Lung phosphodiesterase isoenzymes

N J Pyne, F Burns

Research output: Contribution to journalLiterature review

7 Citations (Scopus)

Abstract

The distinct phosphodiesterase isoenzyme activities in guinea-pig lung were identified and characterised. We demonstrate that protein kinase A catalyses the activation of lung Type V cyclic GMP phosphodiesterase. This occurs via a marked change in the Vmax for cyclic GMP hydrolysis. The sensitivity of the activated PDE to inhibition by zaprinast is also markedly reduced (zaprinast inhibits in PDE activity via a mixed mechanism). We suggest that activation of the PDE by protein kinase A involves a mechanism that leads to alteration in the regulatory action of a non-catalytic cyclic GMP binding site.
LanguageEnglish
Pages35-49
Number of pages15
JournalAgents and actions. Supplements
Volume43
Publication statusPublished - 1993

Fingerprint

Cyclic GMP
Phosphoric Diester Hydrolases
Isoenzymes
Cyclic AMP-Dependent Protein Kinases
Lung
Guinea Pigs
Hydrolysis
Binding Sites
zaprinast

Keywords

  • 3',5'-Cyclic-GMP Phosphodiesterases
  • animals
  • catalysis
  • enzyme activation
  • Guinea Pigs
  • isoenzymes
  • lung
  • muscle
  • perfusion
  • phosphoric diester hydrolases
  • purinones
  • pyrazines

Cite this

Pyne, N J ; Burns, F. / Lung phosphodiesterase isoenzymes. In: Agents and actions. Supplements. 1993 ; Vol. 43. pp. 35-49.
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abstract = "The distinct phosphodiesterase isoenzyme activities in guinea-pig lung were identified and characterised. We demonstrate that protein kinase A catalyses the activation of lung Type V cyclic GMP phosphodiesterase. This occurs via a marked change in the Vmax for cyclic GMP hydrolysis. The sensitivity of the activated PDE to inhibition by zaprinast is also markedly reduced (zaprinast inhibits in PDE activity via a mixed mechanism). We suggest that activation of the PDE by protein kinase A involves a mechanism that leads to alteration in the regulatory action of a non-catalytic cyclic GMP binding site.",
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year = "1993",
language = "English",
volume = "43",
pages = "35--49",
journal = "Agents and actions. Supplements",
issn = "0379-0363",
publisher = "Birkhauser Verlag Basel",

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Lung phosphodiesterase isoenzymes. / Pyne, N J; Burns, F.

In: Agents and actions. Supplements, Vol. 43, 1993, p. 35-49.

Research output: Contribution to journalLiterature review

TY - JOUR

T1 - Lung phosphodiesterase isoenzymes

AU - Pyne, N J

AU - Burns, F

PY - 1993

Y1 - 1993

N2 - The distinct phosphodiesterase isoenzyme activities in guinea-pig lung were identified and characterised. We demonstrate that protein kinase A catalyses the activation of lung Type V cyclic GMP phosphodiesterase. This occurs via a marked change in the Vmax for cyclic GMP hydrolysis. The sensitivity of the activated PDE to inhibition by zaprinast is also markedly reduced (zaprinast inhibits in PDE activity via a mixed mechanism). We suggest that activation of the PDE by protein kinase A involves a mechanism that leads to alteration in the regulatory action of a non-catalytic cyclic GMP binding site.

AB - The distinct phosphodiesterase isoenzyme activities in guinea-pig lung were identified and characterised. We demonstrate that protein kinase A catalyses the activation of lung Type V cyclic GMP phosphodiesterase. This occurs via a marked change in the Vmax for cyclic GMP hydrolysis. The sensitivity of the activated PDE to inhibition by zaprinast is also markedly reduced (zaprinast inhibits in PDE activity via a mixed mechanism). We suggest that activation of the PDE by protein kinase A involves a mechanism that leads to alteration in the regulatory action of a non-catalytic cyclic GMP binding site.

KW - 3',5'-Cyclic-GMP Phosphodiesterases

KW - animals

KW - catalysis

KW - enzyme activation

KW - Guinea Pigs

KW - isoenzymes

KW - lung

KW - muscle

KW - perfusion

KW - phosphoric diester hydrolases

KW - purinones

KW - pyrazines

M3 - Literature review

VL - 43

SP - 35

EP - 49

JO - Agents and actions. Supplements

T2 - Agents and actions. Supplements

JF - Agents and actions. Supplements

SN - 0379-0363

ER -