Protein kinase C inhibits the Ca(2+)-dependent stimulation of phospholipase C-beta 1 in vitro.

I. Litosch

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

Protein kinase C (PKC) inhibited the Ca(2+)-dependent stimulation of a 600-fold purified phospholipase C beta 1 (PLC-beta 1). Inhibition by PKC was time-dependent, and required ATP and diacylglycerol. Inhibition was more pronounced when the PLC assay was conducted with a PIP2 substrate mixture containing phosphatidylserine, then with a substrate mixture containing phosphatidyle-thanolamine. Cyclic AMP-dependent protein kinase A did not inhibit PLC-beta 1 activity. PKC did not affect the rate of PLC-beta 1 activation by Ca2+ or the rate of PLC-beta 1 deactivation by EGTA. PLC-beta 1 purified 1700-fold was less sensitive to inhibition by PKC despite stoichiometric phosphorylation. These results demonstrate that PKC inhibits the Ca(2+)-dependent stimulation of a 600-fold purified PLC-beta 1 in vitro. Furthermore, purification of PLC-beta 1 to homogeneity results in a diminished sensitivity to inhibition by PKC, indicating that other components may participate in mediating the effect of PKC on the Ca(2+)-dependent stimulation of PLC-beta 1 in vitro.

Original languageEnglish
Pages (from-to)87-98
Number of pages12
JournalReceptors & signal transduction
Volume6
Issue number2
StatePublished - Dec 1 1996
Externally publishedYes

Fingerprint

Phospholipase C beta
Protein Kinase C
Cyclic AMP-Dependent Protein Kinases
In Vitro Techniques
Egtazic Acid
Phosphatidylserines
Diglycerides
Adenosine Triphosphate
Phosphorylation

Cite this

Protein kinase C inhibits the Ca(2+)-dependent stimulation of phospholipase C-beta 1 in vitro. / Litosch, I.

In: Receptors & signal transduction, Vol. 6, No. 2, 01.12.1996, p. 87-98.

Research output: Contribution to journalArticle

@article{06610bce7c1e432883230fdb6ababa38,
title = "Protein kinase C inhibits the Ca(2+)-dependent stimulation of phospholipase C-beta 1 in vitro.",
abstract = "Protein kinase C (PKC) inhibited the Ca(2+)-dependent stimulation of a 600-fold purified phospholipase C beta 1 (PLC-beta 1). Inhibition by PKC was time-dependent, and required ATP and diacylglycerol. Inhibition was more pronounced when the PLC assay was conducted with a PIP2 substrate mixture containing phosphatidylserine, then with a substrate mixture containing phosphatidyle-thanolamine. Cyclic AMP-dependent protein kinase A did not inhibit PLC-beta 1 activity. PKC did not affect the rate of PLC-beta 1 activation by Ca2+ or the rate of PLC-beta 1 deactivation by EGTA. PLC-beta 1 purified 1700-fold was less sensitive to inhibition by PKC despite stoichiometric phosphorylation. These results demonstrate that PKC inhibits the Ca(2+)-dependent stimulation of a 600-fold purified PLC-beta 1 in vitro. Furthermore, purification of PLC-beta 1 to homogeneity results in a diminished sensitivity to inhibition by PKC, indicating that other components may participate in mediating the effect of PKC on the Ca(2+)-dependent stimulation of PLC-beta 1 in vitro.",
author = "I. Litosch",
year = "1996",
month = "12",
day = "1",
language = "English",
volume = "6",
pages = "87--98",
journal = "Receptors & signal transduction",
issn = "1087-8475",
publisher = "Humana Press",
number = "2",

}

TY - JOUR

T1 - Protein kinase C inhibits the Ca(2+)-dependent stimulation of phospholipase C-beta 1 in vitro.

AU - Litosch, I.

PY - 1996/12/1

Y1 - 1996/12/1

N2 - Protein kinase C (PKC) inhibited the Ca(2+)-dependent stimulation of a 600-fold purified phospholipase C beta 1 (PLC-beta 1). Inhibition by PKC was time-dependent, and required ATP and diacylglycerol. Inhibition was more pronounced when the PLC assay was conducted with a PIP2 substrate mixture containing phosphatidylserine, then with a substrate mixture containing phosphatidyle-thanolamine. Cyclic AMP-dependent protein kinase A did not inhibit PLC-beta 1 activity. PKC did not affect the rate of PLC-beta 1 activation by Ca2+ or the rate of PLC-beta 1 deactivation by EGTA. PLC-beta 1 purified 1700-fold was less sensitive to inhibition by PKC despite stoichiometric phosphorylation. These results demonstrate that PKC inhibits the Ca(2+)-dependent stimulation of a 600-fold purified PLC-beta 1 in vitro. Furthermore, purification of PLC-beta 1 to homogeneity results in a diminished sensitivity to inhibition by PKC, indicating that other components may participate in mediating the effect of PKC on the Ca(2+)-dependent stimulation of PLC-beta 1 in vitro.

AB - Protein kinase C (PKC) inhibited the Ca(2+)-dependent stimulation of a 600-fold purified phospholipase C beta 1 (PLC-beta 1). Inhibition by PKC was time-dependent, and required ATP and diacylglycerol. Inhibition was more pronounced when the PLC assay was conducted with a PIP2 substrate mixture containing phosphatidylserine, then with a substrate mixture containing phosphatidyle-thanolamine. Cyclic AMP-dependent protein kinase A did not inhibit PLC-beta 1 activity. PKC did not affect the rate of PLC-beta 1 activation by Ca2+ or the rate of PLC-beta 1 deactivation by EGTA. PLC-beta 1 purified 1700-fold was less sensitive to inhibition by PKC despite stoichiometric phosphorylation. These results demonstrate that PKC inhibits the Ca(2+)-dependent stimulation of a 600-fold purified PLC-beta 1 in vitro. Furthermore, purification of PLC-beta 1 to homogeneity results in a diminished sensitivity to inhibition by PKC, indicating that other components may participate in mediating the effect of PKC on the Ca(2+)-dependent stimulation of PLC-beta 1 in vitro.

UR - http://www.scopus.com/inward/record.url?scp=0030346154&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030346154&partnerID=8YFLogxK

M3 - Article

C2 - 9015864

AN - SCOPUS:0030346154

VL - 6

SP - 87

EP - 98

JO - Receptors & signal transduction

JF - Receptors & signal transduction

SN - 1087-8475

IS - 2

ER -