The identification of apparently novel cyclic AMP and cyclic GMP phosphodiesterase activities in guinea-pig tracheal smooth muscle

F Burns, P A Stevens, N J Pyne

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Phosphodiesterase (PDE) activities that were capable of hydrolysing cyclic AMP (Km = 6.8 +/- 2 microM) and cyclic GMP (Km = 6.7 +/- 1.6 microM) were isolated from tracheal smooth muscle. These enzyme(s) activities were insensitive to stimulation by calcium/calmodulin and to inhibition by cyclic GMP, rolipram (type IV inhibitor) and siguazodan (type III inhibitor). Zaprinast was a relatively poor inhibitor of both cyclic AMP and cyclic GMP hydrolysis (IC50 = 46 +/- 9 microM and 45 +/- 14 microM respectively). These results suggest that tracheal smooth muscle may contain an apparently novel PDE. However, KCl (30 mM) which facilitates calcium entry in cells, depressed bradykinin-stimulated intracellular cyclic AMP formation, suggesting that the type I PDE may be functionally present. We suggest that considerable caution be exercised in identifying apparently novel PDE isoforms.
Original languageEnglish
Pages (from-to)3-4
Number of pages2
JournalBritish Journal of Pharmacology
Volume113
Issue number1
Publication statusPublished - Sep 1994

Fingerprint

Cyclic GMP
Phosphoric Diester Hydrolases
Cyclic AMP
Smooth Muscle
Guinea Pigs
Phosphodiesterase I
Rolipram
Calcium
Bradykinin
Calmodulin
Inhibitory Concentration 50
Protein Isoforms
Hydrolysis
Enzymes

Keywords

  • 3',5'-cyclic-AMP phosphodiesterases
  • 3',5'-cyclic-GMP phosphodiesterases
  • animals
  • bradykinin
  • guinea pigs
  • isoenzymes
  • muscle, smooth
  • potassium chloride
  • trachea

Cite this

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title = "The identification of apparently novel cyclic AMP and cyclic GMP phosphodiesterase activities in guinea-pig tracheal smooth muscle",
abstract = "Phosphodiesterase (PDE) activities that were capable of hydrolysing cyclic AMP (Km = 6.8 +/- 2 microM) and cyclic GMP (Km = 6.7 +/- 1.6 microM) were isolated from tracheal smooth muscle. These enzyme(s) activities were insensitive to stimulation by calcium/calmodulin and to inhibition by cyclic GMP, rolipram (type IV inhibitor) and siguazodan (type III inhibitor). Zaprinast was a relatively poor inhibitor of both cyclic AMP and cyclic GMP hydrolysis (IC50 = 46 +/- 9 microM and 45 +/- 14 microM respectively). These results suggest that tracheal smooth muscle may contain an apparently novel PDE. However, KCl (30 mM) which facilitates calcium entry in cells, depressed bradykinin-stimulated intracellular cyclic AMP formation, suggesting that the type I PDE may be functionally present. We suggest that considerable caution be exercised in identifying apparently novel PDE isoforms.",
keywords = "3',5'-cyclic-AMP phosphodiesterases, 3',5'-cyclic-GMP phosphodiesterases, animals, bradykinin, guinea pigs, isoenzymes, muscle, smooth, potassium chloride, trachea",
author = "F Burns and Stevens, {P A} and Pyne, {N J}",
year = "1994",
month = "9",
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volume = "113",
pages = "3--4",
journal = "British Journal of Pharmacology",
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The identification of apparently novel cyclic AMP and cyclic GMP phosphodiesterase activities in guinea-pig tracheal smooth muscle. / Burns, F; Stevens, P A; Pyne, N J.

In: British Journal of Pharmacology, Vol. 113, No. 1, 09.1994, p. 3-4.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The identification of apparently novel cyclic AMP and cyclic GMP phosphodiesterase activities in guinea-pig tracheal smooth muscle

AU - Burns, F

AU - Stevens, P A

AU - Pyne, N J

PY - 1994/9

Y1 - 1994/9

N2 - Phosphodiesterase (PDE) activities that were capable of hydrolysing cyclic AMP (Km = 6.8 +/- 2 microM) and cyclic GMP (Km = 6.7 +/- 1.6 microM) were isolated from tracheal smooth muscle. These enzyme(s) activities were insensitive to stimulation by calcium/calmodulin and to inhibition by cyclic GMP, rolipram (type IV inhibitor) and siguazodan (type III inhibitor). Zaprinast was a relatively poor inhibitor of both cyclic AMP and cyclic GMP hydrolysis (IC50 = 46 +/- 9 microM and 45 +/- 14 microM respectively). These results suggest that tracheal smooth muscle may contain an apparently novel PDE. However, KCl (30 mM) which facilitates calcium entry in cells, depressed bradykinin-stimulated intracellular cyclic AMP formation, suggesting that the type I PDE may be functionally present. We suggest that considerable caution be exercised in identifying apparently novel PDE isoforms.

AB - Phosphodiesterase (PDE) activities that were capable of hydrolysing cyclic AMP (Km = 6.8 +/- 2 microM) and cyclic GMP (Km = 6.7 +/- 1.6 microM) were isolated from tracheal smooth muscle. These enzyme(s) activities were insensitive to stimulation by calcium/calmodulin and to inhibition by cyclic GMP, rolipram (type IV inhibitor) and siguazodan (type III inhibitor). Zaprinast was a relatively poor inhibitor of both cyclic AMP and cyclic GMP hydrolysis (IC50 = 46 +/- 9 microM and 45 +/- 14 microM respectively). These results suggest that tracheal smooth muscle may contain an apparently novel PDE. However, KCl (30 mM) which facilitates calcium entry in cells, depressed bradykinin-stimulated intracellular cyclic AMP formation, suggesting that the type I PDE may be functionally present. We suggest that considerable caution be exercised in identifying apparently novel PDE isoforms.

KW - 3',5'-cyclic-AMP phosphodiesterases

KW - 3',5'-cyclic-GMP phosphodiesterases

KW - animals

KW - bradykinin

KW - guinea pigs

KW - isoenzymes

KW - muscle, smooth

KW - potassium chloride

KW - trachea

M3 - Article

VL - 113

SP - 3

EP - 4

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 1

ER -