium.
Immunocytochemical localization of fibrinogen during thrombin-induced aggregation of washed human platelets.
TLDR
At least some aggregation in response to thrombin can occur without the participation of released fibrinogen, and much of the granule fibr inogen appears to remain localized at sites where granules fuse with the plasma membrane or the open canalicular system.
Localization of internal pools of membrane glycoproteins involved in platelet adhesive responses.
TLDR
Analysis of the distribution of glycoprotein Ib and IIb/IIIa by immunofluorescence and immunoelectron microscopy suggests that GPIIb/ IIIa is present in alpha-granule membranes and may be transported to the cell surface in response to thrombin treatment.
The ultrastructural localization of platelet factor 4 and fibronectin in human platelets
TLDR
Results provide additional evidence that platelet factor 4 and fibronectin are localized in a-granules of platelet and megakaryocyte and suggest that the synthesis occurs inmegakaryocytes where these are packaged into granules before release of platelets into the circulating blood.
Binding of Fibronectin to o -Granule-deficient Platelets
TLDR
Data preclude any simple model in which newly surface expressed thrombospondin (or other a-granule protein) functions as the major thrombin-stimulated plasma fibronectin receptor in this cell type.
Plasma membrane GPIIb/IIIa. Evidence for a cycling receptor pool.
TLDR
Thrombin stimulation of resting platelets resulted in the clearing of this newly internalized pool of GPIIb/IIIa; presumably via translocation to the surface, suggesting the presence of an actively cycling pool of GPIb/ IIIa that has not been described previously.
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