Chemical Control of Cell Differentiation of Human Myeloleukemia K562 Cell Line

Koiso, Yukiko; Nakajima, Osamu; Matsumura, Daisuke; Fujimoto, Yasuyuki; Hashimoto, Yuichi

doi:10.1248/yakushi1947.120.1_104

Cited by 7 publications

(6 citation statements)

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“…Both compounds can upregulate HO-1; however, inhibition of HO-1 activity by SnPPIX suppresses TPA-induced maturation to monocytes. Thus, HO-1 could be suggested as a directional switch and permissive enzyme in monocytic differentiation program of myeloid leukemia (79). Conversely, pharmacologic activation of HO-1 can block maturation of dendritic cells (17) and prevent differentiation of osteoclast precursors to osteoclasts (176).…”

Section: Ho-1 and Cell Differentiationmentioning

confidence: 99%

Heme Oxygenase-1 in Tumors: Is It a False Friend?

Józkowicz

Waś

Dulak

2007

Antioxidants & Redox Signaling

347

307

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Heme oxygenase-1 (HO-1) catalyzes the oxidation of heme to biologically active products: carbon monoxide (CO), biliverdin, and ferrous iron. It participates in maintaining cellular homeostasis and plays an important protective role in the tissues by reducing oxidative injury, attenuating the inflammatory response, inhibiting cell apoptosis, and regulating cell proliferation. HO-1 is also an important proangiogenic mediator. Most studies have focused on the role of HO-1 in cardiovascular diseases, in which its significant, beneficial activity is well recognized. A growing body of evidence indicates, however, that HO-1 activation may play a role in carcinogenesis and can potently influence the growth and metastasis of tumors. HO-1 is very often upregulated in tumor tissues, and its expression is further increased in response to therapies. Although the exact effect can be tissue specific, HO-1 can be regarded as an enzyme facilitating tumor progression. Accordingly, inhibition of HO-1 can be suggested as a potential therapeutic approach sensitizing tumors to radiation, chemotherapy, or photodynamic therapy. HEME OXYGENASE-1 (HO-1)HEME OXYGENASE (HO) is a microsomal enzyme catalyzing the first, rate-limiting step in degradation of heme and playing an important role in recycling of iron (103). It cleaves the α-meso carbon bridge of heme, yielding equimolar quantities of carbon monoxide (CO) and iron ions Fe 2+ and biliverdin (156). CO is then exhaled from the organisms through the lung (50). Free iron induces the expression of the iron-sequestering ferritin and activates FeATPase, an iron transporter, which decrease intracellular Fe 2+ content. Finally, biliverdin is converted by biliverdin reductase to bilirubin (144), which can be oxidized by cytochrome P450 enzymes, such as Cyp1A1, Cyp2B1, or Cyp2a5, or glucoronidated by UDPglucuronyl-transferase and subsequently eliminated as bilirubin glucoronides by the biliaryfecal pathway (25).The enzymatic activity of HO results in decreased oxidative stress, attenuated inflammatory response, and a lower rate of apoptosis (Fig. 1). This is due to removal of heme, a potent prooxidant and proinflammatory agent, but also because of generation of biologically active products. Among them, CO is an important cellular messenger, with the signaling function resembling that of nitric oxide (NO). Like NO, CO induces soluble guanylyl cyclase (sGC) and thereby inhibits platelet aggregation, decreases leukocyte adhesion, and reduces endothelial cell apoptosis. In addition, it exerts antiinflammatory effects by inhibition of tumor necrosis factor (TNF), interleukin-1β (IL-1β), and macrophage inflammatory protein-1β (MIP-1β), or by upregulation of interleukin-10 (IL-10) (123). Ferrous iron, the © Mary Ann Liebert, Inc. Address reprint requests to: Alicja Jozkowicz, Ph.D., D.Sc., Department of Medical Biotechnology, Faculty of Biophysics, Biochemistry and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Krakow, Poland, E-mail:alicia@mol.uj.edu.pl. Europe PMC Funders Gr...

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Section: Ho-1 and Cell Differentiationmentioning

confidence: 99%

Heme Oxygenase-1 in Tumors: Is It a False Friend?

Józkowicz

Waś

Dulak

2007

Antioxidants & Redox Signaling

347

307

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“…Targeted inhibition of HO by polyethylene glycol-linked ZnPP showed growth inhibitory activity against solid Sarcoma-180 tumours in mice (Fang et al 2003). Precise mechanisms as to how the HO/CO system promotes tumour growth are not fully understood, but widespread processes including the induction of resistance to stress and apoptosis (Doi et al 1999;Liu et al 2004;Was et al 2006), the altered expression of cell cycle and differentiation genes Koiso et al 2000;Chauveau et al 2005;Zwerina et al 2005), and the promotion of angiogenesis (Cherrington et al 2000;Dulak et al 2002;Sunamura et al 2003;Cisowski et al 2005;Hirai et al 2007;Deshane et al 2007) have been suggested (Fig. 3).…”

Section: Ho Activation In Cancerous Conditionsmentioning

confidence: 99%

Inhibitors of the heme oxygenase – carbon monoxide system: on the doorstep of the clinic?

Kinobe

Dercho

Nakatsu

2008

Can. J. Physiol. Pharmacol.

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The past decade has seen substantial developments in our understanding of the physiology, pathology, and pharmacology of heme oxygenases (HO), to the point that investigators in the field are beginning to contemplate therapies based on administration of HO agonists or HO inhibitors. A significant amount of our current knowledge is based on the judicious application of metalloporphyrin inhibitors of HO, despite their limitations of selectivity. Recently, imidazole-based compounds have been identified as potent and more selective HO inhibitors. This 'next generation' of HO inhibitors offers a number of desirable characteristics, including isozyme selectivity, negligible effects on HO protein expression, and physicochemical properties favourable for in vivo distribution. Some of the applications of HO inhibitors that have been suggested are treatment of hyperbilirubinemia, neurodegenerative disorders, certain types of cancer, and bacterial and fungal infections. In this review, we address various approaches to altering HO activity with a focus on the potential applications of second-generation inhibitors of HO.

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“…K562 is a chronic myelogenous leukemia (CML) cell line (FAB M1) that harbors the Bcr-Abl fusion protein [8,9]. K562 cells exhibit inducible erythroleukemic and megakaryocytic characteristics [10,11], but are not responsive to either RA [12,13] or D3 treatment [14], and thus serve as a negative control for RA-or D3-induced differentiation. HL60 leukemia cells are FAB M2 lineage-bipotent myeloblasts [15,16] that can differentiate along either the granulocytic lineage (using RA) or monocytic lineage (using D3).…”

Section: Introductionmentioning

confidence: 99%

Induced myelomonocytic differentiation in leukemia cells is accompanied by noncanonical transcription factor expression

et al. 2015

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HighlightsWe surveyed common myeloid leukemia cell lines undergoing differentiation therapy.Lineage progression in induced leukemia cell lines differs from nonmalignant cells.Aberrant transcription factor expression occurs in acute myeloid leukemia cells.A given differentiation therapy elicits different effects in specific cell lines.Although potent tools, cell lines must be employed with circumspection.

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Chemical Control of Cell Differentiation of Human Myeloleukemia K562 Cell Line

Cited by 7 publications

References 0 publications

Heme Oxygenase-1 in Tumors: Is It a False Friend?

Heme Oxygenase-1 in Tumors: Is It a False Friend?

Inhibitors of the heme oxygenase – carbon monoxide system: on the doorstep of the clinic?

Induced myelomonocytic differentiation in leukemia cells is accompanied by noncanonical transcription factor expression

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