Purification and characterization of the Fas-ligand that induces apoptosis (1994)
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BibTeX
@MISC{Suda94purificationand,
author = {Takashi Suda and Shigekazu Nagata},
title = {Purification and characterization of the Fas-ligand that induces apoptosis},
year = {1994}
}
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Abstract
Fas is a 45-kD cell surface protein belonging to the tumor necrosis factor/nerve growth factor receptor family, and transduces the signal for apoptosis. The cytotoxic T lymphocyte (CTL) hybridoma, PC60-dl0S requires the presence of Fas on target cells to induce cytolysis in target ceils. This CTL cell line was weakly but specifically stained by a chimeric protein that consisted of the extracellular domain of mouse Fas and the Fc portion of human immunoglobulin G1 (mFas-Fc). Moreover, mFas-Fc inhibited the cytotoxic activity of PC60-dl0S. Sublines of dl0S that were stained intensively by mFas-Fc were isolated by repetitive fluorescence-activated cell sorter sorting. A cell-surface protein of about 40 kD was specifically precipitated by mFas-Fc from the lysates of these sublines. This protein was homogeneously purified by sequential affinity chromatographies using mFas-Fc and concanavalin A beads. The purified protein exhibited cytotoxic activity against cells expressing Fas but not to the cells which do not express Fas. These results indicated that the 40-kD membrane glycoprotein expressed on PC60-dl0S cells is the Fas-ligand that induces the apoptotic signal by binding to Fas. H omeostasis in mammals is controlled not only by cell
Keyphrases
cytotoxic activity extracellular domain 40-kd membrane glycoprotein purified protein apoptotic signal target cell repetitive fluorescence-activated cell sorter ctl cell line sequential affinity chromatography cytotoxic lymphocyte target ceils cell-surface protein chimeric protein pc60-dl0s cell human immunoglobulin g1 fc portion mouse fa 45-kd cell surface protein
