منابع مشابه
Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin.
Two heme analogs, cobalt- and tin-protoporphyrin (CoPP and SnPP, respectively) have been used to probe the heme-hemopexin interaction, hemopexin receptor binding, and the mechanism of regulation of heme oxygenase (HO) and metallothionein-1 (MT-1) gene expression by hemopexin. Both CoPP and SnPP are HO inhibitors and hemopexin binds SnPP (Morgan, W. T., Alam, J., Deaciuc, V., Muster, P., Tatum, ...
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Heme oxygenase (HO)-mediated heme degradation is the primary mechanism for production of cellular carbon monoxide (CO). Analogous to nitric oxide (NO), CO mediates physiological and cellular functions such as vasodilatation, stimulation of guanylate cyclase, and neuronal transmission. In view of accumulating data demonstrating a correlation between the activity of these two gaseous molecules an...
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Heme oxygenase 1 (HO-1), a stress response protein, is highly induced in response to various agents causing oxidative stress including ultraviolet irradiation, sodium arsenite, hyperoxia, and glutathione depletors. We recently characterized the induction of HO-1 gene expression by nitric oxide (NO) and postulated that the addition of an antioxidant, such as pyrrolidine dithiocarbamate (PDTC), w...
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Heme oxygenase (HO) is a microsomal enzyme that oxidatively cleaves heme to form biliverdin, with the release of iron and carbon monoxide (CO). HO not only controls the availability of heme for the synthesis of heme proteins but also is responsible for the generation of CO, which binds to the heme moiety of heme proteins thus affecting their enzymatic activity. Cyclooxygenase (COX) is a heme pr...
متن کاملRegulation of a glutamyl-tRNA synthetase by the heme status.
Glutamyl-tRNA (Glu-tRNA), formed by Glu-tRNA synthetase (GluRS), is a substrate for protein biosynthesis and tetrapyrrole formation by the C(5) pathway. In this route Glu-tRNA is transformed to delta-aminolevulinic acid, the universal precursor of tetrapyrroles (e.g., heme and chlorophyll) by the action of Glu-tRNA reductase (GluTR) and glutamate semialdehyde aminotransferase. GluTR is a target...
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ژورنال
عنوان ژورنال: Folia Pharmacologica Japonica
سال: 2007
ISSN: 0015-5691,1347-8397
DOI: 10.1254/fpj.130.248