Metabolism of Phosphatidylinositol in Reticulocytes — Isoproterenol Affects the Turnover of Polyphosphoinositides View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1987

AUTHORS

Dieter Maretzki , Barbara Reimann , Evelin Schwartzer , Milosav Kostic , Samuel Rapoport

ABSTRACT

Pulse-chase experiments with rabbit reticulocytes and erythrocytes prelabelled with inorganic 32P-phosphate revealed a high turnover of the phosphomonoester groups of polyphosphoinositides in reticulocytes which declines strongly during maturation. Reticulocytes incorporated H-inositol into phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP) and phosphatidylinositol-4, 5-bisphosphate (PIP2) in the proportion of 17: 1: 1.8, respectively. A slow release of 3H-labelled inositol phosphates was found in reticulocytes, indicating a very low phosphodiesterase activity (Phospholipase C) in the intact cells. Determination of the 32P/3H-ratio in double-labelled phosphatidylinositides in reticulocytes demonstrated an about 3000-fold turnover of the phosphodiester groups as compared with that of the phosphgdiester group. (-)-isoproterenol stimulates the incorporation of 32P-phosphate into the polyphosphoinositides in reticulocytes but did not influence the release of 3H-inositol phosphates. A rapid response to (-)-iso-proterenol (0.1 uM) with an increase of up to 60% was found in the 32P-labelling of PIP2. The effect was antagonized by alprenolol. The stimulation of the polyphosphoinositide phosphate turnover might be mediated by an elevated concentration of cyclic AMP in reticulocytes. More... »

PAGES

311-316

Book

TITLE

Signal Transduction and Protein Phosphorylation

ISBN

978-1-4757-0168-5
978-1-4757-0166-1

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4757-0166-1_40

DOI

http://dx.doi.org/10.1007/978-1-4757-0166-1_40

DIMENSIONS

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