cDNA cloning of gramzyme C, a granule-associated serine protease of cytolytic T lymphocytes

D. Jenne, C. Rey, D. Masson, K. K. Stanley, J. Herz, G. Plaetinck, J. Tschopp

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

A cDNA clone corresponding to the complete amino acid sequence of a putative protease CCP2 of murine cytotoxic T lymphocytes was isolated and sequenced. The clone encodes a 248-residue long serine esterase. The deduced N-terminal amino acid sequence is identical over 40 residues to that of granzyme C, a protease of unknown function present in granules of cytotoxic lymphocytes. Analysis of the sequence of granzyme C/CCP2 reveals high homology to other granzyme proteases, i.e. granzyme A (40%) and granzyme B (67%) and to rat mast cell protease II (46%). The amino acids lining the specificity pocket are well conserved between granzyme B, C and rat mast cell protease II, but not granzyme A, suggesting a similar general specificity of these three proteases.

Original languageEnglish (US)
Pages (from-to)318-323
Number of pages6
JournalJournal of Immunology
Volume140
Issue number1
StatePublished - Jan 1 1988

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint Dive into the research topics of 'cDNA cloning of gramzyme C, a granule-associated serine protease of cytolytic T lymphocytes'. Together they form a unique fingerprint.

  • Cite this

    Jenne, D., Rey, C., Masson, D., Stanley, K. K., Herz, J., Plaetinck, G., & Tschopp, J. (1988). cDNA cloning of gramzyme C, a granule-associated serine protease of cytolytic T lymphocytes. Journal of Immunology, 140(1), 318-323.