Binding sites for /sup 3/H-LTC4 in membranes from guinea pig ileal longitudinal muscle
Leutriene (LTC4) is one of the components of Slow Reacting Substance of Anaphylaxis (SRS-A) and is a potent constrictor of guinea pig ilea. The contraction is likely to be a receptor-mediated process. Here the authors report the existence of specific binding sites for /sup 3/H-LTC4 in a crude membrane preparation from guinea pig ileal longitudinal muscle. At 4 degrees C in the presence of 20 mM Serine-borate, binding increases linearly with protein concentration, reaches equilibrium in 10 minutes, and is reversible upon addition of 3 x 10(-5) M unlabelled LTC4. The dissociation curve is consistent with the existence of more than one class of binding site. Ca++ and Mg++ greatly enhance the binding of /sup 3/H-LTC4 at equilibrium. In the presence of 5 mM CaCl/sub 2/ and MgCl/sub 2/ not only LTC4 (IC50 10(-7)M), but also LTD4 and the SRS-A antagonist FPL 55712 can compete with /sup 3/H-LTC4 for its binding sites. FPL 55712 only displaces 60-70% of the total amount bound, while LTC4 displaces 90-95%. These studies indicate that multiple classes of binding sites exist for /sup 3/H-LTC4 in guinea pig ileal longitudinal muscle, and that at least part of these binding sites might be related to the ability of LTC4 to contract guinea pig ilea.
- Research Organization:
- Univ. of Milan, Italy
- OSTI ID:
- 6306017
- Journal Information:
- Prostaglandins; (United States), Vol. 27:3
- Country of Publication:
- United States
- Language:
- English
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551001* - Physiological Systems- Tracer Techniques