Human mast cell carboxypeptidase. Selective localization to MCTC cells

J Immunol. 1991 Jul 1;147(1):247-53.

Abstract

Two murine mAb were prepared against human mast cell carboxypeptidase (HMC-CP) purified from human skin, and were termed CP1 and CP2, respectively. Double immunohistochemical labeling of Carnoy's-fixed sections of human skin, lung, and gastrointestinal tissue with CP1 and CP2, respectively, and with a murine monoclonal antitryptase antibody demonstrated that HMC-CP was selectively present in a subset of human mast cells. Double labeling experiments with CP1 and CP2, respectively, and a murine anti-chymase mAb demonstrated the presence of HMC-CP in the tryptase-positive, chymase-positive mast cell type (MCTC) only. Immunohistochemical labeling of peripheral blood leukocytes resulted in staining of monocytes with CP2 but not with CP1. In addition to chymase and a cathepsin-G like proteinase, HMC-CP is another neutral protease that is selectively present in the MCTC tryptase-positive, chymase-positive mast cells type of mast cell, thus extending the biochemical definition of human mast cell heterogeneity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Monoclonal / immunology*
  • Carboxypeptidases / immunology*
  • Carboxypeptidases / metabolism
  • Chymases
  • Cross Reactions
  • Humans
  • Immunohistochemistry
  • Mast Cells / enzymology*
  • Monocytes / enzymology
  • Monocytes / immunology
  • Neutrophils / enzymology
  • Neutrophils / immunology
  • Peptide Hydrolases / analysis
  • Serine Endopeptidases / analysis

Substances

  • Antibodies, Monoclonal
  • Carboxypeptidases
  • Peptide Hydrolases
  • tosylarginine methyl ester hydrolase
  • Serine Endopeptidases
  • Chymases