cGMP-Phosphodiesterase Activity Is Up-regulated in Response to Pressure Overload of Rat Ventricles | Zendy

Noriyuki Yanaka | Zendy; Yukie Kurosawa | Zendy; Kouichi Minami | Zendy; Eri Kawai | Zendy; Kenji Omori | Zendy

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cGMP-Phosphodiesterase Activity Is Up-regulated in Response to Pressure Overload of Rat Ventricles

Author(s) -

Noriyuki Yanaka,

Yukie Kurosawa,

Kouichi Minami,

Eri Kawai,

Kenji Omori

Publication year - 2003

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.67.973

Subject(s) - phosphodiesterase , pressure overload , medicine , endocrinology , phosphodiesterase 3 , left ventricles , gene isoform , calmodulin , cyclic nucleotide phosphodiesterase , pde10a , chemistry , ventricular pressure , messenger rna , biology , blood pressure , calcium , enzyme , muscle hypertrophy , biochemistry , cardiac hypertrophy , gene , ventricle

Although expression of natriuretic peptides in cardiac tissues is up-regulated in response to pressure overload, no significant change in cGMP level in hypertrophied ventricles was observed. Activities of two cyclic nucleotide phosphodiesterase (PDE) isoforms, Ca2+/calmodulin-stimulated PDE (PDE1) and cGMP-stimulated PDE (PDE2), were significantly higher in rat left ventricles 14 days after aortic banding. The absence of significant changes in PDE1A and PDE2A mRNA levels indicated that the two PDE activities were post-transcriptionally up-regulated. These results suggested that the increased cGMP-PDE activity in response to pressure overload plays an important role in neutralizing cGMP action in cardiac tissue.

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