Interaction of diazoxide, tolbutamide and ATP4− on nucleotide-dependent K+ channels in an insulin-secreting cell line

1987 ◽  
Vol 99 (3) ◽  
pp. 215-224 ◽  
Author(s):  
M. J. Dunne ◽  
M. C. Illot ◽  
O. H. Petersen
Keyword(s):  
Cell Line ◽  
Secreting Cell ◽  
K Channels

The expression and regulation of depolarization-activated K+ channels in the insulin-secreting cell line INS-1

2001 ◽  
Vol 442 (1) ◽  
pp. 49-56 ◽  
Author(s):  
Jiping Su ◽  
Huang Yu ◽  
Nibedita Lenka ◽  
Jürgen Hescheler ◽  
Susanne Ullrich
Keyword(s):  
Cell Line ◽  
Secreting Cell ◽  
K Channels

scholarly journals Ca2+-activated K+ channels from an insulin-secreting cell line incorporated into planar lipid bilayers

Diabetologia ◽  
1992 ◽  
Vol 35 (7) ◽  
pp. 619-623 ◽  
Author(s):  
Y. Oosawa ◽  
S. J. H. Ashcroft ◽  
F. M. Ashcroft
Keyword(s):  
Cell Line ◽  
Lipid Bilayers ◽  
Planar Lipid Bilayers ◽  
Secreting Cell ◽  
K Channels

Role of tyrosine kinase in insulin release in an insulin secreting cell line (INS-1)

1995 ◽  
Vol 7 (5) ◽  
pp. 505-512 ◽  
Author(s):  
E.J. Verspohl ◽  
B. Tollkühn ◽  
H. Kloss
Keyword(s):  
Tyrosine Kinase ◽  
Cell Line ◽  
Insulin Release ◽  
Secreting Cell

alpha-Glycerophosphate shuttle in a clonal beta-cell line

1989 ◽  
Vol 256 (1) ◽  
pp. E173-E178 ◽  
Author(s):  
M. D. Meglasson ◽  
K. M. Smith ◽  
D. Nelson ◽  
M. Erecinska
Keyword(s):  
Insulin Secretion ◽  
Cell Line ◽  
Electron Transport Chain ◽  
Direct Evidence ◽  
Mitochondrial Fraction ◽  
Secreting Cell ◽  
Transport Chain ◽  
Beta Cell Line ◽  
Atp Generation ◽  
Hit Cells

It has been proposed that the alpha-glycerophosphate (alpha-GOP) shuttle plays a crucial role in regulation of glycolysis in beta-cells by linking reoxidation of cytosolic NADH to formation of ATP in the electron transport chain (J. Biol. Chem. 265: 8287, 1981). Direct evidence for this suggestion is still lacking, however. In this work the operation of the alpha-GOP shuttle was investigated in the insulin-secreting cell line HIT-T15. The constituent enzymes of the pathway were found to be present in HIT cells. Flavin-linked alpha-GOP dehydrogenase was associated with the mitochondrial fraction, whereas NAD+-dependent alpha-GOP dehydrogenase was localized in the cytosol. In the presence of amobarbital (used to preserve the function of the alpha-GOP shuttle under conditions where oxidation of NADH by the respiratory chain was blocked), glucose increased insulin secretion, O2 consumption, and the cell [ATP]/[ADP] when compared with amobarbital alone. These results indicate that the alpha-GOP shuttle contributes to ATP generation in HIT cells and that its activation may be necessary for the initiation of insulin secretion by glucose.

scholarly journals Leptin activates ATP-sensitive potassium channels in the rat insulin-secreting cell line, CRI-G1

1997 ◽  
Vol 504 (3) ◽  
pp. 527-535 ◽  
Author(s):  
J. Harvey ◽  
F. McKenna ◽  
P. S. Herson ◽  
D. Spanswick ◽  
M. L. J. Ashford
Keyword(s):  
Potassium Channels ◽  
Cell Line ◽  
Secreting Cell

scholarly journals Changes in phospholipid metabolism induced by quinine, 4-aminopyridine and tetraethylammonium in the monocytic cell line THP1

1992 ◽  
Vol 282 (2) ◽  
pp. 443-446 ◽  
Author(s):  
C Pelassy ◽  
N Cattan ◽  
C Aussel
Keyword(s):  
Cell Line ◽  
Phospholipid Metabolism ◽  
Choline Transport ◽  
Monocytic Cell ◽  
Monocytic Cell Line ◽  
K Channels ◽  
Human Monocytic Cell Line ◽  
Human Monocytic Cell

Quinine, 4-aminopyridine and tetraethylammonium, three compounds generally used as effectors of K+ channels, strongly modify phospholipid metabolism. In the human monocytic cell line THP1, the three drugs enhanced the incorporation of [3H]serine into phosphatidylserine and that of [3H]inositol into phosphatidylinositol in the absence of significant changes in the uptake of the 3H labels. On the contrary, the biosynthesis of both phosphatidylcholine and phosphatidylethanolamine was strongly inhibited. This inhibition appeared to be mainly due to the inhibition of both [3H]choline and [3H]ethanolamine uptake by the cells, by impairment of choline transport in a competitive mode.

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