Identification and sequencing of cDNA clones encoding the granule-associated serine proteases granzymes D, E, and F of cytolytic T lymphocytes

Détails

ID Serval
serval:BIB_0F4FA095B555
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Identification and sequencing of cDNA clones encoding the granule-associated serine proteases granzymes D, E, and F of cytolytic T lymphocytes
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Jenne  D., Rey  C., Haefliger  J. A., Qiao  B. Y., Groscurth  P., Tschopp  J.
ISSN
0027-8424 (Print)
Statut éditorial
Publié
Date de publication
07/1988
Volume
85
Numéro
13
Pages
4814-8
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul
Résumé
Cytoplasmic granules of cytolytic T lymphocytes contain at least six related serine esterases (granzymes) that are released together with perforin, a pore-forming protein related to complement component C9, during target-cell lysis. Polyclonal antibodies were used to isolate a large number of cDNA clones from an expression library derived from cytolytic-T-cell mRNA. Three distinct full-length cDNA clones coding for granzymes D, E, and F were identified by restriction site mapping and nucleotide sequencing. The three deduced amino acid sequences are highly similar to one another (between 72% and 90% amino acid identities) and to the sequences of granzymes B and C, cathepsin G, and rat mast-cell proteases I and II (between 43% and 57% amino acid identities). Cysteine residues capable of forming intramolecular disulfide bonds are conserved, as are the catalytic-site residues characteristic of serine proteases. Comparison of the cDNA-derived protein sequences with the amino termini of the isolated granzymes provides evidence that they are stored in a fully processed, activated form after removal of the signal peptide and two additional residues (propeptide) at the amino terminus. Immunoelectron microscopic studies demonstrated that granzymes D, E, and F are present in the same morphologically distinct cytoplasmic granules in which perforin has been found previously.
Mots-clé
Amino Acid Sequence Animals Base Sequence Cytoplasmic Granules/enzymology DNA/genetics Granzymes Mice Mice, Inbred C57BL/genetics Molecular Sequence Data Sequence Homology, Nucleic Acid Serine Endopeptidases/*genetics T-Lymphocytes, Cytotoxic/*enzymology/ultrastructure
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 15:19
Dernière modification de la notice
20/08/2019 12:36
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