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

Details

Serval ID
serval:BIB_0F4FA095B555
Type
Article: article from journal or magazin.
Collection
Publications
Title
Identification and sequencing of cDNA clones encoding the granule-associated serine proteases granzymes D, E, and F of cytolytic T lymphocytes
Journal
Proceedings of the National Academy of Sciences of the United States of America
Author(s)
Jenne  D., Rey  C., Haefliger  J. A., Qiao  B. Y., Groscurth  P., Tschopp  J.
ISSN
0027-8424 (Print)
Publication state
Published
Issued date
07/1988
Volume
85
Number
13
Pages
4814-8
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jul
Abstract
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.
Keywords
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
Yes
Create date
24/01/2008 15:19
Last modification date
20/08/2019 12:36
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