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|Title:||Specific high-affinity binding sites for 125I-labelled porcine endothelin in rat cardiac membranes.|
|Authors:||Gu, X H;Casley, David J;Nayler, W|
|Affiliation:||Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australia.|
|Citation:||European Journal of Pharmacology; 167(2): 281-90|
|Abstract:||125I-labelled porcine endothelin (125I-endothelin) was used to identify specific high affinity endothelin binding sites in rat cardiac membrane fragments. Binding was to a single population of sites, with a KD of 0.20 +/- 0.03 nM and a Bmax of 93.5 +/- 6.4 fmol/mg protein at 37 degrees C. Reducing the temperature to 25 degrees C increased (P less than 0.02) the KD without changing Bmax. 125I-Endothelin binding was Ca2+ independent. Specific binding was saturable and displaceable by cold endothelin and sarafotoxin S6b, but not by (-)Bay K8644, nicardipine, (-)D888, (+)cis-diltiazem, prenylamine, lidoflazine, flunarizine, nor by 10(-10)-10(-4) M CoCl2, nor 10(-10)-10(-4) M NiCl2. omega-Conotoxin, prazosin, isoprenaline, angiotensin II and its inhibitor, vasopressin and its inhibitor, glyceryl trinitrate, amiloride, ergometrine and FII stonefish toxin also failed to displace bound 125I-endothelin. 10(-4)-10(-2) M CaCl2, 10(-4)-10(-2) M MgCl2, 3 X 10(-6)-10(-3) M MnCl2, 10(-5)-3 X 10(-4) M NiCl2, and 3 X 10(-5)-3 X 10(-4) M CoCl2 stimulated the binding. Incubation at 100 degrees C for 10 min destroyed specific binding.|
|Internal ID Number:||2556286|
In Vitro Techniques
Iodine Radioisotopes.diagnostic use
Rats, Inbred Strains
Receptors, Cell Surface.metabolism
|Appears in Collections:||Journal articles|
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