The role of guanyl nucleotide binding proteins in the formation of inositol phosphates in adrenal glomerulosa cells

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Abstract

A non-hydrolysable GTP analogue enhanced the formation of [3H]inositol polyphosphates in permeabilized adrenal glomerulosa cells. Pertussis toxin, which ADP-ribosylated Ni, failed to influence angiotensin-induced formation of 3H-labelled inositol phosphates and the incorporation of [32P]phosphate into phosphatidyl inositol and phosphatidic acid. These results show that Ni, is prescot and a G-protein activates phospholipase C also in glomerulosa cells, however, it is not Ni which couples angiotensin receptors to the enzyme.

Original languageEnglish
Pages (from-to)941-947
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume140
Issue number3
DOIs
Publication statusPublished - Nov 14 1986

Fingerprint

Zona Glomerulosa
Polyphosphates
Phosphatidic Acids
Angiotensin Receptors
Inositol Phosphates
Pertussis Toxin
Angiotensins
Type C Phospholipases
Inositol
Phosphatidylinositols
Guanosine Triphosphate
GTP-Binding Proteins
Adenosine Diphosphate
Carrier Proteins
Nucleotides
Phosphates
Phosphatidylinositol Phosphates
Enzymes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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AU - Mucsi, I.

AU - Hunyady, L.

AU - Catt, Kevin J.

AU - Spät, A.

PY - 1986/11/14

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AB - A non-hydrolysable GTP analogue enhanced the formation of [3H]inositol polyphosphates in permeabilized adrenal glomerulosa cells. Pertussis toxin, which ADP-ribosylated Ni, failed to influence angiotensin-induced formation of 3H-labelled inositol phosphates and the incorporation of [32P]phosphate into phosphatidyl inositol and phosphatidic acid. These results show that Ni, is prescot and a G-protein activates phospholipase C also in glomerulosa cells, however, it is not Ni which couples angiotensin receptors to the enzyme.

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