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MDA-MB-231

RRID:CVCL_0062

Organism

Homo sapiens

Comments

Part of: Cancer Cell Line Encyclopedia (CCLE) project. Part of: ENCODE project common cell types; tier 3. Part of: ICBP43 breast cancer cell line panel. Part of: JFCR39 cancer cell line panel. Part of: JFCR45 cancer cell line panel. Part of: KuDOS 95 cell line panel. Part of: MD Anderson Cell Lines Project. Part of: NCI60 cancer cell line panel. Registration: Chiron Master Culture Collection; CMCC 10583 (CMCC #10583). Doubling time: 1.3 days (PubMed=9671407); 41.9 hours (NCI-DTP); 38 hours (ATCC); ~25-30 hours (DSMZ). Microsatellite instability: Stable (MSS) (PubMed=12661003; Sanger). Sequence variation: TP53 p.Arg280Lys (PubMed=18277095). Omics: Array-based CGH. Omics: Cell surface proteome. Omics: CNV analysis. Omics: Deep exome analysis. Omics: Deep proteome analysis. Omics: Deep RNAseq analysis. Omics: DNA methylation analysis. Omics: Fluorescence phenotype profiling. Omics: lncRNA expression profiling. Omics: Metabolome analysis. Omics: miRNA expression profiling. Omics: N-glycan profiling. Omics: Protein expression by reverse-phase protein arrays. Omics: Secretome proteome analysis. Omics: SNP array analysis. Omics: Transcriptome analysis. Misspelling: 'MDA-MD-231' in Cosmic 1071900 and Cosmic 1176602. Misspelling: 'MDA-321' in GEO GSM459713. Misspelling: 'MDA-MG-231' in PubMed=6582512. Discontinued: ATCC; CRL-12532. Derived from metastatic site: Pleural effusion.

Proper Citation

BCRJ Cat# 0164, RRID:CVCL_0062

Category

Cancer cell line

Sex

Female

Synonyms

MDA-MB 231, MDA.MB.231, MDA MB 231, MDA MB231, MDA Mb231, MDA-MB231, MDAMB-231, MDAMB231, MDA-231, MDA231, MB231

Vendor

BCRJ

Cat Num

0164

Cross References

BTO; BTO:0000815 CLO; CLO_0007634 EFO; EFO_0001209 MCCL; MCC:0000313 CLDB; cl3402 CLDB; cl3404 CLDB; cl3405 CLDB; cl4945 ATCC; CRL-12532 ATCC; HTB-26 ATCC; CRM-HTB-26 BCRC; 60425 BCRJ; 0164 BioSample; SAMN03472205 CCLE; MDAMB231_BREAST CCRID; 3111C0001CCC000014 CCRID; 3131C0001000700104 ChEMBL-Cells; CHEMBL3307960 ChEMBL-Targets; CHEMBL400 CLS; 300275/p536_MDA-MB-231 Cosmic; 687494 Cosmic; 871146 Cosmic; 875878 Cosmic; 877450 Cosmic; 894087 Cosmic; 897423 Cosmic; 904377 Cosmic; 905960 Cosmic; 934536 Cosmic; 944294 Cosmic; 974235 Cosmic; 991324 Cosmic; 997929 Cosmic; 1010924 Cosmic; 1018477 Cosmic; 1027053 Cosmic; 1044226 Cosmic; 1046950 Cosmic; 1047693 Cosmic; 1071900 Cosmic; 1092613 Cosmic; 1136369 Cosmic; 1152528 Cosmic; 1175833 Cosmic; 1176602 Cosmic; 1176636 Cosmic; 1183773 Cosmic; 1219444 Cosmic; 1287926 Cosmic; 1289395 Cosmic; 1305383 Cosmic; 1309003 Cosmic; 1312370 Cosmic; 1434952 Cosmic; 1436032 Cosmic; 1466805 Cosmic; 1477428 Cosmic; 1481426 Cosmic; 1524347 Cosmic; 1571793 Cosmic; 1609458 Cosmic; 1927242 Cosmic; 1945862 Cosmic; 1998455 Cosmic; 2009512 Cosmic; 2036667 Cosmic; 2164997 Cosmic; 2301528 Cosmic; 2318377 Cosmic; 2361355 Cosmic-CLP; 905960 DSMZ; ACC-732 ECACC; 92020424 GDSC; 905960 GEO; GSM812 GEO; GSM50184 GEO; GSM50248 GEO; GSM69194 GEO; GSM155213 GEO; GSM185093 GEO; GSM185094 GEO; GSM274653 GEO; GSM344349 GEO; GSM344399 GEO; GSM350547 GEO; GSM378148 GEO; GSM388213 GEO; GSM459713 GEO; GSM481304 GEO; GSM587393 GEO; GSM587394 GEO; GSM750781 GEO; GSM799321 GEO; GSM799384 GEO; GSM847036 GEO; GSM847401 GEO; GSM844594 GEO; GSM844595 GEO; GSM887295 GEO; GSM888370 GEO; GSM967818 GEO; GSM1008905 GEO; GSM1053716 GEO; GSM1153390 GEO; GSM1172979 GEO; GSM1172889 GEO; GSM1181242 GEO; GSM1181365 GEO; GSM1214569 GEO; GSM1374651 GEO; GSM1374652 GEO; GSM1401658 GEO; GSM1613823 GEO; GSM1670080 GEO; GSM1833624 GEO; GSM2095710 GEO; GSM2095711 GEO; GSM2124643 ICLC; HTL99004 IZSLER; BS TCL 223 KCB; KCB 200776YJ KCLB; 30026 LINCS_HMS; 50058 LINCS_LDP; LCL-1461 Lonza; 815 NCBI_Iran; C578 NCI-DTP; MDA-MB-231 PRIDE; PXD000239 PRIDE; PXD000397 PRIDE; PXD000691 PRIDE; PXD000914 PRIDE; PXD001553 PRIDE; PXD002192 PRIDE; PXD002649 SKY/M-FISH/CGH; 2815 TOKU-E; 2394 Wikidata; Q17577870

GLUL Promotes Cell Proliferation in Breast Cancer.

  • Wang Y
  • J. Cell. Biochem.
  • 2017 Aug 28

Literature context: RL-12532, RRID:CVCL_0062), and MCF7


Abstract:

Glutamate-ammonia ligase (GLUL) belongs to the glutamine synthetase family. It catalyzes the synthesis of glutamine from glutamate and ammonia in an ATP-dependent reaction. Here, we found higher expression of GLUL in the breast cancer patients was associated with larger tumor size and higher level of HER2 expression. In addition, GLUL was heterogeneously expressed in various breast cancer cells. The mRNA and protein expression levels of GLUL in SK-BR-3 cells were obviously higher than that in the other types of breast cancer cells. Results showed GLUL knockdown in SK-BR-3 cells could significantly decrease the proliferation ability. Furthermore, GLUL knockdown markedly inhibited the p38 MAPK and ERK1/ERK2 signaling pathways in SK-BR-3 cells. Thus, GLUL may represent a novel target for selectively inhibiting p38 MAPK and ERK1/ERK2 signaling pathways and the proliferation potential of breast cancer cells. J. Cell. Biochem. 118: 2018-2025, 2017. © 2016 Wiley Periodicals, Inc.

Focal Adhesion- and IGF1R-Dependent Survival and Migratory Pathways Mediate Tumor Resistance to mTORC1/2 Inhibition.

  • Yoon SO
  • Mol. Cell
  • 2017 Aug 3

Literature context: Models: Cell LinesMDA-MB-231ATCCHTB-26AU565ATCCCRL-2351MDA-MB-468ATCCH


Abstract:

Aberrant signaling by the mammalian target of rapamycin (mTOR) contributes to the devastating features of cancer cells. Thus, mTOR is a critical therapeutic target and catalytic inhibitors are being investigated as anti-cancer drugs. Although mTOR inhibitors initially block cell proliferation, cell viability and migration in some cancer cells are quickly restored. Despite sustained inhibition of mTORC1/2 signaling, Akt, a kinase regulating cell survival and migration, regains phosphorylation at its regulatory sites. Mechanistically, mTORC1/2 inhibition promotes reorganization of integrin/focal adhesion kinase-mediated adhesomes, induction of IGFR/IR-dependent PI3K activation, and Akt phosphorylation via an integrin/FAK/IGFR-dependent process. This resistance mechanism contributes to xenograft tumor cell growth, which is prevented with mTOR plus IGFR inhibitors, supporting this combination as a therapeutic approach for cancers.

Sam68 Allows Selective Targeting of Human Cancer Stem Cells.

  • Benoit YD
  • Cell Chem Biol
  • 2017 Jul 20

Literature context: PMID:19122652OCI AML3DSMZACC 582MDA-MB-231ATCC ®HTB-26™MCF7ATCC®HTB-22™HT29ATCC®HTB-38™


Abstract:

Targeting of human cancer stem cells (CSCs) requires the identification of vulnerabilities unique to CSCs versus healthy resident stem cells (SCs). Unfortunately, dysregulated pathways that support transformed CSCs, such as Wnt/β-catenin signaling, are also critical regulators of healthy SCs. Using the ICG-001 and CWP family of small molecules, we reveal Sam68 as a previously unappreciated modulator of Wnt/β-catenin signaling within CSCs. Disruption of CBP-β-catenin interaction via ICG-001/CWP induces the formation of a Sam68-CBP complex in CSCs that alters Wnt signaling toward apoptosis and differentiation induction. Our study identifies Sam68 as a regulator of human CSC vulnerability.

Amplification of F-Actin Disassembly and Cellular Repulsion by Growth Factor Signaling.

  • Yoon J
  • Dev. Cell
  • 2017 Jul 24

Literature context: 0Experimental Models: Cell LinesHuman: MDA-MB-231 cellsATCCHTB-26Human: MCF-7 cellsATCCHTB-22Huma


Abstract:

Extracellular cues that regulate cellular shape, motility, and navigation are generally classified as growth promoting (i.e., growth factors/chemoattractants and attractive guidance cues) or growth preventing (i.e., repellents and inhibitors). Yet, these designations are often based on complex assays and undefined signaling pathways and thus may misrepresent direct roles of specific cues. Here, we find that a recognized growth-promoting signaling pathway amplifies the F-actin disassembly and repulsive effects of a growth-preventing pathway. Focusing on Semaphorin/Plexin repulsion, we identified an interaction between the F-actin-disassembly enzyme Mical and the Abl tyrosine kinase. Biochemical assays revealed Abl phosphorylates Mical to directly amplify Mical Redox-mediated F-actin disassembly. Genetic assays revealed that Abl allows growth factors and Semaphorin/Plexin repellents to combinatorially increase Mical-mediated F-actin disassembly, cellular remodeling, and repulsive axon guidance. Similar roles for Mical in growth factor/Abl-related cancer cell behaviors further revealed contexts in which characterized positive effectors of growth/guidance stimulate such negative cellular effects as F-actin disassembly/repulsion.

mTORC2 Regulates Amino Acid Metabolism in Cancer by Phosphorylation of the Cystine-Glutamate Antiporter xCT.

  • Gu Y
  • Mol. Cell
  • 2017 Jul 6

Literature context: CCHTB-17Human: Hs578TATCCHTB-126Human: MDA-MB-231ATCCHTB-26Human: A549ATCCCCL-185Human: HEK


Abstract:

Mutations in cancer reprogram amino acid metabolism to drive tumor growth, but the molecular mechanisms are not well understood. Using an unbiased proteomic screen, we identified mTORC2 as a critical regulator of amino acid metabolism in cancer via phosphorylation of the cystine-glutamate antiporter xCT. mTORC2 phosphorylates serine 26 at the cytosolic N terminus of xCT, inhibiting its activity. Genetic inhibition of mTORC2, or pharmacologic inhibition of the mammalian target of rapamycin (mTOR) kinase, promotes glutamate secretion, cystine uptake, and incorporation into glutathione, linking growth factor receptor signaling with amino acid uptake and utilization. These results identify an unanticipated mechanism regulating amino acid metabolism in cancer, enabling tumor cells to adapt to changing environmental conditions.

Synergistic interactions with PI3K inhibition that induce apoptosis.

  • Zwang Y
  • Elife
  • 2017 May 31

Literature context: A-MB-231 (RRID:CVCL_0062), CAL-120


Abstract:

Activating mutations involving the PI3K pathway occur frequently in human cancers. However, PI3K inhibitors primarily induce cell cycle arrest, leaving a significant reservoir of tumor cells that may acquire or exhibit resistance. We searched for genes that are required for the survival of PI3K mutant cancer cells in the presence of PI3K inhibition by conducting a genome scale shRNA-based apoptosis screen in a PIK3CA mutant human breast cancer cell. We identified 5 genes (PIM2, ZAK, TACC1, ZFR, ZNF565) whose suppression induced cell death upon PI3K inhibition. We showed that small molecule inhibitors of the PIM2 and ZAK kinases synergize with PI3K inhibition. In addition, using a microscale implementable device to deliver either siRNAs or small molecule inhibitors in vivo, we showed that suppressing these 5 genes with PI3K inhibition induced tumor regression. These observations identify targets whose inhibition synergizes with PI3K inhibitors and nominate potential combination therapies involving PI3K inhibition.

Cellular Migration Ability Is Modulated by Extracellular Purines in Ovarian Carcinoma SKOV-3 Cells.

  • Martínez-Ramírez AS
  • J. Cell. Biochem.
  • 2017 May 2

Literature context: 75/p536_MDA-MB-231, RRID:CVCL_0062) cells. These cellular lines we


Abstract:

Extracellular nucleotides and nucleosides have emerged as important elements regulating tissue homeostasis. Acting through specific receptors, have the ability to control gene expression patterns to direct cellular fate. We observed that SKOV-3 cells express the ectonucleotidases: ectonucleotide pyrophosphatase 1 (ENPP1), ecto-5'-nucleotidase (NT5E), and liver alkaline phosphatase (ALPL). Strikingly, in pulse and chase experiments supplemented with ATP, SKOV-3 cells exhibited low catabolic efficiency in the conversion of ADP into AMP, but they were efficient in converting AMP into adenosine. Since these cells release ATP, we proposed that the conversion of ADP into AMP is a regulatory node associated with the migratory ability and the mesenchymal characteristics shown by SKOV-3 cells under basal conditions. The landscape of gene expression profiles of SKOV-3 cell cultures treated with apyrase or adenosine demonstrated similarities (e.g., decrease FGF16 transcript) and differences (e.g., the negative regulation of Wnt 2, and 10B by adenosine). Thus, in SKOV-3 we analyzed the migratory ability and the expression of epithelium to mesenchymal transition (EMT) markers in response to apyrase. Apyrase-treatment favored the epithelial-like phenotype, as revealed by the re-location of E-cadherin to the cell to cell junctions. Pharmacological approaches strongly suggested that the effect of Apyrase involved the accumulation of extracellular adenosine; this notion was strengthened when the incubation of the SKOV-3 cell with α,β-methylene ADP (CD73 inhibitor) or adenosine deaminase was sufficient to abolish the effect of apyrase on cell migration. Overall, adenosine signaling is a fine tune mechanism in the control of cell phenotype in cancer. J. Cell. Biochem. 9999: 1-11, 2017. © 2017 Wiley Periodicals, Inc.

TGF-β reduces DNA ds-break repair mechanisms to heighten genetic diversity and adaptability of CD44+/CD24- cancer cells.

  • Pal D
  • Elife
  • 2017 Jan 16

Literature context: 31 (RRID:CVCL_0062), MDA-MB-4


Abstract:

Many lines of evidence have indicated that both genetic and non-genetic determinants can contribute to intra-tumor heterogeneity and influence cancer outcomes. Among the best described sub-population of cancer cells generated by non-genetic mechanisms are cells characterized by a CD44+/CD24- cell surface marker profile. Here, we report that human CD44+/CD24- cancer cells are genetically highly unstable because of intrinsic defects in their DNA-repair capabilities. In fact, in CD44+/CD24- cells, constitutive activation of the TGF-beta axis was both necessary and sufficient to reduce the expression of genes that are crucial in coordinating DNA damage repair mechanisms. Consequently, we observed that cancer cells that reside in a CD44+/CD24- state are characterized by increased accumulation of DNA copy number alterations, greater genetic diversity and improved adaptability to drug treatment. Together, these data suggest that the transition into a CD44+/CD24- cell state can promote intra-tumor genetic heterogeneity, spur tumor evolution and increase tumor fitness.

TP53 drives invasion through expression of its Δ133p53β variant.

  • Gadea G
  • Elife
  • 2016 Sep 15

Literature context: 1 (RRID:CVCL-0062), MCF7 (RR


Abstract:

TP53 is conventionally thought to prevent cancer formation and progression to metastasis, while mutant TP53 has transforming activities. However, in the clinic, TP53 mutation status does not accurately predict cancer progression. Here we report, based on clinical analysis corroborated with experimental data, that the p53 isoform Δ133p53β promotes cancer cell invasion, regardless of TP53 mutation status. Δ133p53β increases risk of cancer recurrence and death in breast cancer patients. Furthermore Δ133p53β is critical to define invasiveness in a panel of breast and colon cell lines, expressing WT or mutant TP53. Endogenous mutant Δ133p53β depletion prevents invasiveness without affecting mutant full-length p53 protein expression. Mechanistically WT and mutant Δ133p53β induces EMT. Our findings provide explanations to 2 long-lasting and important clinical conundrums: how WT TP53 can promote cancer cell invasion and reciprocally why mutant TP53 gene does not systematically induce cancer progression.