作者: Simon A. Jones , Sankichi Horiuchi , Daniela Novick , Naoki Yamamoto , Gerald M. Fuller
DOI: 10.1002/(SICI)1521-4141(199811)28:11<3514::AID-IMMU3514>3.0.CO;2-T
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摘要: The soluble IL-6 receptor (sIL-6R) is generated through either proteolytic shedding of the cognate (PC-sIL-6R), or released as product differential mRNA splicing (DS-sIL-6R). Using monocytic THP-1 cells, we demonstrate that both mechanisms are independently regulated, and each process contributes to sIL-6R production. Shedding IL-6R was activated by Ca2+ ionophore, ionomycin, inhibited TNF-alpha protease inhibitor (TAPI). In contrast, basal release unaffected depletion largely insensitive TAPI. Moreover, although inactivated serum starvation, non-stimulated production remained intact. Basal via shown inhibitory action brefeldin A an enzyme-linked immunosorbent assay specific for DS-sIL-6R. Release this isoform ionomycin TAPI, indicating mobilization activates PC-sIL-6R generation, but not divergent control these isoforms indicates they may influence inflammatory response.