Activation of endothelial guanylate cyclase inhibits cellular reactivity

R. Heller; F. Bussolino; D. Ghigo; G. P. Pescarmona; R. Calvino; A. Gasco; U. Till; A. Bosia

Activation of endothelial guanylate cyclase inhibits cellular reactivity

R. Heller, F. Bussolino, D. Ghigo, G. P. Pescarmona, R. Calvino, A. Gasco, U. Till, A. Bosia

Istituto Oncologico Candiolo

Research output: Contribution to journal › Article › peer-review

Abstract

The study shows that endothelial cells from human umbilical veins have a soluble guanylate cyclase which can be activated by sodium nitroprusside (SNP), SIN-1 (3-morpholinosydnonimine) and S35b (4-methyl-3-phenylsulfonylfuroxan). Cells which were pretreated with these compounds showed an inhibition of thrombin-induced arachidonic acid release, PGI ₂ formation, PAF synthesis and PMNL adhesion. Endothelial guanylate cyclase can also be activated by nitric oxide (NO) which is generated in endothelial cells upon stimulation with thrombin or ionomycin. It is suggested that endogenously produced NO might control cell activation and endothelial function through a cGMP-dependent mechanism.

Original language	English
Pages (from-to)	177-181
Number of pages	5
Journal	Agents and Actions
Volume	45
Issue number	SUPPL. I
Publication status	Published - 1995

ASJC Scopus subject areas

Pharmacology (medical)
Toxicology

Cite this

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abstract = "The study shows that endothelial cells from human umbilical veins have a soluble guanylate cyclase which can be activated by sodium nitroprusside (SNP), SIN-1 (3-morpholinosydnonimine) and S35b (4-methyl-3-phenylsulfonylfuroxan). Cells which were pretreated with these compounds showed an inhibition of thrombin-induced arachidonic acid release, PGI 2 formation, PAF synthesis and PMNL adhesion. Endothelial guanylate cyclase can also be activated by nitric oxide (NO) which is generated in endothelial cells upon stimulation with thrombin or ionomycin. It is suggested that endogenously produced NO might control cell activation and endothelial function through a cGMP-dependent mechanism.",

author = "R. Heller and F. Bussolino and D. Ghigo and Pescarmona, {G. P.} and R. Calvino and A. Gasco and U. Till and A. Bosia",

year = "1995",

language = "English",

volume = "45",

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journal = "Inflammation Research",

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T1 - Activation of endothelial guanylate cyclase inhibits cellular reactivity

AU - Heller, R.

AU - Bussolino, F.

AU - Ghigo, D.

AU - Pescarmona, G. P.

AU - Calvino, R.

AU - Gasco, A.

AU - Till, U.

AU - Bosia, A.

PY - 1995

Y1 - 1995

N2 - The study shows that endothelial cells from human umbilical veins have a soluble guanylate cyclase which can be activated by sodium nitroprusside (SNP), SIN-1 (3-morpholinosydnonimine) and S35b (4-methyl-3-phenylsulfonylfuroxan). Cells which were pretreated with these compounds showed an inhibition of thrombin-induced arachidonic acid release, PGI 2 formation, PAF synthesis and PMNL adhesion. Endothelial guanylate cyclase can also be activated by nitric oxide (NO) which is generated in endothelial cells upon stimulation with thrombin or ionomycin. It is suggested that endogenously produced NO might control cell activation and endothelial function through a cGMP-dependent mechanism.

AB - The study shows that endothelial cells from human umbilical veins have a soluble guanylate cyclase which can be activated by sodium nitroprusside (SNP), SIN-1 (3-morpholinosydnonimine) and S35b (4-methyl-3-phenylsulfonylfuroxan). Cells which were pretreated with these compounds showed an inhibition of thrombin-induced arachidonic acid release, PGI 2 formation, PAF synthesis and PMNL adhesion. Endothelial guanylate cyclase can also be activated by nitric oxide (NO) which is generated in endothelial cells upon stimulation with thrombin or ionomycin. It is suggested that endogenously produced NO might control cell activation and endothelial function through a cGMP-dependent mechanism.

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AN - SCOPUS:0028843227

SN - 1023-3830

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JF - Inflammation Research

IS - SUPPL. I

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Activation of endothelial guanylate cyclase inhibits cellular reactivity

Abstract

ASJC Scopus subject areas

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