Molecular characterization of a CD95 signaling mutant
| Autor: | Kevin M. Latinis, Erik J. Peterson, Gary A. Koretzky |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Genetics
Immunology Mutant chemical and pharmacologic phenomena hemic and immune systems Transfection Biology Fas receptor Jurkat cells biological factors Cell biology Rheumatology hemic and lymphatic diseases Complementary DNA Ultraviolet light Immunology and Allergy Pharmacology (medical) biological phenomena cell phenomena and immunity Signal transduction Death domain |
| Zdroj: | Arthritis & Rheumatism. 41:1047-1053 |
| ISSN: | 1529-0131 0004-3591 |
| DOI: | 10.1002/1529-0131(199806)41:6<1047::aid-art11>3.0.co;2-t |
| Popis: | OBJECTIVE To study the intracellular signaling events associated with ligation of the surface receptor CD95. METHODS A mutant clone of Jurkat T cells, DD3, which fails to transmit apoptotic signals through CD95, was selected for study. Surface expression of CD95 and the primary nucleotide sequence of CD95, as well as the functional effects of a mutant CD95 molecule found in DD3, were examined. RESULTS DD3, while exhibiting impaired ability to undergo apoptosis after CD95 ligation, retained the ability to die after ultraviolet light stimulation. A CD95 complementary DNA (cDNA) cloned from DD3 encoded a mutant transmembrane protein lacking the carboxy-terminal "death domain." Western blotting confirmed the presence of both wild-type and mutant CD95 protein in DD3. Transfection of the mutant CD95 cDNA into parental Jurkat cells conferred protection from CD95-mediated apoptosis. CONCLUSION A mutant CD95 receptor lacking the cytoplasmic "death domain" can interfere with wild-type receptor function in T cells. |
| Databáze: | OpenAIRE |
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