A cromoglycate binding protein from rat mast cells of a leukemia line is a nucleoside diphosphate kinase

Biochemistry ◽  
1992 ◽  
Vol 31 (19) ◽  
pp. 4574-4579 ◽  
Author(s):  
Stefan Hemmerich ◽  
Yosef Yarden ◽  
Israel Pecht
1992 ◽  
Vol 288 (1) ◽  
pp. 181-187 ◽  
Author(s):  
T H W Lillie ◽  
B D Gomperts

Exocytosis from metabolically depleted permeabilized rat mast cells was measured in response to provision of Ca2+ and guanine nucleotide [GTP or guanosine 5′-[gamma-thio]triphosphate (GTP[S])]. For cells permeabilized in simple salt solutions (NaCl), both of these effectors were required to induce secretion. Exclusion of Mg2+ caused an increase in both the sensitivity of the system to GTP and the extent of secretion elicited, while having no such effects on secretion induced by GTP[S]. The effect of Mg2+ depletion on the ability of GTP to stimulate secretion is probably due to the dependence on Mg2+ of the GTPase activity of GE (a postulated GTP-binding protein which mediates exocytosis). This argues that a persistent stimulus to the G-protein is required to support secretion. Affinity for both GTP[S] and GTP is enhanced when the cells are permeabilized in zwitterionic electrolytes (glutamate, gamma-aminobutyric acid, glycine) instead of NaCl. Under these conditions, secretion occurs in response to provision of either GTP[S] [in the effective absence of Ca2+ (pCa 9)] or Ca2+ (in the absence of guanine nucleotide). Secretion induced by GTP[S] is strongly promoted by the presence of Mg2+ at concentrations in the millimolar range; this promotion by Mg2+ declines as the concentration of Ca2+ is elevated towards pCa 7. At pCa 6, Mg2+ is without effect. Ca(2+)-induced secretion requires the provision of MgATP. Since this is further enhanced by low concentrations (< 100 microM) and then inhibited by high concentrations of GDP, the essential role of ATP is likely to be in the maintenance of GTP via transphosphorylation by a nucleoside diphosphate kinase reaction. Thus, under conditions of high affinity (glutamate environment), GTP[S] alone is capable of inducing exocytosis. Ca2+ acts in concert with guanine nucleotides: it enhances the rate and extent of secretion and increases the affinity for Mg2+ and guanine nucleotides in the activation of the GTP-binding protein (GE) which regulates exocytosis.


FEBS Letters ◽  
1991 ◽  
Vol 287 (1-2) ◽  
pp. 15-18 ◽  
Author(s):  
Ichiro Fujimoto ◽  
Kazuhiro Ikenaka ◽  
Tetsuro Kondo ◽  
Saburo Aimoto ◽  
Miyuki Kuno ◽  
...  

1976 ◽  
Vol 13 (4) ◽  
pp. 345-353 ◽  
Author(s):  
Wolfgang König ◽  
Kimishige Ishizaka
Keyword(s):  

1995 ◽  
Vol 7 (2) ◽  
pp. 251-258 ◽  
Author(s):  
Masahiko Yasuda ◽  
Yukihito Hasunuma ◽  
Hiroyasu Adachi ◽  
Chiyoko Sekine ◽  
Tamami Sakanishi ◽  
...  

1992 ◽  
Vol 29 (6) ◽  
pp. 495-498 ◽  
Author(s):  
L. M. Botana ◽  
E. Arnaez ◽  
M. R. Vieytes ◽  
A. Alfonso ◽  
M. J. Bujan ◽  
...  

1987 ◽  
Vol 105 (1) ◽  
pp. 191-197 ◽  
Author(s):  
T W Howell ◽  
S Cockcroft ◽  
B D Gomperts

Rat mast cells, pretreated with metabolic inhibitors and permeabilized by streptolysin-O, secrete histamine when provided with Ca2+ (buffered in the micromolar range) and nucleoside triphosphates. We have surveyed the ability of various exogenous nucleotides to support or inhibit secretion. The preferred rank order in support of secretion is ITP greater than XTP greater than GTP much greater than ATP. Pyrimidine nucleotides (UTP and CTP) are without effect. Nucleoside diphosphates included alongside Ca2+ plus ITP inhibit secretion in the order 2'-deoxyGDP greater than GDP greater than o-GDP greater than ADP approximately equal to 2'deoxyADP approximately equal to IDP. Secretion from the metabolically inhibited and permeabilized cells can also be induced by stable analogues of GTP (GTP-gamma-S greater than GppNHp greater than GppCH2p) which synergize with Ca2+ to trigger secretion in the absence of phosphorylating nucleotides. ATP enhances the effective affinity for Ca2+ and GTP analogues in the exocytotic process but does not alter the maximum extent of secretion. The results suggest that the presence of Ca2+ combined with activation of events controlled by a GTP regulatory protein provide a sufficient stimulus to exocytotic secretion from mast cells.


Author(s):  
A. M. Rothschild ◽  
M. P. O. Antonio ◽  
J. J. Dias ◽  
A. Castania ◽  
L. C. Neves
Keyword(s):  

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