Suramin inhibits the binding of complement-fixing antibody/double-stranded DNA immune complexes to CR1

Taylor, Ronald P.; Horgan, Carol; Harbin, Alisa; Burge, J

doi:10.1016/0090-1229(84)90077-1

Cited by 5 publications

(5 citation statements)

References 39 publications

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“…Suramin associates, apparently in a nonspecific low-affinity manner, with a number of proteins and has been shown to inhibit a large number of enzymatic activities in vitro (26)(27)(28)(29). From the present study it is clear that suramin also neutralizes the activities of several growth factors.…”

Section: Discussionsupporting

confidence: 49%

Efficient reversion of simian sarcoma virus-transformation and inhibition of growth factor-induced mitogenesis by suramin.

Betsholtz¹,

Johnsson²,

Heldin³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

231

104

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Simian sarcoma virus, an acutely transforming primate retrovirus with capacity to induce gliomas and sarcomas in experimental animals, has acquired its transforming properties by transducing the cellular gene sequences that encode one of the constituent chains of platelet-derived growth factor. Suramin, a drug used in the treatment of trypanosomiasis and onchocerciasis, has previously been reported to inhibit the interaction of platelet-derived growth factor with its cell surface receptor. We show here that suramin efficiently reverts the simian sarcoma virus-induced transformed phenotype in human and rat fibroblasts and propose that this is due to neutralization of an externalized v-sis product. Moreover, we show that suramin inhibits the action of a broad spectrum of growth factors.

show abstract

Section: Discussionsupporting

confidence: 49%

Efficient reversion of simian sarcoma virus-transformation and inhibition of growth factor-induced mitogenesis by suramin.

Betsholtz¹,

Johnsson²,

Heldin³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

231

104

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“…I) showed that factor I, and not intact classical or alternative pathway complement function, was essential for the release of CRl-bound, complement opsonized TT-aTT. The consistency with data reported on TT-aTT (18) and other IC-systems (9,13,14,15,16,17,18,26,28,29) demonstrated that the TT-aTT used were not unique in their binding (30) and release properties. Further, in accordance with previous studies regarding antigenicity (26) and function of CRl (3,17), the receptors were found to be antigenically unchanged by the binding and release of TT-aTT.…”

Section: Discussionsupporting

confidence: 81%

“…2 and 3). This observation is decisive for interpretation of in vitro studies involving EDTA and suramin (28). This observation is decisive for interpretation of in vitro studies involving EDTA and suramin (28).…”

Section: Discussionmentioning

confidence: 88%

“…Since the interaction of C3b with factor I is charge-dependent (24), and the polyanionic suramin is supposed to bind directly to complement components (5, 28) EDTA might interfere through a charge-dependent interaction. This observation is decisive for interpretation of in vitro studies involving EDTA and suramin (28). Suramin is a potent, rapidly acting and selective (non-specific) but also reversible and firmly protein-bound inhibitor of factor I (4,5,6,22).…”

Section: Discussionmentioning

confidence: 99%

“…Factor I is not inhibited by protease inhibitors or cheiating agents such as 50 mM EDTA (23) but a selective inhibiting effect has been obtained by the use of suramin (15,24) or K76 monocarboxylic acid (7,8,15,16) at appropriate concentrations. However, it has recently been reported that suramin can cause release of IC bound to CRl on RBC as well as block the binding of IC to the receptors (28).…”

mentioning

confidence: 99%

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Release of Immune Complexes Bound to CR1 on Erythrocytes; Suramin Inhibits Factor I in the Presence of EDTA

Thomsen

Nielsen

Bendixen

1986

Allergy

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An experimental model was established in order to study the release of immune complexes (IC) bound by complement C3b receptors (CR1) on human erythrocytes (RBC). Soluble tetanus toxoid anti-tetanus toxoid complexes were incubated with RBC in the presence of autologous serum at optimal conditions for binding. The RBC carrying complement-opsonized complexes were incubated with appropriate serum reagents, and it was shown that factor I was required for release of the complexes, which occurred without loss of CR1. Suramin was, irrespective of factor I, found to induce release of CR1-bound IC in the absence of EDTA, whereas factor I-mediated release was inhibited by suramin in the presence of EDTA. EDTA probably interfered through a charge-dependent interaction. These observations are decisive for the interpretation of in vitro experiments involving these reagents. The combination of EDTA and suramin was found inappropriate for use in quantitative determination of in vivo CR1-bound IC.

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Suramin inhibits antibody binding to cell surface antigens and disrupts complement-mediated mesangial cell lysis

Piao

Chi

Zhang

et al. 2016

Journal of Pharmacological Sciences

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Suramin inhibits immune responses and protects cells against inflammatory cell injury. However, little is known about its mechanisms. Using an in vitro model of glomerular mesangial cell (MC) lysis induced by antibodies plus complement, we investigated the potential protective effects and mechanisms of suramin on immunologic cell injury. Exposure of rat MCs to anti-Thy-1 antibody plus complement or anti-MC rabbit serum caused complement-dependent cell lysis, which was blocked by suramin and its structural analogue NF023 and NF049, but not by PPADS, an antagonist of purinergic receptors. Addition of exogenous ATP also failed to affect MC lysis. Further analysis revealed that suramin interfered with antibody binding to cell membrane antigens and suppressed antibody-induced phosphorylation of several proteins, including p38. Inhibition of p38 with chemical inhibitor significantly attenuated cell injury. Collectively, our results indicate that suramin protects cells against antibody-initiated and complement-dependent cell injury through inhibition of antibody binding to cell surface antigens and suppression of p38 activation. Our study thus provides novel mechanistic insights into the actions of suramin and suggests that suramin might be used to treat certain immune diseases.

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Suramin inhibits the binding of complement-fixing antibody/double-stranded DNA immune complexes to CR1

Cited by 5 publications

References 39 publications

Efficient reversion of simian sarcoma virus-transformation and inhibition of growth factor-induced mitogenesis by suramin.

Efficient reversion of simian sarcoma virus-transformation and inhibition of growth factor-induced mitogenesis by suramin.

Release of Immune Complexes Bound to CR1 on Erythrocytes; Suramin Inhibits Factor I in the Presence of EDTA

Suramin inhibits antibody binding to cell surface antigens and disrupts complement-mediated mesangial cell lysis

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