Localization of felodipine (dihydropyridine) binding site on calmodulin

Biochemistry ◽  
1986 ◽  
Vol 25 (8) ◽  
pp. 2226-2231 ◽  
Author(s):  
J. David Johnson ◽  
Laura A. Wittenauer ◽  
Eva Thulin ◽  
Sture Forsen ◽  
Hans J. Vogel
Keyword(s):  
Binding Site ◽  
Dihydropyridine Binding Site

scholarly journals A novel 1,4-dihydropyridine-binding site on mitochondrial membranes from guinea-pig heart, liver and kidney

1988 ◽  
Vol 253 (1) ◽  
pp. 49-58 ◽  
Author(s):  
G Zernig ◽  
H Glossmann
Keyword(s):  
Guinea Pig ◽  
Binding Site ◽  
Binding Sites ◽  
Ph Dependence ◽  
High Capacity ◽  
Mitochondrial Membranes ◽  
Guinea Pig Heart ◽  
Heat Stable ◽  
Liver And Kidney ◽  
Dihydropyridine Binding Site

The 1,4-dihydropyridine (+/-)-[3H]nitrendipine reversibly binds to mitochondrial preparations from guinea-pig heart with a dissociation constant (Kd) of 593 +/- 77 nM and a maximum density of binding sites (Bmax.) of 1.75 +/- 0.27 nmol/mg of protein. This low-affinity high-capacity 1,4-dihydropyridine-binding site does not discriminate between the enantiomers of nitrendipine and is also found in mitochondrial membranes from guinea-pig liver (Kd 586 +/- 91 nM; Bmax. 0.36 +/- 0.04 nmol/mg of protein) and kidney (Kd 657 +/- 149 nM; Bmax. 0.56 +/- 0.12 nmol/mg of protein). Phenylalkylamines (e.g. verapamil) inhibit (+/-)-[3H]nitrendipine binding with micromolar inhibition constants, but the benzothiazepine D-cis-diltiazem, a potent Ca2+-channel blocker, is without effect. The binding is heat-stable, shows a V-shaped pH-dependence with a minimum around pH 7.0, and is strongly dependent on ionic strength in the incubation medium. The cations La3+ greater than Cd2+ much greater than Co2+ greater than Ca2+ much greater than Ba2+ greater than Mg2+ greater than Li+ greater than Na+ and the anions NO3- greater than C1- greater than or equal to F- stimulate the binding, whereas PO4(3-) greater than SO4(2-) slightly inhibit it. The low-affinity (+/-)-[3H]nitrendipine-binding site located on the mitochondrial inner membrane is biochemically and pharmacologically different from the 1,4-dihydropyridine-receptor domain of the L-type Ca2+ channel. Furthermore, it is not identical with any of the low-affinity 1,4-dihydropyridine-binding sites described so far.

scholarly journals Motif III S5 of L-type Calcium Channels Is Involved in the Dihydropyridine Binding Site

1997 ◽  
Vol 272 (5) ◽  
pp. 2629-2633 ◽  
Author(s):  
Ming He ◽  
Ilona Bodi ◽  
Gabor Mikala ◽  
Arnold Schwartz
Keyword(s):  
Calcium Channels ◽  
Binding Site ◽  
Dihydropyridine Binding Site

A functional correlate for the dihydropyridine binding site in rat brain

Nature ◽  
1985 ◽  
Vol 314 (6006) ◽  
pp. 94-96 ◽  
Author(s):  
D. N. Middlemiss ◽  
M. Spedding
Keyword(s):  
Binding Site ◽  
Rat Brain ◽  
Dihydropyridine Binding Site

Purified dihydropyridine-binding site from skeletal muscle t-tubules is a functional calcium channel

Nature ◽  
1986 ◽  
Vol 323 (6083) ◽  
pp. 66-68 ◽  
Author(s):  
Veit Flockerzi ◽  
Hans-Jochem Oeken ◽  
Franz Hofmann ◽  
Dieter Pelzer ◽  
Adolfo Cavalié ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Calcium Channel ◽  
Binding Site ◽  
T Tubules ◽  
Dihydropyridine Binding Site
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