Correlation of the Lipolytic Action of Synthetic Peptides with Their Structures: Importance of Acidic and Basic Amino Acid Residues in the N-Terminal Region(Biological Chemistry)

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The effects on lipolysis in fat cells of synthetic peptides with different amino acid residues added to the N-terminal region of the sequence Phe-Phe-Phe were examined. Several synthetic peptides elicited free fatty acid (FFA) release from fat cells, the order of efficacy of their lipolytic actions being, Arg-Glu--Arg-Glu-Gly- > Glu-Arg-Gly- > Lys-Asp- 〜 Lys-Asp-Gly- 〜 Glu-Arg- > Asp-Lys-Gly-. Arg(NO_2)-Glu-Gly-Gly-Phe-Phe-Phe did not cause any release of FFA from fat cells.Arg-Glu-Phe-Phe-Phe stimulated lipolysis of fat cells even when calcium ions were not present in the reaction mixture, but other peptides required calcium ions for their lipolytic actions. The β-adrenergic blocker propranolol completely inhibited the lipolysis stimulated by Arg-Glu-Gly-Phe-Phe-Phe or Arg-Glu-Phe-Phe-Phe. The α-adrenergic blocker phenoxybenzamine had little effect on the lipolytic action stimulated by these two peptides. Lys-Asp-Gly-Phe-Phe-Tyr and Asp-Lys-Gly-Phe-Phe-Tyr also stimulated lipolysis, the stimulatory effect of the latter being about 58% of that of the former. Glu-Arg-Gly-Phe-Phe-Tyr and Arg-Glu-Gly-Phe-Phe-Tyr did not cause any release of FFA from fat cells.
社団法人日本農芸化学会の論文
1988-05-23