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Hydrolysis-resistant analogues of GTP specifically stimulate the formation of [3H]inositol mono-, bis- and trisphosphates by saponin-permeabilized Swiss 3T3 cells prelabelled with [3H]inositol. Each inositol phosphate is formed largely by hydrolysis of its parent lipid and not by dephosphorylation of inositol 1,4,5-trisphosphate [(1,4,5)IP3]. Although hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) is most sensitive to guanine nucleotides, hydrolysis of phosphatidyl-inositol (PI) and phosphatidylinositol 4-phosphate (PIP) is quantitatively more important. These results suggest that a guanine nucleotide-dependent regulatory protein(s) (G-protein) is involved in regulating the hydrolysis of PI and PIP, as well as PIP2, and so may allow formation of diacylglycerol (DG) without simultaneous production of (1,4,5)IP3 and mobilization of intracellular Ca2+.
C W Taylor, and
D M Blakeley, and
K D Brown
March 1988,
The Biochemical journal,
C W Taylor, and
D M Blakeley, and
K D Brown
December 1988,
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C W Taylor, and
D M Blakeley, and
K D Brown
November 1986,
FEBS letters,
C W Taylor, and
D M Blakeley, and
K D Brown
April 1987,
Journal of biochemistry,
C W Taylor, and
D M Blakeley, and
K D Brown
May 1988,
The Journal of biological chemistry,
C W Taylor, and
D M Blakeley, and
K D Brown
January 1990,
The Biochemical journal,
C W Taylor, and
D M Blakeley, and
K D Brown
July 1989,
Biochemical and biophysical research communications,
C W Taylor, and
D M Blakeley, and
K D Brown
April 1987,
The Journal of biological chemistry,
C W Taylor, and
D M Blakeley, and
K D Brown
August 1987,
Life sciences,
C W Taylor, and
D M Blakeley, and
K D Brown
April 1991,
Biochemical Society transactions,
