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Rabbit and rat platelets do not respond to thrombin receptor peptides that
activate human platelets
RL Kinlough-Rathbone, ML Rand and MA Packham
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.
Human platelets are aggregated and induced to release their granule
contents and form thromboxane by peptides as short as 6-amino acid residues
(SFLLRN) corresponding to the newly released N-terminus of the thrombin
receptor that is cleaved by thrombin. Using washed platelets, we found that
these responses to SFLLRN (2 to 6 mumol/L) were enhanced by fibrinogen.
However, neither SFLLRN nor SFLLRNPNDKYEPF had any effect on washed rabbit
or rat platelets, although they were fully responsive to human thrombin.
Concentrations of the peptides as high as 100 mumol/L did not cause the
platelets of rabbits or rats to change shape, aggregate, release granule
contents, or form thromboxane. SFLLRN did not affect the extent of
aggregation induced by adenosine diphosphate (ADP) or a low concentration
of thrombin. Pig platelets responded to 50 mumol/L SFLLRN with reversible
aggregation, which was enhanced by fibrinogen, but not accompanied by the
release of dense granule contents. Guinea pig platelets aggregated and
released granule contents in response to 25 or 50 mumol/L of SFLLRN, but
responded with only shape change to lower concentrations. Thus, these
experiments indicate that rabbit and rat platelets lack a functional
response to human thrombin receptor peptides that fully activate the
previously described human thrombin receptor, despite a full response of
both rabbit and rat platelets to human thrombin, and that pig and guinea
pig platelets have incomplete responses to these human thrombin receptor
peptides. The results suggest that platelets of rabbits and rats, and
perhaps guinea pigs and pigs, respond to thrombin through an alternative
receptor that has also been suggested to be present on human platelets.
Volume 82,
Issue 1,
pp. 103-106,
07/01/1993
Copyright © 1993 by The American Society of Hematology
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