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Immunology |
The Huntsman Cancer Institute, Division of Molecular Pharmacology, Salt Lake City, Utah 84112
We have examined the activity of a new member of the tumor necrosis
factor (TNF) family identified through Expressed Sequence Tag database
searching using TNF
protein as the search query. We have termed this
protein TNF-related death ligand-1 (TRDL-1). Traditional cDNA
library screening identified two additional splice variants designated
TRDL-1ß and TRDL-1
that differed from TRDL-1 by the deletion of
two small regions within the protein coding region. TRDL-1 is
identical in sequence to the recently described molecule, APRIL,
that may induce cell proliferation. We found, however, that purified,
FLAG-tagged TRDL-1 caused Jurkat cell death with kinetics that
paralleled FasL. In vitro binding experiments
demonstrated that TRDL-1 coprecipitated Fas and HVEM and suggested
TRDL-1 as an alternate ligand for these receptors. TRDL-1 localized
to chromosome 17p13.3 and its expression was widespread in normal
tissues. Examination of 48 tumor samples revealed high levels of TRDL-1
expression in several tumors, including those from the gastrointestinal
tract. Expression of TRDL-1 in COS-1 cells confirmed membrane
association of TRDL-1, typical of TNF family members.
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