The social network of carbon monoxide in medicine

Węgiel, Barbara; Hanto, Douglas W.; Otterbein, Leo E.

doi:10.1016/j.molmed.2012.10.001

Cited by 92 publications

(88 citation statements)

References 77 publications

(90 reference statements)

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“…1C). HO-1 is a biologically protective enzyme induced in the face of multiple stressors that catabolizes free heme to produce known antiinflammatory and antioxidant molecules, CO, and bilirubin (Tenhunen et al 1968(Tenhunen et al , 1969Stocker et al 1987;Hayashi et al 1999;Otterbein et al 2000;Kirkby and Adin 2006;Wegiel et al 2013). We utilized the pharmacological agent CoPPIX to specifically induce HO-1 expression in utricles.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, protection conferred from the HO-1/macrophage axis has been demonstrated in other systems, particularly in response to ischemiareperfusion injury in the liver (Devey et al 2009). In that system, HO-1 appears to regulate the cytokine secretion profile of the macrophages in a manner in which increased HO-1 expression results in a switch from pro-to anti-inflammatory cytokine secretion (Weis et al 2009;Wegiel et al 2013). Thus, HO-1 levels may influence whether resident macrophages exhibit a pro-inflammatory phenotype that promotes cell death versus a non-inflammatory phenotype that promotes cell survival.…”

Section: Discussionmentioning

confidence: 99%

“…Like other inducible heat shock proteins, HO-1 is upregulated in response to a variety of stressors, including heat shock (Shibahara et al 1987;Fairfield et al 2004;Wegiel et al 2013). However, unlike some HSPs, HO-1 does not have chaperone activity.…”

Section: Introductionmentioning

confidence: 99%

“…However, unlike some HSPs, HO-1 does not have chaperone activity. Instead HO-1 is an enzyme responsible for heme catabolism, the products of which include bilirubin, carbon monoxide (CO), and free iron (Tenhunen et al 1968(Tenhunen et al , 1969Wegiel et al 2013). Bilirubin and CO each have antioxidant and antiinflammatory properties (Stocker et al 1987;Hayashi et al 1999;Otterbein et al 2000;Kirkby and Adin 2006;Wegiel et al 2013).…”

Section: Introductionmentioning

confidence: 99%

“…Instead HO-1 is an enzyme responsible for heme catabolism, the products of which include bilirubin, carbon monoxide (CO), and free iron (Tenhunen et al 1968(Tenhunen et al , 1969Wegiel et al 2013). Bilirubin and CO each have antioxidant and antiinflammatory properties (Stocker et al 1987;Hayashi et al 1999;Otterbein et al 2000;Kirkby and Adin 2006;Wegiel et al 2013). Pharmacological induction of HO-1 is protective against multiple stresses in many tissue types, including ischemia-reperfusion injury in liver and retina (Tsuchihashi et al 2007;Sun et al 2010).…”

Section: Introductionmentioning

confidence: 99%

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Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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Cisplatin is a highly successful and widely used chemotherapy for the treatment of various solid malignancies in both adult and pediatric patients. Side effects of cisplatin treatment include nephrotoxicity and ototoxicity. Cisplatin ototoxicity results from damage to and death of cells in the inner ear, including sensory hair cells. We showed previously that heat shock inhibits cisplatin-induced hair cell death in whole-organ cultures of utricles from adult mice. Since heat shock protein 70 (HSP70) is the most upregulated HSP in response to heat shock, we investigated the role of HSP70 as a potential protectant against cisplatin-induced hair cell death. Our data using utricles from HSP70 −/− mice indicate that HSP70 is necessary for the protective effect of heat shock against cisplatin-induced hair cell death. In addition, constitutive expression of inducible HSP70 offered modest protection against cisplatin-induced hair cell death. We also examined a second heat-inducible protein, heme oxygenase-1 (HO-1, also called HSP32). HO-1 is an enzyme responsible for the catabolism of free heme. We previously showed that induction of HO-1 using cobalt protoporphyrin IX (CoPPIX) inhibits aminoglycoside-induced hair cell death. Here, we show that HO-1 also offers significant protection against cisplatin-induced hair cell death. HO-1 induction occurred primarily in resident macrophages, with no detectable expression in hair cells or supporting cells. Depletion of macrophages from utricles abolished the protective effect of HO-1 induction. Together, our data indicate that HSP induction protects against cisplatin-induced hair cell death, and they suggest that resident macrophages mediate the protective effect of HO-1 induction.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Baker

Roy

Brandon

et al. 2014

JARO

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Release of Bioactive Molecules Using Metal Complexes

Simpson¹,

Schatzschneider²

2014

Inorganic Chemical Biology

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Four iron(II) carbonyl complexes containing both pyridyl and halide ligands: Their synthesis, characterization, stability, and anticancer activity

Guo

Jin

Xiao

et al. 2020

Applied Organom Chemis

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Four iron(II) carbonyl complexes, fac-[Fe (CO) 3 X 2 (py)] (X = I − , 1 and Br − , 3), fac-[{Fe (CO) 3 X 2 } 2 (bipy)] (X = I − , 2 and Br − , 4), were facilely synthesized by reacting cis-[Fe (CO) 4 X 2 ] (X = I − , Br −) with pyridine (py) and 4,4 0-dipyridine (bipy) ligands, respectively, in good yields (70%85%). These complexes were fully characterized, and the structures of Complexes 2 and 3 were crystallographically analyzed. In dimethyl sulfoxide, they decomposed rapidly to release carbon monoxide (CO), and in methanol, they showed better stability which allowed kinetically analyzing their decomposing behaviors. The selfdecomposing in methanol fitted first-order kinetics with a half-time ranging from several minutes to 1 h. Our results suggested that the ligand with great conjugation (bipy) and strong electron-donating capability (iodide) could stabilize the iron(II) carbonyl complexes. The decomposition of the iodo complexes (1 and 2) involved the production of iodine radicals. MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide) assessments revealed that the efficacy against human bladder carcinoma cell line (RT112) is in the following trend: 1 > 2 > 3 > 4. The relatively strong efficacy of Complexes 1 and 2 is mainly contributed to the in situ generated iodine radicals. The combination of the cytotoxicity of the in situ generated radicals with the anticancer activity of CO as reported in literatures may lead to developing novel anticancer drugs with enhanced efficacy. K E Y W O R D S anticancer activity, carbon monoxide release and kinetics, iodine radical, iron carbonyl compounds, solvolysis Zhuming Guo and Jing Jin contributed equally to this work.

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The social network of carbon monoxide in medicine

Cited by 92 publications

References 77 publications

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Heat Shock Protein-Mediated Protection Against Cisplatin-Induced Hair Cell Death

Release of Bioactive Molecules Using Metal Complexes

Four iron(II) carbonyl complexes containing both pyridyl and halide ligands: Their synthesis, characterization, stability, and anticancer activity

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