Correlation between plasma membrane ATPase activity of mast cells and histamine secretion

1979 ◽  
Vol 9 (1) ◽  
pp. 62-63 ◽  
Author(s):  
N. Chakravarty
Keyword(s):  
Plasma Membrane ◽  
Mast Cells ◽  
Atpase Activity ◽  
Plasma Membrane Atpase ◽  
Histamine Secretion ◽  
Membrane Atpase

Change in plasma membrane ATPase activity during dormancy release of vegetative peach-tree buds

1999 ◽  
Vol 106 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Henri-Luc Aue ◽  
Isabelle Lecomte ◽  
Michel Gendraud ◽  
Gilles Pétel
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Dormancy Release ◽  
Peach Tree ◽  
Plasma Membrane Atpase ◽  
Membrane Atpase

Direct Action of Insulin on Plasma Membrane ATPase Activity in Human Lymphocytes

1972 ◽  
Vol 235 (58) ◽  
pp. 174-177 ◽  
Author(s):  
JOHN W. HADDEN ◽  
ELBA M. HADDEN ◽  
EDWIN E. WILSON ◽  
ROBERT A. GOOD ◽  
RONALD G. COFFEY
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Direct Action ◽  
Human Lymphocytes ◽  
Plasma Membrane Atpase ◽  
Membrane Atpase

Vanadate-resistant mutants of Saccharomyces cerevisiae show alterations in protein phosphorylation and growth control

1990 ◽  
Vol 10 (3) ◽  
pp. 898-909
Author(s):  
C Kanik-Ennulat ◽  
N Neff
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Atpase Activity ◽  
Protein Phosphorylation ◽  
Growth Control ◽  
Plasma Membrane Atpase ◽  
Membrane Atpase ◽  
Resistant Mutants ◽  
Diploid Cells

This work describes two spontaneous vanadate-resistant mutants of Saccharomyces cerevisiae with constitutive alterations in protein phosphorylation, growth control, and sporulation. Vanadate has been shown by a number of studies to be an efficient competitor of phosphate in biochemical reactions, especially those that involve phosphoproteins as intermediates or substrates. Resistance to toxic concentrations of vanadate can arise in S. cerevisiae by both recessive and dominant spontaneous mutations in a large number of loci. Mutations in two of the recessive loci, van1-18 and van2-93, resulted in alterations in the phosphorylation of a number of proteins. The mutant van1-18 gene also showed an increase in plasma membrane ATPase activity in vitro and a lowered basal phosphatase activity under alkaline conditions. Cells containing the van2-93 mutant allele had normal levels of plasma membrane ATPase activity, but this activity was not inhibited by vanadate. Both of these mutants failed to enter stationary phase, were heat shock sensitive, showed lowered long-term viability, and sporulated on rich medium in the presence of 2% glucose. The wild-type VAN1 gene was isolated and sequenced. The open reading frame predicts a protein of 522 amino acids, with no significant homology to any genes that have been identified. Diploid cells that contained two mutant alleles of this gene demonstrated defects in spore viability. These data suggest that the VAN1 gene product is involved in regulation of the phosphorylation of a number of proteins, some of which appear to be important in cell growth control.

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