Literature DB >> 8554311

G-protein-sensitive guanylyl cyclase activity associated with plasma membranes.

I Lippo de Bécemberg1, M F Correa de Adjounian, S Sánchez de Villaroel, E Peña de Aguilar, R González de Alfonzo, M Alfonzo.   

Abstract

A mammalian plasma-membrane-bound guanylyl cyclase is inhibited by NaCl and this inhibition is dependent on GTP concentrations and independent of the chloride salt type. This chloride inhibition is reversed by GTP analogs such as GTP gamma S, suggesting the involvement of G proteins. When the ability of bacterial toxins to affect this chloride-sensitive guanylyl cyclase was examined, pertussis toxin decreased the basal activity and the chloride sensitivity was greatly reduced. Cholera toxin induced a slight activation of the basal activity, without significant changes in the NaCl inhibition. These data indicate that G proteins regulate the chloride sensitivity of this guanylyl cyclase activity. Another property described here is the ability of ATP and analogs to inhibit the basal activity. However, these nucleotides did not modify the chloride sensitivity of the membrane-bound guanylyl cyclase activity.

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Year:  1995        PMID: 8554311     DOI: 10.1006/abbi.1995.0032

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  1 in total

1.  Role of the M2 muscarinic receptor pathway in lidocaine-induced potentiation of the relaxant response to atrial natriuretic peptide in bovine tracheal smooth muscle.

Authors:  Motonari Yunoki; Tsutomu Nakahara; Akiko Mitani; Kenji Sakamoto; Kunio Ishii
Journal:  Naunyn Schmiedebergs Arch Pharmacol       Date:  2002-11-30       Impact factor: 3.000

  1 in total

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