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Caco-2

RRID:CVCL_0025

Organism

Homo sapiens

Comments

Part of: AstraZeneca Colorectal cell line (AZCL) panel. Part of: Cancer Cell Line Encyclopedia (CCLE) project. Part of: ENCODE project common cell types; tier 3. Part of: MD Anderson Cell Lines Project. Doubling time: ~80 hours (DSMZ); ~32 hours (PBCF); ~60-70 hours (CLS). HLA typing: A*02:01,02:01; B*15:05,56/39; C*04:01,04:01 (PubMed=25960936). Microsatellite instability: Stable (MSS) (PubMed=24042735; PubMed=25926053; PubMed=28683746). Sequence variation: APC p.Gln1367Ter (c.4099C>T) (PubMed=24755471; CCLE). Sequence variation: Heterozygous for CTNNB1 p.Gly245Ala (c.734G>C) (PubMed=9294210). Sequence variation: SMAD4 p.Asp351His (c.1051G>C) (PubMed=24755471; CCLE). Sequence variation: TP53 p.Glu204Ter (c.610G>T) (PubMed=16418264; PubMed=24755471; PubMed=28683746; CCLE). Omics: Deep antibody staining analysis. Omics: Deep exome analysis. Omics: Deep phosphoproteome analysis. Omics: Deep proteome analysis. Omics: Deep RNAseq analysis. Omics: H3K4me3 ChIP-seq epigenome analysis. Omics: H3K27me3 ChIP-seq epigenome analysis. Omics: H3K36me3 ChIP-seq epigenome analysis. Omics: miRNA expression profiling. Omics: N-glycan profiling. Omics: Protein expression by reverse-phase protein arrays. Omics: SNP array analysis. Omics: Transcriptome analysis. Genome ancestry: African=3.33%; Native American=0%; East Asian, North=4.59%; East Asian, South=0%; South Asian=0%; European, North=47.35%; European, South=44.73% (PubMed=30894373). DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Proper Citation

CLS Cat# 300137/p1665_CaCo-2, RRID:CVCL_0025

Category

Cancer cell line DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Sex

DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Synonyms

CaCo-2, CACO-2, Caco 2, CACO 2, CACO2, CaCo2, CaCO2, Caco2, Caco-2/ATCC DT Created: 04-04-12, Last updated: 05-07-19, Version: 31

Vendor

CLS

Cat Num

300137/p1665_CaCo-2

Cross References

BTO; BTO:0000195 CLO; CLO_0002172 CLO; CLO_0050627 EFO; EFO_0001099 MCCL; MCC:0000120 CLDB; cl614 CLDB; cl615 CLDB; cl616 CLDB; cl617 CLDB; cl618 CLDB; cl619 CLDB; cl621 CLDB; cl5174 AddexBio; C0009009/29 ArrayExpress; E-MTAB-2706 ATCC; HTB-37 BCRJ; 0059 BioSample; SAMN03473140 BioSample; SAMN05292461 BioSample; SAMN10989600 CCLE; CACO2_LARGE_INTESTINE CCRID; 3111C0001CCC000100 CCRID; 3131C0001000700066 CCRID; 3131C0001000700146 CCRID; 3142C0001000000137 CCTCC; GDC0153 Cell_Model_Passport; SIDM00891 ChEMBL-Cells; CHEMBL3307519 ChEMBL-Targets; CHEMBL614058 CLS; 300137/p1665_CaCo-2 ColonAtlas; CACO2 Cosmic; 720340 Cosmic; 873696 Cosmic; 875297 Cosmic; 876709 Cosmic; 887244 Cosmic; 889531 Cosmic; 948127 Cosmic; 948829 Cosmic; 983736 Cosmic; 995392 Cosmic; 1043805 Cosmic; 1122320 Cosmic; 1132564 Cosmic; 1132694 Cosmic; 1184081 Cosmic; 1187299 Cosmic; 1310931 Cosmic; 1466811 Cosmic; 1479620 Cosmic; 1524334 Cosmic; 1552180 Cosmic; 1676742 Cosmic; 1708415 Cosmic; 1803940 Cosmic; 1933015 Cosmic; 2036652 Cosmic; 2145574 Cosmic; 2156940 Cosmic; 2301543 Cosmic; 2301964 Cosmic; 2667879 DepMap; ACH-000003 DSMZ; ACC-169 ECACC; 09042001 ECACC; 86010202 ENCODE; ENCBS311PHE ENCODE; ENCBS390JMI ENCODE; ENCBS391ENC ENCODE; ENCBS530YXL ENCODE; ENCBS700RKG ENCODE; ENCBS890JZY FCS-free; 192-2-378-1-3-3 GEO; GSM206450 GEO; GSM274711 GEO; GSM274712 GEO; GSM274725 GEO; GSM472900 GEO; GSM472933 GEO; GSM513908 GEO; GSM514182 GEO; GSM741244 GEO; GSM784006 GEO; GSM845394 GEO; GSM843481 GEO; GSM843482 GEO; GSM945162 GEO; GSM945203 GEO; GSM945206 GEO; GSM945236 GEO; GSM1006210 GEO; GSM1006211 GEO; GSM1006212 GEO; GSM1346866 GEO; GSM1374426 GEO; GSM1448160 GEO; GSM2549989 IARC_TP53; 21749 IBRC; C10094 ICLC; HTL97023 IZSLER; BS TCL 87 KCB; KCB 200710YJ KCLB; 30037.1 LINCS_LDP; LCL-1170 Lonza; 36 MeSH; D018938 MetaboLights; MTBLS227 MetaboLights; MTBLS328 NCBI_Iran; C139 PRIDE; PXD001550 PRIDE; PXD005354 RCB; RCB0988 TOKU-E; 762 Wikidata; Q5016050 DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Hierarchy

DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Originate from Same Individual

DT Created: 04-04-12; Last updated: 05-07-19; Version: 31

Mitochondria Restrict Growth of the Intracellular Parasite Toxoplasma gondii by Limiting Its Uptake of Fatty Acids.

  • Pernas L
  • Cell Metab.
  • 2018 Apr 3

Literature context:


Abstract:

How intracellular pathogens acquire essential non-diffusible host metabolites and whether the host cell counteracts the siphoning of these nutrients by its invaders are open questions. Here we show that host mitochondria fuse during infection by the intracellular parasite Toxoplasma gondii to limit its uptake of fatty acids (FAs). A combination of genetics and imaging of FA trafficking indicates that Toxoplasma infection triggers lipophagy, the autophagy of host lipid droplets (LDs), to secure cellular FAs essential for its proliferation. Indeed, Toxoplasma FA siphoning and growth are reduced in host cells genetically deficient for autophagy or triglyceride depots. Conversely, Toxoplasma FA uptake and proliferation are increased in host cells lacking mitochondrial fusion, required for efficient mitochondrial FA oxidation, or where mitochondrial FA oxidation is pharmacologically inhibited. Thus, mitochondrial fusion can be regarded as a cellular defense mechanism against intracellular parasites, by limiting Toxoplasma access to host nutrients liberated by lipophagy.

Funding information:
  • NIAID NIH HHS - 5 R44 AI051036(United States)

Listeria Adhesion Protein Induces Intestinal Epithelial Barrier Dysfunction for Bacterial Translocation.

  • Drolia R
  • Cell Host Microbe
  • 2018 Apr 11

Literature context:


Abstract:

Intestinal epithelial cells are the first line of defense against enteric pathogens, yet bacterial pathogens, such as Listeria monocytogenes, can breach this barrier. We show that Listeria adhesion protein (LAP) induces intestinal epithelial barrier dysfunction to promote bacterial translocation. These disruptions are attributed to the production of pro-inflammatory cytokines TNF-α and IL-6, which is observed in mice challenged with WT and isogenic strains lacking the surface invasion protein Internalin A (ΔinlA), but not a lap- mutant. Additionally, upon engagement of its surface receptor Hsp60, LAP activates canonical NF-κB signaling, facilitating myosin light-chain kinase (MLCK)-mediated opening of the epithelial barrier via cellular redistribution of the epithelial junctional proteins claudin-1, occludin, and E-cadherin. Pharmacological inhibition of MLCK or NF-κB in cells or genetic ablation of MLCK in mice prevents mislocalization of junctional proteins and L. monocytogenes translocation. Thus, L. monocytogenes uses LAP to exploit epithelial defenses and cross the intestinal epithelial barrier.

Funding information:
  • Howard Hughes Medical Institute - HD043569(United States)

The HDAC6 Inhibitor Tubacin Induces Release of CD133+ Extracellular Vesicles From Cancer Cells.

  • Chao OS
  • J. Cell. Biochem.
  • 2018 Jan 2

Literature context:


Abstract:

Tumor-derived extracellular vesicles (EVs) are emerging as an important mode of intercellular communication, capable of transferring biologically active molecules that facilitate the malignant growth and metastatic process. CD133 (Prominin-1), a stem cell marker implicated in tumor initiation, differentiation and resistance to anti-cancer therapy, is reportedly associated with EVs in various types of cancer. However, little is known about the factors that regulate the release of these CD133+ EVs. Here, we report that the HDAC6 inhibitor tubacin promoted the extracellular release of CD133+ EVs from human FEMX-I metastatic melanoma and Caco-2 colorectal carcinoma cells, with a concomitant downregulation of intracellular CD133. This effect was specific for tubacin, as inhibition of HDAC6 deacetylase activity by another selective HDAC6 inhibitor, ACY-1215 or the pan-HDAC inhibitor trichostatin A (TSA), and knockdown of HDAC6 did not enhance the release of CD133+ EVs. The tubacin-induced EV release was associated with changes in cellular lipid composition, loss of clonogenic capacity and decrease in the ability to form multicellular aggregates. These findings indicate a novel potential anti-tumor mechanism for tubacin in CD133-expressing malignancies. J. Cell. Biochem. 118: 4414-4424, 2017. © 2017 Wiley Periodicals, Inc.

Nicotine increases colon cancer cell migration and invasion through epithelial to mesenchymal transition (EMT): COX-2 involvement.

  • Dinicola S
  • J. Cell. Physiol.
  • 2017 Dec 8

Literature context:


Abstract:

Cigarette smoking is a recognized risk factor for colon cancer and nicotine, the principal active component of tobacco, plays a pivotal role in increasing colon cancer cell growth and survival. The aim of this study was to determine the effect of nicotine on cellular Caco-2 and HCT-8 migration and invasion, focusing on epithelial to mesenchymal transition (EMT) induction, and COX-2 pathway involvement. In both these cell lines, treatment with nicotine increased COX-2 expression and the release of its enzymatic product PGE2 . Moreover, nicotine-stimulated cells showed increased migratory and invasive behavior, mesenchymal markers up-regulation and epithelial markers down-regulation, nuclear translocation of the β-catenin, increase of MMP-2 and MMP-9 activity, and enhanced NF-κB expression. Noticeably, all these effects are largely mediated by COX-2 activity, as simultaneous treatment of both cell lines with nicotine and NS-398, a selective COX-2 inhibitor, greatly reduced the number of migrating and invading cells and reverted nicotine-induced EMT. These findings emphasize that nicotine triggers EMT, leading hence to increased migration and invasiveness of colon cancer cells. Thereby, the use of COX-2 inhibitor drugs might likely counteract nicotine-mediated EMT effects on colon cancer development and progression.

Funding information:
  • NCI NIH HHS - R01 CA119018-04(United States)

Epiregulin (EREG) is upregulated through an IL-1β autocrine loop in Caco-2 epithelial cells with reduced CFTR function.

  • Massip-Copiz M
  • J. Cell. Biochem.
  • 2017 Nov 2

Literature context:


Abstract:

CFTR is a cAMP-regulated chloride channel, whose mutations produce cystic fibrosis. The impairment of CFTR activity increases the intracellular Cl- concentration, which in turn produces an increased interleukin-1β (IL-1β) secretion. The secreted IL-1β then induces an autocrine positive feedback loop, further stimulating IL-1β priming and secretion. Since IL-1β can transactivate the epidermal growth factor receptor (EGFR), we study here the levels of expression for different EGFR ligands in Caco-2/pRS26 cells (expressing shRNA against CFTR resulting in a reduced CFTR expression and activity). The epiregulin (EREG), amphiregulin (AREG), and heparin binding EGF like growth factor (HBEGF) mRNAs, were found overexpressed in Caco-2/pRS26 cells. The EREG mRNA had the highest differential expression and was further characterized. In agreement with its mRNA levels, Western blots (WB) showed increased EREG levels in CFTR-impaired cells. In addition, EREG mRNA and protein levels were stimulated by incubation with exogenous IL-1β and inhibited by the Interleukin 1 receptor type I (IL1R1) antagonist IL1RN, suggesting that the overexpression of EREG is a consequence of the autocrine IL-1β loop previously described for these cells. In addition, the JNK inhibitor SP600125, and the EGFR inhibitors AG1478 and PD168393, also had an inhibitory effect on EREG expression, suggesting that EGFR, activated in Caco-2/pRS26 cells, is involved in the observed EREG upregulation. In conclusion, in Caco-2 CFTR-shRNA cells, the EGFR ligand EREG is overexpressed due to an active IL-1β autocrine loop that indirectly activates EGFR, constituting new signaling effectors for the CFTR signaling pathway, downstream of CFTR, Cl- , and IL-1β.

Promotion of Early Gut Colonization by Probiotic Intervention on Microbiota Diversity in Pregnant Sows.

  • Veljović K
  • Front Microbiol
  • 2017 Nov 7

Literature context:


Abstract:

The aim of this work was to design a novel mixed probiotic culture for piglets and to evaluate its beneficial effect on the piglets' gut health. The possible mechanisms of probiotic activity, such as adhesion, competitive pathogen exclusion and influence on gut microbiota diversity were determined. Mixed probiotic starter culture is composed of three thermophilic lactic acid bacteria (LAB) strains: Lactobacillus helveticus BGRA43, Lactobacillus fermentum BGHI14 and Streptococcus thermophilus BGVLJ1-44. The strains BGVLJ1-44 and BGRA43 showed good technological properties (fast milk curdling, strong proteolytic activity). In addition, the strain BGVLJ1-44 produces exopolysaccharide (EPS), BGHI14 is heterofermentative LAB strain with significant immunomodulatory effect, while the strain BGRA43 showed strong antimicrobial activity against different pathogens and exhibited significantly higher level of adhesion to Caco-2 cells comparing to other two strains. Both lactobacilli strains BGRA43 and BGHI14 (p < 0.05), as well as probiotic combination (p < 0.01) significantly reduced the adhesion of Escherichia coli ATCC25922 to Caco-2 cells, while the strains BGVLJ1-44 (p < 0.01) and BGRA43 (p < 0.05) significantly reduced adhesion of Salmonella 654/7E (veterinary isolate). The results of farm trial revealed that treatment of sows with new fermented dairy probiotic influenced the piglets' gut colonization with beneficial bacteria and reduced the number of enterobacteriaceae in litters from some treated sows (no significant due to high variability among animals). Finally, this is the first study reporting that the treatment of sows with probiotic combination resulted in the improved microbiota diversity in neonatal piglets.

Funding information:
  • NINDS NIH HHS - R37NS008174(United States)

PTEN controls glandular morphogenesis through a juxtamembrane β-Arrestin1/ARHGAP21 scaffolding complex.

  • Javadi A
  • Elife
  • 2017 Jul 27

Literature context:


Abstract:

PTEN controls three-dimensional (3D) glandular morphogenesis by coupling juxtamembrane signaling to mitotic spindle machinery. While molecular mechanisms remain unclear, PTEN interacts through its C2 membrane-binding domain with the scaffold protein β-Arrestin1. Because β-Arrestin1 binds and suppresses the Cdc42 GTPase-activating protein ARHGAP21, we hypothesize that PTEN controls Cdc42 -dependent morphogenic processes through a β-Arrestin1-ARHGAP21 complex. Here, we show that PTEN knockdown (KD) impairs β-Arrestin1 membrane localization, β-Arrestin1-ARHGAP21 interactions, Cdc42 activation, mitotic spindle orientation and 3D glandular morphogenesis. Effects of PTEN deficiency were phenocopied by β-Arrestin1 KD or inhibition of β-Arrestin1-ARHGAP21 interactions. Conversely, silencing of ARHGAP21 enhanced Cdc42 activation and rescued aberrant morphogenic processes of PTEN-deficient cultures. Expression of the PTEN C2 domain mimicked effects of full-length PTEN but a membrane-binding defective mutant of the C2 domain abrogated these properties. Our results show that PTEN controls multicellular assembly through a membrane-associated regulatory protein complex composed of β-Arrestin1, ARHGAP21 and Cdc42.

Computationally designed high specificity inhibitors delineate the roles of BCL2 family proteins in cancer.

  • Berger S
  • Elife
  • 2016 Nov 2

Literature context:


Abstract:

Many cancers overexpress one or more of the six human pro-survival BCL2 family proteins to evade apoptosis. To determine which BCL2 protein or proteins block apoptosis in different cancers, we computationally designed three-helix bundle protein inhibitors specific for each BCL2 pro-survival protein. Following in vitro optimization, each inhibitor binds its target with high picomolar to low nanomolar affinity and at least 300-fold specificity. Expression of the designed inhibitors in human cancer cell lines revealed unique dependencies on BCL2 proteins for survival which could not be inferred from other BCL2 profiling methods. Our results show that designed inhibitors can be generated for each member of a closely-knit protein family to probe the importance of specific protein-protein interactions in complex biological processes.

Funding information:
  • NIDDK NIH HHS - R21 DK106584(United States)