PMID- 1903188
OWN - NLM
STAT- MEDLINE
DCOM- 19910619
LR  - 20190725
IS  - 0028-1298 (Print)
IS  - 0028-1298 (Linking)
VI  - 343
IP  - 1
DP  - 1991 Jan
TI  - Phosphate and thiophosphate group donating adenine and guanine nucleotides 
      inhibit glibenclamide binding to membranes from pancreatic islets.
PG  - 83-9
AB  - In microsomes obtained from mouse pancreatic islets, the Mg complex of adenosine 
      5'-triphosphate (MgATP) increased the dissociation constant (KD) for binding of 
      [3H]glibenclamide by sixfold. In the presence of Mg2+, not only ATP but also 
      adenosine 5'-0-(3-thiotriphosphate) (ATP gamma S), adenosine 5'-diphosphate 
      (ADP), guanosine 5'-triphosphate (GTP), guanosine 5'-diphosphate (GDP), guanosine 
      5'-0-(3-thiotriphosphate) (GTP gamma S) and guanosine 5'-0-(2-thiodiphosphate) 
      (GDP beta S) inhibited binding of [3H]glibenclamide. These effects were not 
      observed in the absence of Mg2+. Half maximally effective concentrations of the 
      Mg complexes of ATP, ADP, ATP gamma S and GDP were 11.6, 19.0, 62.3 and 90.1 
      mumol/l, respectively. The non-hydrolyzable analogues adenosine 
      5'-(beta,gamma-imidotriphosphate) (AMP-PNP) and guanosine 
      5'-(beta,gamma-imidotriphosphate) (GMP-PNP) did not alter [3H]glibenclamide 
      binding in the presence of Mg2+, MgADP acted much more slowly than MgATP and both 
      MgADP and MgGDP did not inhibit [3H]glibenclamide binding when the concentrations 
      of MgATP and MgGTP were kept low by the hexokinase reaction. Development of 
      MgATP-induced inhibition of [3H]glibenclamide binding and dissociation of 
      [3H]glibenclamide binding occurred at similar rates. However, the reversal of 
      MgATP-induced inhibition of [3H]glibenclamide binding was slower than the 
      association of [3H]glibenclamide with its binding site. Exogenous alkaline 
      phosphatase accelerated the reversal of MgATP-induced inhibition of 
      [3H]glibenclamide binding. MgATP enhanced displacement of [3H]glibenclamide 
      binding by diazoxide. The data suggest that sulfonylureas and diazoxide exert 
      their effects by interaction with the same binding site at the sulfonylurea 
      receptor and that protein phosphorylation modulates the affinity of the receptor.
FAU - Schwanstecher, M
AU  - Schwanstecher M
AD  - Institut fur Pharmakologie und Toxikologie, Universitat Gottingen, Federal 
      Republic of Germany.
FAU - Loser, S
AU  - Loser S
FAU - Rietze, I
AU  - Rietze I
FAU - Panten, U
AU  - Panten U
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Germany
TA  - Naunyn Schmiedebergs Arch Pharmacol
JT  - Naunyn-Schmiedeberg's archives of pharmacology
JID - 0326264
RN  - 0 (Adenine Nucleotides)
RN  - 0 (Guanine Nucleotides)
RN  - 0 (Organothiophosphates)
RN  - 0 (Phosphates)
RN  - 10028-17-8 (Tritium)
RN  - 146-91-8 (Guanosine Diphosphate)
RN  - 61D2G4IYVH (Adenosine Diphosphate)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - I38ZP9992A (Magnesium)
RN  - O5CB12L4FN (Diazoxide)
RN  - SX6K58TVWC (Glyburide)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Adenine Nucleotides/*pharmacology
MH  - Adenosine Diphosphate/pharmacology
MH  - Adenosine Triphosphate/pharmacology
MH  - Animals
MH  - Binding, Competitive
MH  - Calcium/pharmacology
MH  - Diazoxide/metabolism
MH  - Glyburide/*metabolism
MH  - Guanine Nucleotides/*pharmacology
MH  - Guanosine Diphosphate/pharmacology
MH  - Guanosine Triphosphate/pharmacology
MH  - Islets of Langerhans/*metabolism/ultrastructure
MH  - Kinetics
MH  - Magnesium/pharmacology
MH  - Membranes/metabolism
MH  - Mice
MH  - Microsomes/metabolism
MH  - Organothiophosphates/*pharmacology
MH  - Phosphates/*pharmacology
MH  - Phosphorylation
MH  - Tritium
EDAT- 1991/01/01 00:00
MHDA- 1991/01/01 00:01
CRDT- 1991/01/01 00:00
PHST- 1991/01/01 00:00 [pubmed]
PHST- 1991/01/01 00:01 [medline]
PHST- 1991/01/01 00:00 [entrez]
AID - 10.1007/BF00180681 [doi]
PST - ppublish
SO  - Naunyn Schmiedebergs Arch Pharmacol. 1991 Jan;343(1):83-9. doi: 
      10.1007/BF00180681.