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*
Department of Human Genetics, Mount Sinai School of Medicine, New York, NY 10029; Departments of
Gastroenterology, Hepatology, and Infectious Diseases and
Pediatric Hematology and Oncology, and
Institute of Immunology, Otto-von-Guericke University, Magdeburg, Germany; and
¶ Medical Faculty, Institute of Physiological Chemistry, Martin Luther University Halle-Wittenberg, Wittenberg, Germany
Human cathepsin W (also called lymphopain) is a recently described
papain-like cysteine protease of unknown function whose gene expression
was found to be restricted to cytotoxic cells. Here we demonstrate that
cathepsin W is expressed predominantly in NK cells and, to a lesser
extent, in CTLs. Quantitative RT-PCR revealed that NK cells contained
21 times more cathepsin W transcript than CTLs. The predominant
expression of cathepsin W in NK cells was further confirmed by Western
blot analysis and immunohistochemistry. IL-2-mediated stimulation of NK
cells and CTLs revealed a stronger up-regulation of the cathepsin W
gene and protein expression in NK cells (7-fold) than in CTLs (2-fold).
Transfection experiments of HeLa cells and biochemical analyses
revealed that cathepsin W is exclusively "high mannose-type"
glycosylated and is mainly targeted to the endoplasmic reticulum (ER).
Interestingly, the ER localization of cathepsin W was also found in NK
cells, in which colocalization studies revealed an overlapping staining
of cathepsin W and Con A, an ER-specific lectin. Furthermore,
subcellular fractionation of cathepsin W-expressing cells confirmed the
ER localization and showed that cathepsin W is membrane associated.
Based on the results of this study, cathepsin W might represent a
putative component of the ER-resident proteolytic machinery. The
constitutive expression in NK cells and the stronger up-regulation of
cathepsin W by IL-2 in NK cells than CTLs suggest that cathepsin W is
not just a marker of cytotoxic cells but is, rather, specifically
expressed in NK cells.
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