Biological activities of granzyme K are conserved in the mouse and account for residual Z-Lys-SBzl activity in granzyme A-deficient mice

Détails

ID Serval
serval:BIB_ED5C982CDDBD
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Biological activities of granzyme K are conserved in the mouse and account for residual Z-Lys-SBzl activity in granzyme A-deficient mice
Périodique
FEBS Letters
Auteur⸱e⸱s
Wilharm  E., Tschopp  J., Jenne  D. E.
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
10/1999
Volume
459
Numéro
1
Pages
139-42
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Oct 1
Résumé
Tryptase-like activities of T and NK cells contribute to the induction of target cell apoptosis, but only granzyme A (GzmA) has been shown to exhibit Z-Lys-SBzl esterase activity in murine T cells. GzmA-deficient mice exhibit residual Z-Lys-SBzl hydrolyzing activity and almost normal levels of lymphocyte-mediated cytotoxicity. Here we report the cloning and biochemical characterization of recombinant mouse granzyme K (GzmK). The purified murine protein shows Z-Lys-SBzl hydrolyzing activity and is inhibited by bikunin, the light chain of inter-alpha-trypsin inhibitor, like the human homolog. We conclude that GzmK expressed by GzmA-deficient T cells accounts for the remaining Z-Lys-SBzl activity. Functional similarities between GzmA and GzmK may explain the subtle immunological deficits observed in GzmA-deficient mice.
Mots-clé
Animals Chymases Cloning, Molecular DNA, Complementary/analysis Escherichia coli Glycoproteins/metabolism Granzymes Humans Lysine/*metabolism *Membrane Glycoproteins Mice Models, Molecular Recombinant Proteins/metabolism Serine Endopeptidases/genetics/*metabolism Serine Proteinase Inhibitors/metabolism Substrate Specificity *Trypsin Inhibitor, Kunitz Soybean Tryptases
Pubmed
Web of science
Création de la notice
24/01/2008 15:17
Dernière modification de la notice
20/08/2019 16:15
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