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

Abstract:

: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 microM, 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.

journal_name

Peptides

journal_title

Peptides

authors

Goldstein SM,Leong J,Bunnett NW

doi

10.1016/0196-9781(91)90049-u

subject

Has Abstract

pub_date

1991-09-01 00:00:00

pages

995-1000

issue

5

eissn

0196-9781

issn

1873-5169

pii

0196-9781(91)90049-U

journal_volume

12

pub_type

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