Abstract:
:In HL-60 cells signal transduction via sphingomyelin hydrolysis (sphingomyelin cycle) is induced by binding of tumor necrosis factor alpha (TNFalpha) to cell surface TNFalpha receptor. We found that IgG immunoglobulins activate sphingomyelin hydrolysis in plasma membrane of HL-60 cells, with kinetics similar to that of activation by TNFalpha. Activation was induced by different IgG isotypes (most of which are irrelevant to known inducers of the sphingomyelin cycle) and also by Fcgamma fragments of IgG. The facts that inhibiting the binding of the antibodies to the cell surface by protein A prevents activation of sphingomyelin hydrolysis and that soluble TNF receptor of 55-kDa subtype (TBP55) inhibits activation, suggest that the mechanism of IgG-induced sphingomyelin hydrolysis involves binding of IgGs through their Fcgamma domain to Fcgamma surface receptors which mediate autocrine secretion of TNFalpha. The latter is responsible for inducing sphingomyelin hydrolysis. This study suggests that TBP55 may be an effective inhibitor of the sphingomyelin cycle.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Glick D,Barenholz Ydoi
10.1016/0014-5793(96)00958-1subject
Has Abstractpub_date
1996-10-07 00:00:00pages
237-40issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00958-1journal_volume
394pub_type
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