[^3H] TRYPTAMINE BINDING TO RECONSTITUTED FRACTION OF ACIDIC LIPIDS

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概要

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• The possible involvement of sulphatides (CS), phosphatidylserine (PS) and phosphatidylinositol (PI) in [^3H] tryptamine binding to various reconstituted fractions of these acidic lipids was examined by Sephadex LH_<20> column chromatography. The results indicated that each of the four systems, PS, PS-CS, PS-PI and PS-CS-PI, had the same binding capacity for [^3H] tryptamine, whereas other systems (CS, PI and CS-PI systems) had no binding capacity. Furthermore, competitive inhibition experiments revealed that among these four reconstituted systems, the PS-CS system exhibited the highest affinity for 5-methoxytryptamine. Kinetic studies suggested that at least two binding components (or sites) are implicated in the binding of [^3H] tryptamine to the reconstituted system of PS and CS with apparent K_D values of 3 and 10 nM. Displacement studies with various compounds indicated that only tryptamine and 5-methoxytryptamine inhibited the [^3H] tryptamine binding to this fraction, while other indoleamine analogues and neurotransmitters had no effect. In addition, we subjected whole rat brain synaptic plasma membranes to treatment with several kinds of lipid-modifying reagents and examined the [^3H] tryptamine binding capacities of the membranes by a radioreceptor-binding assay. [^3H] Tryptamine binding was decreased by treatment with Azure A and phospholipase A_2,while phospholipase D had no effect. All these observations led to the inference that PS and CS may be involved in the tryptamine binding activities as recognition sites.

• 公益社団法人日本薬学会の論文

著者

• Karasawa A

  Group Of Neuropharmacology Faculty Of Pharmaceutical Sciences Josai University

• Ogihara Masahiko

  Group Of Biochemical Pharmacology Faculty Of Pharmaceutical Sciences Josai University

• Ogihara Masahiko

  Group Of Neuropharmacology Faculty Of Pharmaceutical Sciences Josai University

• KARASAWA AKIRA

  Group of Neuropharmacology, Faculty of Pharmaceutical Sciences, Josai University

• ISHITANI RYOICHI

  Group of Neuropharmacology, Faculty of Pharmaceutical Sciences, Josai University

• Ishitani R

  Group Of Neuropharmacology Faculty Of Pharmaceutical Sciences Josai University

• KARASAWA Akira

  Group of Biochemical Pharmacology, Josai University

• ISHITANI Ryoichi

  Group of Biochemical Pharmacology, Josai University

• OGIHARA Masahiko

  Group of Bichemical Phamacology, Faculty of Pharmaceutical Scuebces, Josai University

関連論文

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• [^3H] TRYPTAMINE BINDING TO RECONSTITUTED FRACTION OF ACIDIC LIPIDS
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• Butanol extracts from myelin fragements: some characteristics of tryptamine binding.
• Effect of Phospholipase A2 on Temperature-Induced High-Affinity (3H)Tryptamine Binding Sites in Rat Brain.
• Effects of protein-modifying reagents on brain tryptamine binding sites: Possible involvement of a thiol group in temperature-induced high-affinity (3H)tryptamine binding sites.
• (3H)5-hydroxytryptamine binding to reconstituted fraction with sulphatides, phosphatidylserine and phosphatidylinositol.
• Effects of calcium channel blockers and hydralazine on plasma glucose levels in streptozotocin-induced diabetic rats in vivo.

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