The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes.

Details

Ressource 1Request a copy Under indefinite embargo.
UNIL restricted access
State: Public
Version: Final published version
License: Not specified
Serval ID
serval:BIB_751462C2078F
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The calcium-binding protein calreticulin is a major constituent of lytic granules in cytolytic T lymphocytes.
Journal
The Journal of experimental medicine
Author(s)
Dupuis M., Schaerer E., Krause K.H., Tschopp J.
ISSN
0022-1007
ISSN-L
0022-1007
Publication state
Published
Issued date
01/01/1993
Peer-reviewed
Oui
Volume
177
Number
1
Pages
1-7
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
Cytolytic T lymphocytes (CTL), natural killer cells, and lymphokine-activated killer (LAK) cells are cytolytic cells known to release the cytolytic protein perforin and a family of proteases, named granzymes, from cytoplasmic stores upon interaction with target cells. We now report the purification of an additional major 60-kD granule-associated protein (grp 60) from human LAK cells and from mouse cytolytic T cells. The NH2-terminal amino acid sequence of the polypeptide was found to be identical to calreticulin. Calreticulin is a calcium storage protein and carries a COOH-terminal KDEL sequence, known to act as a retention signal for proteins destined to the lumen of the endoplasmic reticulum. In CTLs, however, calreticulin colocalizes with the lytic perforin to the lysosome-like secretory granules, as confirmed by double label immunofluorescence confocal microscopy. Moreover, when the release of granule-associated proteins was triggered by stimulation of the T cell receptor complex, calreticulin was released along with granzymes A and D. Since perforin is activated and becomes lytic in the presence of calcium, we propose that the role of calreticulin is to prevent organelle autolysis due to the protein's calcium chelator capacity.
Keywords
Amino Acid Sequence, Animals, Calcium-Binding Proteins/analysis, Calcium-Binding Proteins/isolation & purification, Calcium-Binding Proteins/metabolism, Calreticulin, Cytoplasmic Granules/chemistry, Humans, Mice, Molecular Sequence Data, Receptors, Antigen, T-Cell/physiology, T-Lymphocytes, Cytotoxic/chemistry
Pubmed
Web of science
Open Access
Yes
Create date
24/01/2008 16:19
Last modification date
09/08/2024 15:53
Usage data