Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: EC:1.3.5.1 (
succinate dehydrogenase
)
8,177
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Monosodium titanate (MST) is an inorganic sorbent/ion exchanger developed for the removal of radionuclides from nuclear wastes. We investigated the ability of MST to bind Cd(II), Hg(II), Au(III), or the Au-organic compound auranofin to establish the utility of MST for applications in environmental decontamination or medical therapy (drug delivery). Adsorption isotherms for MST were determined at pH 7-7.5 in water or phosphate-buffered saline. The extent of metal binding was determined spectroscopically by measuring the concentrations of the metals in solution before and after contact with the MST. Cytotoxic responses to MST were assessed using
THP1
monocytes and
succinate dehydrogenase
activity. Monocytic activation by MST was assessed by TNFalpha secretion (ELISA) with or without lipopolysaccharide (LPS) activation. MST adsorbed Cd(II), Hg(II), and Au(III) under conditions similar to those in physiological systems. MST exhibited the highest affinity for Cd(II) followed by Hg(II) and Au (III). MST (up to 100 mg/L) exhibited only minor (<25% suppression of
succinate dehydrogenase
) cytotoxicity and did not trigger TNFalpha secretion nor modulate LPS-induced TNFalpha secretion from monocytes. MST exhibits high affinity for biometals with no significant biological liabilities in these introductory studies. MST deserves further scrutiny as a substance with the capacity to decontaminate biological environments or deliver metals or metal compounds for therapeutic applications.
...
PMID:Adsorption of biometals to monosodium titanate in biological environments. 1636 65
Titanates are inorganic compounds with high affinity for specific metal ions or metal compounds, including gold. We have previously demonstrated that both monosodium titanate (MST) and amorphous peroxo-titanate (APT) alone do not suppress cellular metabolism of several cell types, and we have shown that MST and APT adsorb and release gold compounds in biological salt solutions. In the current study, we extend this work and show that MST and APT loaded with two gold compounds deliver sufficient levels of these compounds to alter the metabolism of mammalian cells. Fibroblasts (L929) or monocytes (
THP1
) were exposed to MST and APT loaded with either Au(III) or Auranofin(R), a Au(I)-organic compound, for 24-72 h, after which
succinate dehydrogenase
(
SDH
) activity of the cells was measured using the MTT method. MST or APT alone did not suppress
SDH
activity of either cell type. AF and Au(III) alone suppressed
SDH
activity completely above 2 muM or 300 muM, respectively. APT and MST loaded with either gold compound suppressed L929 fibroblast
SDH
activity by 30-80% after 72 h, but Au(III)-loaded APT was more potent than AF-loaded APT. Monocyte
SDH
activity was not affected by any loaded titanate. Our results suggest that titanates could be used for solid phase delivery of metal compounds to affect mammalian cell function of some types of cells.
...
PMID:Titanate particles as agents to deliver gold compounds to fibroblasts and monocytes. 1970 10