Ectoenzymes as sites of peptide regulation

Christopher S. Konkoy, Thomas P Davis

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The ectoenzyme-mediated metabolism of neuropeptides may be an important regulatory site of peptide-mediated activity. These membrane-bound, extracellularly oriented peptidases are not only responsible for inactivating peptide substrates, but also lead to the formation of metabolic fragments. Peptide fragments formed after enzymatic proteolysis have been shown to display novel bioactivity as a consequence of a shift in receptor selectivity. This example of nervous system plasticity through peptide biotransformation can have multiple consequences. Centrally acting drugs have been shown to have profound effects on peptide-mediated systems throughout the brain and spinal cord including a differential alteration in ectoenzyme activity and ectoenzyme-mediated metabolism of neuropeptides. In this review, Tom Davis and Chris Konkoy suggest that the modulation of ectoenzyme-mediated peptide metabolism represents an additional level at which the concentration of extracellular neuropeptides, and thus peptide-mediated transmission, can be regulated.

Original languageEnglish (US)
Pages (from-to)288-294
Number of pages7
JournalTrends in Pharmacological Sciences
Volume17
Issue number8
DOIs
StatePublished - Aug 1996

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Peptides
Neuropeptides
Metabolism
Proteolysis
Peptide Fragments
Neurology
Biotransformation
Bioactivity
Nervous System
Plasticity
Brain
Spinal Cord
Peptide Hydrolases
Modulation
Membranes
Substrates
Pharmaceutical Preparations

ASJC Scopus subject areas

  • Pharmacology
  • Toxicology

Cite this

Ectoenzymes as sites of peptide regulation. / Konkoy, Christopher S.; Davis, Thomas P.

In: Trends in Pharmacological Sciences, Vol. 17, No. 8, 08.1996, p. 288-294.

Research output: Contribution to journalArticle

Konkoy, Christopher S. ; Davis, Thomas P. / Ectoenzymes as sites of peptide regulation. In: Trends in Pharmacological Sciences. 1996 ; Vol. 17, No. 8. pp. 288-294.
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