Hydrolysis of cyclic GMP in rat peritoneal macrophages.

• Authors: Hanna Witwicka , Marcin Kobiałka , Wojciech A Gorczyca
• Languages of publication: EN

Abstracts

EN

Intact rat peritoneal macrophages (rPM) treated with 3-isobutyl-1-methylxanthine (IBMX), an inhibitor of phosphodiesterases (PDEs), accumulated more cGMP than untreated cells. A PDE activity toward [3H]cGMP was detected in the soluble and particulate fractions of rPM. The hydrolysis of cGMP was Ca2+/calmodulin-independent but increased in the presence of cGMP excess. Similar results were obtained when [3H]cAMP was used as a substrate. The hydrolytic activity towards both nucleotides was inhibited in the presence of IBMX. Therefore, the PDEs of families 2, 5, 10 and 11 are potential candidates for cGMP hydrolysis in the rPM. They may not only regulate the cGMP level in a feedback-controlled way but also link cGMP-dependent pathways with those regulated by cAMP.

Keywords

EN

signal transduction; phosphodiesterases; cyclic nucleotides; macrophages

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2002
• Volume: 49
• Issue: 4
• Pages: 891-897

Dates

published

2002

received

2002-10-19

revised

2002-11-20

accepted

2002-11-21

Contributors

author

Hanna Witwicka

• Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Marcin Kobiałka

• Laboratory of Signaling Proteins, L. Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław, Poland

author

Wojciech A Gorczyca

• Department of Biogenic Amines, Łódź, Poland

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