Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane

B. Sarkadi, A. Enyedi, A. Faragó, G. Mészáros, T. Kremmer, G. Gárdos

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Inside-out vesicles from lymphocyte plasma membrane were phosphorylated in the presence of [γ-32P]ATP. The dissociated catalytic subunit of cyclic AMP-dependent protein kinase stimulated both membrane protein and membrane lipid phosphorylation, indicating the presence of a phosphorylation cascade. The phosphorylated membrane lipids were analyzed by thin-layer chromatography. Increase of 32P-labelling stimulated by the cyclic AMP-dependent protein kinase was found exclusively in polyphosphoinositides.

Original languageEnglish
Pages (from-to)195-198
Number of pages4
JournalFEBS Letters
Volume152
Issue number2
DOIs
Publication statusPublished - Feb 21 1983

Fingerprint

Phosphatidylinositol Phosphates
Phosphorylation
Lymphocytes
Cell membranes
Membrane Lipids
Cyclic AMP-Dependent Protein Kinases
Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
Cell Membrane
Thin layer chromatography
Thin Layer Chromatography
Labeling
Membrane Proteins
Adenosine Triphosphate

Keywords

  • Cyclic AMP
  • Lymphocyte
  • Membrane phosphorylation
  • Phosphatidylinositol metabolism
  • Polyphosphoinositide
  • Protein kinase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Cyclic AMP-dependent protein kinase stimulates the formation of polyphosphoinositides in lymphocyte plasma membrane. / Sarkadi, B.; Enyedi, A.; Faragó, A.; Mészáros, G.; Kremmer, T.; Gárdos, G.

In: FEBS Letters, Vol. 152, No. 2, 21.02.1983, p. 195-198.

Research output: Contribution to journalArticle

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AU - Kremmer, T.

AU - Gárdos, G.

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