Phosphodiesterase isoenzymes in equine platelets and their influence on platelet adhesion

Bettina Dunkel Department of Veterinary Basic Sciences, The Royal Veterinary College, North Mymms, Herts AL9 7TA, England

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 DVM
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Karen J. Rickards Sackler Institute of Pulmonary Pharmacology, Division of Pharmacology and Therapeutics, King's College London, London Bridge, London SE1 9RT, England

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 BVSc, PhD
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Clive P. Page Sackler Institute of Pulmonary Pharmacology, Division of Pharmacology and Therapeutics, King's College London, London Bridge, London SE1 9RT, England

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Fiona M. Cunningham Department of Veterinary Basic Sciences, The Royal Veterinary College, North Mymms, Herts AL9 7TA, England

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Abstract

Objective—To determine the phosphodiesterase (PDE) isoenzymes in equine platelets and evaluate their influence on platelet adhesion.

Sample Population—Platelets obtained from healthy New Forest Pony geldings that ranged from 12 to 20 years of age (mean ± SEM, 17.3 ± 1.1 years).

Procedures—PDE isoenzyme activity in equine platelets was determined by use of a 2-step radioactive assay. Functional importance of PDE isoenzymes was established by use of selective inhibitors in a colorimetric adhesion assay.

Results—PDE1, PDE2, PDE3, and PDE5 and small amounts of PDE4 were found in equine platelets. Inhibition of PDE3 abolished platelet adhesion almost completely, whereas inhibition of PDE4 and PDE5 had little effect.

Conclusions and Clinical Relevance—Function of equine platelets can be influenced by inhibition of PDE3. Selective PDE3 inhibitors may be clinically useful to regulate platelet function. They offer the advantage of increased potency with fewer adverse effects, compared with those for nonselective PDE inhibitors.

Abstract

Objective—To determine the phosphodiesterase (PDE) isoenzymes in equine platelets and evaluate their influence on platelet adhesion.

Sample Population—Platelets obtained from healthy New Forest Pony geldings that ranged from 12 to 20 years of age (mean ± SEM, 17.3 ± 1.1 years).

Procedures—PDE isoenzyme activity in equine platelets was determined by use of a 2-step radioactive assay. Functional importance of PDE isoenzymes was established by use of selective inhibitors in a colorimetric adhesion assay.

Results—PDE1, PDE2, PDE3, and PDE5 and small amounts of PDE4 were found in equine platelets. Inhibition of PDE3 abolished platelet adhesion almost completely, whereas inhibition of PDE4 and PDE5 had little effect.

Conclusions and Clinical Relevance—Function of equine platelets can be influenced by inhibition of PDE3. Selective PDE3 inhibitors may be clinically useful to regulate platelet function. They offer the advantage of increased potency with fewer adverse effects, compared with those for nonselective PDE inhibitors.

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