Cyclic AMP-dependent protein kinase stimulates the phosphorylation of phosphatidylinositol to phosphatidylinositol-4-monophosphate in a plasma membrane preparation from pig granulocytes

G. Farkas, A. Enyedi, B. Sarkadi, G. Gárdos, Z. Nagy, A. Faragó

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Abstract

Plasma membranes prepared from pig granulocytes were incubated in the presence of [γ-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated the incorporation of 32P into both the protein and lipid fractions of the membrane. The SDS gel-electrophoretic analysis of the 32P-labelled proteins showed that the protein kinase phosphorylated preferentially a 24000-Mr protein, though other 32P-labelled proteins were also detected. 32P-labelled membrane lipids were analysed in two different thin layer chromatographic systems. 32P-labelling was found exclusively in polyphosphoinositides. On addition of the protein kinase the 32P-labelling of both polyphosphoinositides was increased but a higher amount of phosphate was incorporated into phosphatidylinositol-4-phosphate than into phosphatidylinositol-4,5-bisphosphate.

Original languageEnglish
Pages (from-to)871-876
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume124
Issue number3
DOIs
Publication statusPublished - Nov 14 1984

Fingerprint

Phosphorylation
Cell membranes
Phosphatidylinositols
Cyclic AMP-Dependent Protein Kinases
Granulocytes
Swine
Cell Membrane
Phosphatidylinositol Phosphates
Membrane Lipids
Protein Kinases
Labeling
Proteins
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
Adenosine Triphosphate
Gels
Phosphates
Membranes
Lipids
phosphatidylinositol 4-phosphate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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abstract = "Plasma membranes prepared from pig granulocytes were incubated in the presence of [γ-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated the incorporation of 32P into both the protein and lipid fractions of the membrane. The SDS gel-electrophoretic analysis of the 32P-labelled proteins showed that the protein kinase phosphorylated preferentially a 24000-Mr protein, though other 32P-labelled proteins were also detected. 32P-labelled membrane lipids were analysed in two different thin layer chromatographic systems. 32P-labelling was found exclusively in polyphosphoinositides. On addition of the protein kinase the 32P-labelling of both polyphosphoinositides was increased but a higher amount of phosphate was incorporated into phosphatidylinositol-4-phosphate than into phosphatidylinositol-4,5-bisphosphate.",
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T1 - Cyclic AMP-dependent protein kinase stimulates the phosphorylation of phosphatidylinositol to phosphatidylinositol-4-monophosphate in a plasma membrane preparation from pig granulocytes

AU - Farkas, G.

AU - Enyedi, A.

AU - Sarkadi, B.

AU - Gárdos, G.

AU - Nagy, Z.

AU - Faragó, A.

PY - 1984/11/14

Y1 - 1984/11/14

N2 - Plasma membranes prepared from pig granulocytes were incubated in the presence of [γ-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated the incorporation of 32P into both the protein and lipid fractions of the membrane. The SDS gel-electrophoretic analysis of the 32P-labelled proteins showed that the protein kinase phosphorylated preferentially a 24000-Mr protein, though other 32P-labelled proteins were also detected. 32P-labelled membrane lipids were analysed in two different thin layer chromatographic systems. 32P-labelling was found exclusively in polyphosphoinositides. On addition of the protein kinase the 32P-labelling of both polyphosphoinositides was increased but a higher amount of phosphate was incorporated into phosphatidylinositol-4-phosphate than into phosphatidylinositol-4,5-bisphosphate.

AB - Plasma membranes prepared from pig granulocytes were incubated in the presence of [γ-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated the incorporation of 32P into both the protein and lipid fractions of the membrane. The SDS gel-electrophoretic analysis of the 32P-labelled proteins showed that the protein kinase phosphorylated preferentially a 24000-Mr protein, though other 32P-labelled proteins were also detected. 32P-labelled membrane lipids were analysed in two different thin layer chromatographic systems. 32P-labelling was found exclusively in polyphosphoinositides. On addition of the protein kinase the 32P-labelling of both polyphosphoinositides was increased but a higher amount of phosphate was incorporated into phosphatidylinositol-4-phosphate than into phosphatidylinositol-4,5-bisphosphate.

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