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.

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概要

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• To investigate the biochemical nature of temperature-induced highaffinity [<SUP>3</SUP>H]tryptamine binding sites, we subjected whole rat brain synaptic membranes to treatment with various protein-modifying reagents and examined the subsequent [<SUP>3</SUP>H]tryptamine binding properties of the membranes. Pretreatment of the membrane preparations with NEM, NBS, PCMB, PAPMA and MA, but not with iodoacetamide, DTT, glutathione and cysteine, reduced the [<SUP>3</SUP>H]tryptamine binding. In addition, to at least approx. 10<SUP>-4</SUP> M, the inactivation properties of NEM, PCMB, PAPMA and MA, except for NBS, were temperature-dependent. Furthermore, it was revealed that the Scatchard plot of [<SUP>3</SUP>H]tryptamine binding in membranes pretreated with these thiol reagents conformed to a curved line, as well as in the case of the control membranes. Nonlinear regression analysis of these data showed that NEM decreased the B<SUB>max</SUB> values of both the high and low affinity binding sites with no significant alteration in the K<SUB>D</SUB> values, whereas PCMB, PAPMA and MA increased only the K<SUB>D</SUB> value of the high affinity sites, accompanying the decrease of the B<SUB>max</SUB> values of both sites. These results indicate that the temperature-induced high-affinity [<SUP>3</SUP>H]tryptamine binding molecule(s) is a thiol protein.

• 公益社団法人 日本薬理学会の論文

著者

• ISHITANI Ryoichi

  Group of Biochemical Pharmacology, Josai University

• SAITO Michiko

  Group of Neuropharmacology, Josai University

• SERIKYAKU Shigefumi

  Group of Neuropharmacology, Josai University

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