Enzymatic Degradation of Proctolin in the CNS of the Locust, Schistocerca Gregaria, by Membrane Bound Enzymes

  • R. Elwyn Isaac
Part of the Experimental and Clinical Neuroscience book series (ECN)

Abstract

Although a number of mechanisms may be involved in the termination of neuropeptide signals, recent studies in vertebrate neurochemistry have indicated an important role for extracellular membrane enzymes in the inactivation of neuropeptides (Turner et al., 1985). Whether similar membrane enzymes are also involved in the inactivation of insect neuropeptides is unclear. A study on the metabolism of proctolin (Arg-Tyr-Leu-Pro-Thre) by tissues of P. americana showed that this peptide was degraded primarily by two soluble enzyme activities which cleaved the Arg-Tyr and Tyr-Leu bonds (Quistad et al., 1984). Membrane fractions possessed only weak degradative activity towards proctolin.

Keywords

Hydrolysis Tyrosine Enzymatic Degradation Succinate Dipeptide 

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References

  1. Quistad, G.B., Adams, M.E., Scarborough, R.M., Carney, R.L. and Schooley, D.A. (1984). Life Sci. 34, 569–576.PubMedCrossRefGoogle Scholar
  2. Turner, A.J., Matsas, R. and Kenny, A.J. (15S5). Biochem. Pharmacol. 34, 1347–1356.CrossRefGoogle Scholar

Copyright information

© The Humana Press Inc. 1986

Authors and Affiliations

  • R. Elwyn Isaac
    • 1
  1. 1.Department of Pure and Applied ZoologyUniversity of LeedsLeedsUK

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