Novel insights into the biological function of mast cell carboxypeptidase A

Gunnar Pejler; Stefan David Knight; Frida Henningsson; Sara Wernersson

doi:10.1016/j.it.2009.04.008

Novel insights into the biological function of mast cell carboxypeptidase A

Gunnar Pejler
, Stefan David Knight
, Frida Henningsson
, Sara Wernersson

Publication: Contribution to journal › Review article › peer-review

Abstract

When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type. MC-CPA is a dominant protein component of the mast cell granule and the MC-CPAgene is extremely highly expressed. Despite this, relatively little has been known of its biological function. However, the recent generation of mouse strains lacking MC-CPA has opened up new possibilities for investigations related to this protease. This recent development has revealed a role for MC-CPA in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venom toxins. Here, we summarize the current knowledge of MC-CPA.

Original language	English
Pages (from-to)	401-408
Number of pages	8
Journal	Trends in Immunology
Volume	30
Issue number	8
DOIs	https://doi.org/10.1016/j.it.2009.04.008
Publication status	Published - 2009

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title = "Novel insights into the biological function of mast cell carboxypeptidase A",

abstract = "When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type. MC-CPA is a dominant protein component of the mast cell granule and the MC-CPAgene is extremely highly expressed. Despite this, relatively little has been known of its biological function. However, the recent generation of mouse strains lacking MC-CPA has opened up new possibilities for investigations related to this protease. This recent development has revealed a role for MC-CPA in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venom toxins. Here, we summarize the current knowledge of MC-CPA.",

author = "Gunnar Pejler and Knight, \{Stefan David\} and Frida Henningsson and Sara Wernersson",

year = "2009",

doi = "10.1016/j.it.2009.04.008",

language = "English",

volume = "30",

pages = "401--408",

journal = "Trends in Immunology",

issn = "1471-4906",

number = "8",

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TY - JOUR

T1 - Novel insights into the biological function of mast cell carboxypeptidase A

AU - Pejler, Gunnar

AU - Knight, Stefan David

AU - Henningsson, Frida

AU - Wernersson, Sara

PY - 2009

Y1 - 2009

N2 - When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type. MC-CPA is a dominant protein component of the mast cell granule and the MC-CPAgene is extremely highly expressed. Despite this, relatively little has been known of its biological function. However, the recent generation of mouse strains lacking MC-CPA has opened up new possibilities for investigations related to this protease. This recent development has revealed a role for MC-CPA in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venom toxins. Here, we summarize the current knowledge of MC-CPA.

AB - When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type. MC-CPA is a dominant protein component of the mast cell granule and the MC-CPAgene is extremely highly expressed. Despite this, relatively little has been known of its biological function. However, the recent generation of mouse strains lacking MC-CPA has opened up new possibilities for investigations related to this protease. This recent development has revealed a role for MC-CPA in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venom toxins. Here, we summarize the current knowledge of MC-CPA.

UR - https://res.slu.se/id/publ/27732

U2 - 10.1016/j.it.2009.04.008

DO - 10.1016/j.it.2009.04.008

M3 - Review article

C2 - 19643669

SN - 1471-4906

VL - 30

SP - 401

EP - 408

JO - Trends in Immunology

JF - Trends in Immunology

IS - 8

ER -

Novel insights into the biological function of mast cell carboxypeptidase A

Abstract

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