Novel insights into the biological function of mast cell carboxypeptidase A.
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-CPA gene 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.
Pejler
Gunnar
G
Swedish University of Agricultural Sciences, Dept of Anatomy, Physiology and Biochemistry, Uppsala 75123, Sweden. Gunnar.Pejler@afb.slu.se
Knight
Stefan D
SD
Henningsson
Frida
F
Wernersson
Sara
S
D000818:Animals; D043422:Carboxypeptidases A / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D006801:Humans; D007113:Immunity, Innate / Q000502:physiology*; D008407:Mast Cells / Q000201:enzymology*; D051379:Mice; D051381:Rats; D022142:Secretory Vesicles / Q000378:metabolism*; D013379:Substrate Specificity
D043422:Carboxypeptidases A