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

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

doi:10.1016/0196-9781(91)90049-U

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

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

Molecular Pathobiology

Research output: Contribution to journal › Article › peer-review

Abstract

Purified mast cell carboxypeptidase cleaved the C-terminal leucines from Leu⁵-enkephalin (Leu-ENK), neurotensin (NT), and kinetensin (KT), with K_m values of 36, 16, and 15 μM, and k_cat 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 language	English (US)
Pages (from-to)	995-1000
Number of pages	6
Journal	Peptides
Volume	12
Issue number	5
DOIs	https://doi.org/10.1016/0196-9781(91)90049-U
State	Published - 1991

Keywords

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

ASJC Scopus subject areas

Biochemistry
Physiology
Endocrinology
Cellular and Molecular Neuroscience

Access to Document

10.1016/0196-9781(91)90049-U

Cite this

@article{d1c3f69894db44309b5ea0d8438b5186,

title = "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 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.",

keywords = "Carboxypeptidase, Chymase, Kinetensin, Leu-enkephalin, Mast cell proteases, Neurotensin, Skin mast cells, Tryptase",

author = "Goldstein, {Sanford M.} and Jane Leong and Bunnett, {Nigel W.}",

note = "Funding Information: Mast cell carboxypeptidase was purified from human skin extracts as described (14). Dispersed mast cells were prepared from the facial skin of patients undergoing cosmetic surgical procedures (14,28). Released mast cell supernatants were obtained by incubation of 5 x 105 dispersed mast cells of 13.2% purity in 2.5 ml PAGCM buffer (15) with calcium ionophore 1This work was supported by grants AM31901, DK39957, DK42341, RR01614 and RR04112 from the National Institutes of Health. 2Requests for reprints should be addressed to Sanford M. Goldstein, Dermatology Research, Box 0536, UCSF, San Francisco, CA 94143-0536.",

year = "1991",

doi = "10.1016/0196-9781(91)90049-U",

language = "English (US)",

volume = "12",

pages = "995--1000",

journal = "Peptides",

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publisher = "Elsevier Inc.",

number = "5",

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T1 - Human mast cell proteases hydrolyze neurotensin, kinetensin and Leu5-enkephalin

AU - Goldstein, Sanford M.

AU - Leong, Jane

AU - Bunnett, Nigel W.

N1 - Funding Information: Mast cell carboxypeptidase was purified from human skin extracts as described (14). Dispersed mast cells were prepared from the facial skin of patients undergoing cosmetic surgical procedures (14,28). Released mast cell supernatants were obtained by incubation of 5 x 105 dispersed mast cells of 13.2% purity in 2.5 ml PAGCM buffer (15) with calcium ionophore 1This work was supported by grants AM31901, DK39957, DK42341, RR01614 and RR04112 from the National Institutes of Health. 2Requests for reprints should be addressed to Sanford M. Goldstein, Dermatology Research, Box 0536, UCSF, San Francisco, CA 94143-0536.

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

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