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Cross-talk between adenosine and the oxatriazole derivative GEA 3175 in platelets

Asplund Persson, Anna, 1966- (author)
Linköpings universitet,Farmakologi,Hälsouniversitetet
Zalavary, Stefan (author)
Linköpings universitet,Hälsouniversitetet
Lindström, Eva, 1961- (author)
Linköpings universitet,Farmakologi,Hälsouniversitetet
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Whiss, Per A, 1966- (author)
Linköpings universitet,Farmakologi,Hälsouniversitetet
Bengtsson, Torbjörn, 1955- (author)
Linköpings universitet,Farmakologi,Hälsouniversitetet
Grenegård, Magnus, 1963- (author)
Linköpings universitet,Farmakologi,Hälsouniversitetet
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 (creator_code:org_t)
Elsevier BV, 2005
2005
English.
In: European Journal of Pharmacology. - : Elsevier BV. - 0014-2999 .- 1879-0712. ; 517:3, s. 149-157
  • Journal article (peer-reviewed)
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  • We examined the interplay between adenosine and the nitric oxide (NO)-containing oxatriazole derivative GEA 3175 in human platelets. The importance of cyclic guanosine 3′5′-monophosphate (cGMP)-inhibited phosphodiesterases (PDEs) was elucidated by treating the platelets with adenosine combined with either GEA 3175 or the PDE3-inhibitor milrinone. The drug combinations provoked similar cyclic adenosine 3′5′-monophosphate (cAMP) responses. On the contrary, cGMP levels were increased only in GEA 3175-treated platelets. Both drug combinations reduced P-selectin exposure, platelet adhesion and fibrinogen-binding. However, adenosine together with GEA 3175 was more effective in inhibiting platelet aggregation and ATP release. Thrombin-induced rises in cytosolic Ca2+ were suppressed by the two drug combinations. Adenosine administered with GEA 3175 was, however, more effective in reducing Ca2+ influx.In conclusion, the interaction between adenosine and GEA 3175 involves cGMP-mediated inhibition of PDE3. The results also imply that inhibition of Ca2+ influx represent another cGMP-specific mechanism that enhances the effect of adenosine.

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