Adenine-nucleotide binding sites on the inositol 1,4,5-trisphosphate receptor bind caffeine, but not adenophostin A or cyclic ADP-ribose

Cell Calcium ◽  
1999 ◽  
Vol 25 (2) ◽  
pp. 143-152 ◽  
Author(s):  
K. Maes ◽  
L. Missiaen ◽  
J.B. Parys ◽  
I. Sienaert ◽  
G. Bultynck ◽  
...  
Keyword(s):  
Binding Sites ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Nucleotide Binding Sites ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
Adenophostin A ◽  
Trisphosphate Receptor

scholarly journals ADENINE NUCLEOTIDE-INDUCED CONTRACTION OF THE INNER MITOCHONDRIAL MEMBRANE

1973 ◽  
Vol 56 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Clinton D. Stoner ◽  
Howard D. Sirak
Keyword(s):  
Binding Sites ◽  
Mitochondrial Membrane ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Nucleotide Binding ◽  
Nucleotide Exchange ◽  
Inner Mitochondrial Membrane ◽  
Inner Membrane ◽  
Nucleotide Binding Sites ◽  
Bongkrekic Acid

In bovine heart mitochondria bongkrekic acid at concentrations as low as about 4 nmol/mg protein (a) completely inhibits phosphorylation of exogenous adenosine diphosphate (ADP) and dephosphorylation of exogenous adenosine triphosphate (ATP), (b) completely reverses atractyloside inhibition of inner membrane contraction induced by exogenous adenine nucleotides, and (c) decreases the amount of adenine nucleotide required to elicit maximal exogenous adenine nucleotide-induced inner membrane contraction to a level which appears to correspond closely with the concentration of contractile, exogenous adenine nucleotide binding sites Bongkrekic acid at concentrations greater than 4 nmol/mg protein induces inner membrane contraction which seems to depend on the presence of endogenous ADP and/or ATP. The findings appear to be consistent with the interpretations (a) that the inner mitochondrial membrane contains two types of contractile, adenine nucleotide binding sites, (b) that the two sites differ markedly with regard to adenine nucleotide affinity, (c) that the high affinity site is identical with the adenine nucleotide exchange carrier, (d) that the low affinity site is accessible exclusively to endogenous adenine nucleotides and is largely unoccupied in the absence of bongkrekic acid, and (e) that bongkrekic acid increases the affinity of both sites in proportion to the amount of the antibiotic bound to the inner membrane.

scholarly journals Functional Linkage of Adenine Nucleotide Binding Sites in Mammalian Muscle 6-Phosphofructokinase

2012 ◽  
Vol 287 (21) ◽  
pp. 17546-17553 ◽  
Author(s):  
Antje Brüser ◽  
Jürgen Kirchberger ◽  
Marco Kloos ◽  
Norbert Sträter ◽  
Torsten Schöneberg
Keyword(s):  
Binding Sites ◽  
Adenine Nucleotide ◽  
Nucleotide Binding ◽  
Mammalian Muscle ◽  
Nucleotide Binding Sites ◽  
Functional Linkage
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