Human mast cell proteases hydrolyze neurotensin, kinetensin and Leu5-enkephalin

Sanford M. Goldstein, Jane Leong, Nigel W. Bunnett

Research output: Contribution to journalArticlepeer-review


Purified mast cell carboxypeptidase cleaved the C-terminal leucines from Leu5-enkephalin (Leu-ENK), neurotensin (NT), and kinetensin (KT), with Km values of 36, 16, and 15 μM, and kcat values of 44, 51, and 53 s-1, respectively. To better predict potential in vivo hydrolysis products generated by mast cell proteases, these peptides were incubated with released skin mast cell supernatants. Leu5-enkephalin was hydrolyzed only by carboxypeptidase. Kinetensin was cleaved by tryptase, chymase, and carboxypeptidase to yield KT(1-3), KT(1-7), KT(1-8), KT(4-7), and KT(4-8), the last two peptides by the concerted action of two of the proteases. NT(1-11) and NT(1-12) were generated from neurotensin by chymase and carboxypeptidase, respectively.

Original languageEnglish (US)
Pages (from-to)995-1000
Number of pages6
Issue number5
StatePublished - 1991


  • Carboxypeptidase
  • Chymase
  • Kinetensin
  • Leu-enkephalin
  • Mast cell proteases
  • Neurotensin
  • Skin mast cells
  • Tryptase

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience


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