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G-1 Sale

目录号 : GC12766

G-1 is a selective and potent agonist of GPR30 with EC50 value about 2 nM.

G-1 Chemical Structure

Cas No.:881639-98-1

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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment [1]:

Cell lines

A549 human lung cancer cells

Preparation Method

A549 human lung cancer cells were treated with various concentrations (10-8, 10-7, 10-6, 10-5 and 10-4 M) of 17β-estradiol and G-1 in 96-well plates and incubated for 48 or 72 h. Following incubation, MTT solution (Sigma-Aldrich) was added to each well at a concentration of 0.5 mg/ml, and incubated for 4 h at 37°C.

Reaction Conditions

0.01-100 µM for 48 and 72 h

Applications

Treatment with G-1 (10-5 and 10-4 M) for 48 and 72 h significantly decreased cell proliferation.

Animal experiment [2]:

Animal models

SJL mice (5-7 weeks old)

Preparation Method

SJL mice were immunized s.c. with 50 µg PLP139-151 and CFA (400 µg Mycobacterium tuberculosis). Mice were treated with 50 mg/kg/day G-1 daily for 21 days beginning at the day of disease induction. Control mice were similarly treated with vehicle (5% Dimethyl sulfoxide (DMSO), 95% Polyethylene glycol (PEG)-300.

Dosage form

50 mg/kg/day for 21 days

Applications

G-1 administration significantly reduced the severity of actively induced experimental allergic encephalomyelitis (EAE) but not the incidence of disease.

References:

[1]: Kurt A H, Çelik A, Kelleci B M. Oxidative/antioxidative enzyme-mediated antiproliferative and proapoptotic effects of the GPER1 agonist G-1 on lung cancer cells[J]. Oncology Letters, 2015, 10(5): 3177-3182.
[2]: Blasko E, Haskell C A, Leung S, et al. Beneficial role of the GPR30 agonist G-1 in an animal model of multiple sclerosis[J]. Journal of neuroimmunology, 2009, 214(1-2): 67-77.

产品描述

G-1 is a selective and potent agonist of GPR30 with EC50 value about 2 nM [1].

G-1 treatment (10-5 and 10-4 M) for 48 and 72 h significantly decreased A549 cell proliferation, at 72 h, the IC50 value for G-1 was calculated to be 2×10-5 M [2]. G-1 treatment at a concentration of 2×10-5 M had no significant effect on CAT activity but led to a significant increase in SOD activity, GPx activity and NO level [2]. G-1 inhibited TNF-α and IL-6 release on primary human macrophages derived from monocytes treated with GM-CSF over 6 days. The agonist inhibited the induction of both cytokines with IC50 values of 209 nM and 317 nM, respectively [3]. G-1 was also able to inhibit LPS induction of TNF-α in a mouse macrophage cell line, RAW 264.7 [3].

G-1 (50 mg/kg/day, 21 days) administration significantly reduced the severity of actively induced experimental allergic encephalomyelitis (EAE). G-1 treatment reduced the qualitative degree of inflammation in the lumbar spinal cord. G-1 treatment reduced the fraction of CNS-infiltrating macrophages (CD45hiCD11b+) in three individually analyzed mice [3]. G-1 could exert protective effects on motoneurons. The intraperitoneal injection of the GPR30 agonist G-1 for 14 days induces neuroprotective effects similar with the same dose of E2 [4].

References:
[1]. Bologa C G, Revankar C M, Young S M, et al. Virtual and biomolecular screening converge on a selective agonist for GPR30[J]. Nature chemical biology, 2006, 2(4): 207-212.
[2]. Kurt A H, Çelik A, Kelleci B M. Oxidative/antioxidative enzyme-mediated antiproliferative and proapoptotic effects of the GPER1 agonist G-1 on lung cancer cells[J]. Oncology Letters, 2015, 10(5): 3177-3182.
[3]. Blasko E, Haskell C A, Leung S, et al. Beneficial role of the GPR30 agonist G-1 in an animal model of multiple sclerosis[J]. Journal of neuroimmunology, 2009, 214(1-2): 67-77.
[4]. Cheng Q, Meng J, Wang X, et al. G-1 exerts neuroprotective effects through G protein-coupled estrogen receptor 1 following spinal cord injury in mice[J]. Bioscience Reports, 2016, 36(4).

Chemical Properties

Cas No. 881639-98-1 SDF
化学名 rel-1-[4-(6-bromo-1,3-benzodioxol-5-yl)-3aR,4S,5,9bS-tetrahydro-3H-cyclopenta[c]quinolin-8-yl]-ethanone
Canonical SMILES CC(C1=CC([C@@](C=CC2)([H])[C@@]2([H])[C@H](C3=CC(OCO4)=C4C=C3Br)N5)=C5C=C1)=O
分子式 C21H18BrNO3 分子量 412.28
溶解度 1mg/ml in ethanol; 20mg/ml in DMSO; 30mg/ml in DMF 储存条件 Store at -20°C
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溶解性数据

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1 mM 2.4255 mL 12.1277 mL 24.2554 mL
5 mM 0.4851 mL 2.4255 mL 4.8511 mL
10 mM 0.2426 mL 1.2128 mL 2.4255 mL
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Research Update

The G-Protein-Coupled Estrogen Receptor Agonist G-1 Inhibits Proliferation and Causes Apoptosis in Leukemia Cell Lines of T Lineage

Front Cell Dev Biol2022 Feb 14;10:811479.PMID: 35237599DOI: 10.3389/fcell.2022.811479

The G-protein-coupled estrogen receptor (GPER) mediates non-genomic action of estrogen. Due to its differential expression in some tumors as compared to the original healthy tissues, the GPER has been proposed as a therapeutic target. Accordingly, the non-steroidal GPER agonist G-1, which has often demonstrated marked cytotoxicity in experimental models, has been suggested as a novel anticancer agent for several sensitive tumors. We recently revealed that cell lines derived from acute T-cell (query) lymphoblastic leukemia (T-ALL) express the GPER. Here, we address the question whether G-1 is cytotoxic to T-ALL. We have shown that G-1 causes an early rise of intracellular Ca2+, arrests the cell cycle in G2/M, reduces viability, and provokes apoptosis in T-ALL cell lines. Importantly, G-1 caused destabilization and depolymerization of microtubules. We assume that it is a disturbance of the cytoskeleton that causes G-1 cytotoxic and cytostatic effects in our model. The observed cytotoxic effects, apparently, were not triggered by the interaction of G-1 with the GPER as pre-incubation with the highly selective GPER antagonist G-36 was ineffective in preventing the cytotoxicity of G-1. However, G-36 prevented the intracellular Ca2+ rise provoked by G-1. Finally, G-1 showed only a moderate negative effect on the activation of non-leukemic CD4+ lymphocytes. We suggest G-1 as a potential antileukemic drug.

Molecular Characterization of the Dual Effect of the GPER Agonist G-1 in Glioblastoma

Int J Mol Sci2022 Nov 18;23(22):14309.PMID: 36430793DOI: 10.3390/ijms232214309

Glioblastoma (GBM) is the most common primary brain tumor in adults. Despite conventional treatment, consisting of a chirurgical resection followed by concomitant radio-chemotherapy, the 5-year survival rate is less than 5%. Few risk factors are clearly identified, but women are 1.4-fold less affected than men, suggesting that hormone and particularly estrogen signaling could have protective properties. Indeed, a high GPER1 (G-protein-coupled estrogen receptor) expression is associated with better survival, especially in women who produce a greater amount of estrogen. Therefore, we addressed the anti-tumor effect of the GPER agonist G-1 in vivo and characterized its molecular mechanism of action in vitro. First, the antiproliferative effect of G-1 was confirmed in a model of xenografted nude mice. A transcriptome analysis of GBM cells exposed to G-1 was performed, followed by functional analysis of the differentially expressed genes. Lipid and steroid synthesis pathways as well as cell division processes were both affected by G-1, depending on the dose and duration of the treatment. ANGPTL4, the first marker of G-1 exposure in GBM, was identified and validated in primary GBM cells and patient samples. These data strongly support the potential of G-1 as a promising chemotherapeutic compound for the treatment of GBM.

Determination of Clonogenic Radiosensitivity of HeLa Cells in Early and Late G1 Phases

Anticancer Res2022 Nov;42(11):5407-5413.PMID: 36288874DOI: 10.21873/anticanres.16045

Background/aim: Using a fluorescent ubiquitination-based cell cycle indicator (Fucci), we recently reported that post irradiation of HeLa cells, micronuclei frequency increased in the early G1 phase in comparison with that in the late G1 phase. This is inconsistent with the results of well-recognized studies that used clonogenic assays. In this study, we determined radiosensitivity of the cells using a clonogenic assay by making the best use of the Fucci property, while simultaneously characterizing cell cycle kinetics and DNA damage responses.
Materials and methods: Early and late G1 phase cell fractions were isolated using a cell sorter by exploiting the different red fluorescence intensities of Fucci. Radiosensitivity was determined by the colony formation assay. Time-lapse imaging and immunostaining were performed to analyze cell cycle kinetics and DNA damage.
Results: Late G1 cells were more radioresistant than early G1 cells. Cells irradiated in the early and late G1 phases induced G2 arrest, while the latter demonstrated a significantly longer duration of G2 arrest. This difference became more evident as the radiation dose increased. Furthermore, 16 h after irradiation, a greater number of γH2AX foci remained in cells irradiated in the early G1 phase than in those irradiated in the late G1 phase.
Conclusion: HeLa cells in the late G1 phase are more radioresistant than those in the early G1 phase, presumably because DNA damage is efficiently repaired during a longer G2 arrest in late G1 cells.

Interaction of aflatoxin G1 with free DNA in vitro and possibility of its application in removing aflatoxin G1

J Environ Sci Health B2021;56(10):932-940.PMID: 34554053DOI: 10.1080/03601234.2021.1979838

The present study sought to evaluate the interaction between aflatoxin G1 and free DNA in vitro through different analytical techniques. The UV-visible spectra results showed that the structure of DNA might be changed with a new aflatoxin G1-DNA complex forming, which indicated that the interacting mode between them was the intercalating mode. The DNA melting temperature increased by 12.80 °C, suggesting that the DNA double helix structure was more compact and stable through intercalation. The circular dichroism (CD) spectra results indicated that the interaction of aflatoxin G1 with DNA induced the DNA base stacking changes. The results of agarose gel electrophoresis and fluorescence microscope further verified that the interacting mode between aflatoxin G1 and DNA was intercalation mode. According to the fluorescence spectrum data, the binding constant was calculated 6.24 × 104 L·mol-1. The thermodynamic results demonstrated that the reaction of aflatoxin G1 intercalating to DNA was a spontaneous reaction. The elimination results suggested that aflatoxin G1 could be enriched and removed by DNA intercalation through magnetic beads separation, with the removal efficiency of 93.73%. The study results would provide a theoretical basis for establishing a new aflatoxin removal method based on DNA intercalation.

Final checkup of neoplastic DNA replication: evidence for failure in decision-making at the mitotic cell cycle checkpoint G(1)/S

Exp Hematol2008 Nov;36(11):1403-16.PMID: 18940520DOI: 10.1016/j.exphem.2008.07.009

Objectives: Processing of epigenomic transcriptional information by cell cycle phase G(1) and decision-making at checkpoint G(1)/S are the final organizational steps preceding gene replication in transcriptional reorientation programs (i.e., switches from proliferation to cycle arrest and neoplastic transformation). Further analyses of cycle progression will open up new approaches in antineoplastic therapy.
Materials and methods: The following bibliographic databases were consulted: Central Medical Library Cologne, PubMed (English), the last search was done on April 23,2008 and key words searched were: cell cycle, cell memory, DNA methylation, embryonal/neoplastic stem cells, enzyme-modulated chromatin, G(1)-G(1)/S checkpoint, genomic/epigenomics, genomic viral DNA, histones, telomere/telomerases, transcription factors, neoplastic transformation, senescence.
Results: Gene transcription and epigenomic surveillance form a functional entity. In proliferation programs, transcriptional information is mediated by chromatin and DNA methylation, analyzed and processed in G(1) phase, and converged on the parental checkpoint G(1)/S for final decision-making on DNA replication. Genomic reorientation appears to be associated with transcriptional instability, which normally is corrected, possibly during the G(2)/M phase, to new levels of epigenomic equilibria. We speculate that daughter stem cells inherit persistent neoplasm-specific transcriptional instabilities through failure of the parental G(1)/S checkpoint. Foreign, silenced, potentially oncogenic DNA sequences, i.e. regular components of the human genome such as endogenous retroviruses, could conceivably be activated for expression in neoplastic transformation by epigenomic histone deacetylase/acetyl transferase/histone methyltransferase-mixed lineage leukemia deregulations.
Conclusions: Failure of cell cycle G(1)/S decision-making for DNA replication is the final and possibly a major cause in neoplastic transformation. Therefore, further analysis of the dynamics of G(1)-G(1)/Sphases could provide new opportunities for therapeutic strategies.