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C6

RRID:CVCL_0194

Organism

Rattus norvegicus

Comments

Doubling time: ~24 hours (CLS); ~25-30 hours (DSMZ). Transformant: ChEBI; CHEBI:50102; N-methyl-N-nitrosourea (NMU). Omics: Mitochondrial genome sequenced. Breed/subspecies: Wistar Furth.

Proper Citation

JCRB Cat# JCRB9096, RRID:CVCL_0194

Category

Cancer cell line

Sex

Male

Synonyms

C-6, C 6, RGC-6, RGC6, RGc6

Vendor

JCRB

Cat Num

JCRB9096

Cross References

BTO; BTO:0000529 CLO; CLO_0002072 CLO; CLO_0002140 CLO; CLO_0051387 CLO; CLO_0051388 MCCL; MCC:0000085 CLDB; cl579 CLDB; cl580 CLDB; cl581 CLDB; cl583 CLDB; cl5165 ATCC; CCL-107 BCRC; 60046 BCRJ; 0057 CCRID; 3111C0001CCC000131 CCRID; 3111C0002000000048 CCRID; 3131C0001001000001 ChEMBL-Cells; CHEMBL3308345 ChEMBL-Targets; CHEMBL614657 CLS; 500142/p672_C6 DSMZ; ACC-550 ECACC; 92090409 ICLC; ATL95007 IZSLER; BS TCL 5 JCRB; IFO50110 JCRB; JCRB9096 KCB; KCB 93026YJ KCLB; 10107 Lonza; 27 NCBI_Iran; C575 RCB; RCB2783 RCB; RCB2854 TKG; TKG 0242 TKG; TKG 0589 TOKU-E; 750 Wikidata; Q54808212

Publications that use this research resource

A novel selective MAO-B inhibitor with neuroprotective and anti-Parkinsonian properties.

  • Chan HH
  • Eur. J. Pharmacol.
  • 2018 Jan 5

Literature context: C6 ATCC, CCL-107, RRID:CVCL_0194 GraphPad Prism GraphPad, (no ca


Abstract:

We previously reported that 1,3-bisbenzylimidazolium (DBZIM) bromide was neuroprotective for the dopaminergic system in Parkinson's disease (PD) models of rodent, however the underlying mechanism was unclear. We currently further confirmed that DBZIM ameliorated the Parkinsonian motor deficit and protected the nigrostriatal tract from the neurotoxicity of 1-methyl-4-(2'-methylphenyl)-1,2,3,6-tetrahydropyridine (2'-CH3-MPTP) in C57Bl/6 mice. The dopaminergic degeneration in the substantia nigra par compacta (SNc) and striatum was analyzed by immunohistochemistry while the monoamine oxidase B (MAO-B) inhibition effect of DBZIM was determined by enzyme kinetics. DBZIM was at least as effective as the clinically approved anti-PD drug, l-deprenyl (Selegiline), for both neuroprotection and correction of motor deficits. Mechanistically, DBZIM inhibited the specific activity of MAO-B in the striatum and C6 cells without affecting the protein expression. DBZIM directly inhibited the enzymatic activity of a purified MAO-B protein with an estimated Ki value from 780 to 940nM, in par with that of l-deprenyl (970nM). The physical interaction between DBZIM and MAO-B was proven by NMR analysis, with Kd around 21.5-46.8μM. Our binding and modelling data further illustrated that DBZIM is a mixed inhibitor with its binding to active site partially hindering the substrate binding. Therefore, inhibiting MAO-B is a major mechanism through which DBZIM confers neuroprotection for the dopaminergic neurons against 2'-CH3-MPTP toxicity. Remarkably, the post-lesion treatment with DBZIM provided greater anti-parkinsonian and neuroprotective effects than the l-deprenyl. The current study, together with our previous findings in a 6-OHDA PD model, demonstrated that DBZIM is a promising neuroprotectant for PD with anti-MAO-B property.

Protective Effects of Fetal Zone Steroids Are Comparable to Estradiol in Hyperoxia-Induced Cell Death of Immature Glia.

  • Hübner S
  • Endocrinology
  • 2017 May 1

Literature context: 0β+GFAP−; RRID:CVCL_0194) (55, 56)


Abstract:

Impaired neurodevelopment in preterm infants is caused by prematurity itself; however, hypoxia/ischemia, inflammation, and hyperoxia contribute to the extent of impairment. Because preterm birth is accompanied by a dramatic decrease in 17β-estradiol (E2) and progesterone, preliminary clinical studies have been carried out to substitute these steroids in preterm infants; however, they failed to confirm significantly improved neurologic outcomes. We therefore hypothesized that the persistently high postnatal production of fetal zone steroids [mainly dehydroepiandrosterone (DHEA)] until term could interfere with E2-mediated protection. We investigated whether E2 could reduce hyperoxia-mediated apoptosis in three immature glial cell types and detected the involved receptors. Thereafter, we investigated protection by the fetal zone steroids DHEA, 16α-hydroxy-DHEA, and androstenediol. For DHEA, the involved receptors were evaluated. We examined aromatases, which convert fetal zone steroids into more estrogenic compounds. Finally, cotreatment was compared against single hormone treatment to investigate synergism. In all cell types, E2 and fetal zone steroids resulted in significant dose-dependent protection, whereas the mediating receptors differed. The neuroprotection by fetal zone steroids highly depended on the cell type-specific expression of aromatases, the receptor repertoire, and the potency of the fetal zone steroids toward these receptors. No synergism in fetal zone steroid and E2 cotreatment was detected in two of three cell types. Therefore, E2 supplementation may not be beneficial with respect to neuroprotection because fetal zone steroids circulate in persistently high concentrations until term in preterm infants. Hence, a refined experimental model for preterm infants is required to investigate potential treatments.

Evidence for purine nucleoside phosphorylase (PNP) release from rat C6 glioma cells.

  • Giuliani P
  • J. Neurochem.
  • 2017 Mar 2

Literature context: e (ECACC, RRID:CVCL_0194) was purch


Abstract:

Intracellular purine turnover is mainly oriented to preserving the level of triphosphate nucleotides, fundamental molecules in vital cell functions that, when released outside cells, act as receptor signals. Conversely, high levels of purine bases and uric acid are found in the extracellular milieu, even in resting conditions. These compounds could derive from nucleosides/bases that, having escaped to cell reuptake, are metabolized by extracellular enzymes similar to the cytosolic ones. Focusing on purine nucleoside phosphorylase (PNP) that catalyzes the reversible phosphorolysis of purine (deoxy)-nucleosides/bases, we found that it is constitutively released from cultured rat C6 glioma cells into the medium, and has a molecular weight and enzyme activity similar to the cytosolic enzyme. Cell exposure to 10 μM ATP or guanosine triphosphate (GTP) increased the extracellular amount of all corresponding purines without modifying the levels/activity of released PNP, whereas selective activation of ATP P2Y1 or adenosine A2A metabotropic receptors increased PNP release and purine base formation. The reduction to 1% in oxygen supply (2 h) to cells decreased the levels of released PNP, leading to an increased presence of extracellular nucleosides and to a reduced formation of xanthine and uric acid. Conversely, 2 h cell re-oxygenation enhanced the extracellular amounts of both PNP and purine bases. Thus, hypoxia and re-oxygenation modulated in opposite manner the PNP release/activity and, thereby, the extracellular formation of purine metabolism end-products. In conclusion, extracellular PNP and likely other enzymes deputed to purine base metabolism are released from cells, contributing to the purinergic system homeostasis and exhibiting an important pathophysiological role.