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CHO

RRID:CVCL_0213

Organism

Cricetulus griseus

Comments

DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

Proper Citation

KCB Cat# KCB 83004YJ, RRID:CVCL_0213

Category

Spontaneously immortalized cell line DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

Sex

DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

Synonyms

Chinese Hamster Ovary, CHO-ori DT Created: 04-04-12, Last updated: 24-05-19, Version: 15

Vendor

KCB

Cat Num

KCB 83004YJ

Cross References

BTO; BTO:0000246 CLO; CLO_0002421 MCCL; MCC:0000102 CLDB; cl721 CLDB; cl722 CLDB; cl724 CCRID; 3111C0001CCC000116 CCRID; 3131C0001000100003 CCRID; 3153C0001000000050 ChEMBL-Cells; CHEMBL3308072 ChEMBL-Targets; CHEMBL613853 CLS; 603479/p746_CHO ECACC; 85050302 IBRC; C10028 ICLC; ATL95003 KCB; KCB 82012YJ KCB; KCB 83004YJ Lonza; 755 MeSH; D016466 NCBI_Iran; C111 Wikidata; Q56646 DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

Hierarchy

DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

Originate from Same Individual

DT Created: 04-04-12; Last updated: 24-05-19; Version: 15

A dual role for Integrin α6β4 in modulating hereditary neuropathy with liability to pressure palsies.

  • Poitelon Y
  • J. Neurochem.
  • 2018 Jan 10

Literature context:


Abstract:

Peripheral myelin protein 22 (PMP22) is a component of compact myelin in the peripheral nervous system. The amount of PMP22 in myelin is tightly regulated, and PMP22 over or under-expression cause Charcot-Marie-Tooth 1A (CMT1A) and Hereditary Neuropathy with Pressure Palsies (HNPP). Despite the importance of PMP22, its function remains largely unknown. It was reported that PMP22 interacts with the β4 subunit of the laminin receptor α6β4 integrin, suggesting that α6β4 integrin and laminins may contribute to the pathogenesis of CMT1A or HNPP. Here we asked if the lack of α6β4 integrin in Schwann cells influences myelin stability in the HNPP mouse model. Our data indicate that PMP22 and β4 integrin may not interact directly in myelinating Schwann cells, however, ablating β4 integrin delays the formation of tomacula, a characteristic feature of HNPP. In contrast, ablation of integrin β4 worsens nerve conduction velocities and non-compact myelin organization in HNPP animals. This study demonstrates that indirect interactions between an extracellular matrix receptor and a myelin protein influence the stability and function of myelinated fibers.

Funding information:
  • NINDS NIH HHS - R01 NS038902(United States)
  • NINDS NIH HHS - R01 NS045630()
  • NINDS NIH HHS - R01 NS100464()

A potent human neutralizing antibody Fc-dependently reduces established HBV infections.

  • Li D
  • Elife
  • 2017 Sep 26

Literature context:


Abstract:

Hepatitis B virus (HBV) infection is a major global health problem. Currently-available therapies are ineffective in curing chronic HBV infection. HBV and its satellite hepatitis D virus (HDV) infect hepatocytes via binding of the preS1 domain of its large envelope protein to sodium taurocholate cotransporting polypeptide (NTCP). Here, we developed novel human monoclonal antibodies that block the engagement of preS1 with NTCP and neutralize HBV and HDV with high potency. One antibody, 2H5-A14, functions at picomolar level and exhibited neutralization-activity-mediated prophylactic effects. It also acts therapeutically by eliciting antibody-Fc-dependent immunological effector functions that impose durable suppression of viral infection in HBV-infected mice, resulting in reductions in the levels of the small envelope antigen and viral DNA, with no emergence of escape mutants. Our results illustrate a novel antibody-Fc-dependent approach for HBV treatment and suggest 2H5-A14 as a novel clinical candidate for HBV prevention and treatment of chronic HBV infection.

Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair.

  • Robu M
  • Proc. Natl. Acad. Sci. U.S.A.
  • 2017 Aug 15

Literature context:


Abstract:

Xeroderma pigmentosum C (XPC) protein initiates the global genomic subpathway of nucleotide excision repair (GG-NER) for removal of UV-induced direct photolesions from genomic DNA. The XPC has an inherent capacity to identify and stabilize at the DNA lesion sites, and this function is facilitated in the genomic context by UV-damaged DNA-binding protein 2 (DDB2), which is part of a multiprotein UV-DDB ubiquitin ligase complex. The nuclear enzyme poly(ADP-ribose) polymerase 1 (PARP1) has been shown to facilitate the lesion recognition step of GG-NER via its interaction with DDB2 at the lesion site. Here, we show that PARP1 plays an additional DDB2-independent direct role in recruitment and stabilization of XPC at the UV-induced DNA lesions to promote GG-NER. It forms a stable complex with XPC in the nucleoplasm under steady-state conditions before irradiation and rapidly escorts it to the damaged DNA after UV irradiation in a DDB2-independent manner. The catalytic activity of PARP1 is not required for the initial complex formation with XPC in the nucleoplasm but it enhances the recruitment of XPC to the DNA lesion site after irradiation. Using purified proteins, we also show that the PARP1-XPC complex facilitates the handover of XPC to the UV-lesion site in the presence of the UV-DDB ligase complex. Thus, the lesion search function of XPC in the genomic context is controlled by XPC itself, DDB2, and PARP1. Our results reveal a paradigm that the known interaction of many proteins with PARP1 under steady-state conditions could have functional significance for these proteins.

Funding information:
  • NIDCR NIH HHS - U01 DE024427(United States)

A Splice Variant of Centrosomin Converts Mitochondria to Microtubule-Organizing Centers.

  • Chen JV
  • Curr. Biol.
  • 2017 Jul 10

Literature context:


Abstract:

Non-centrosomal microtubule organizing centers (MTOCs) direct microtubule (MT) organization to exert diverse cell-type-specific functions. In Drosophila spermatids, the giant mitochondria provide structural platforms for MT reorganization to support elongation of the extremely long sperm. However, the molecular basis for this mitochondrial MTOC and other non-centrosomal MTOCs has not been discerned. Here we report that Drosophila centrosomin (cnn) expresses two major protein variants: the centrosomal form (CnnC) and a non-centrosomal form in testes (CnnT). CnnC is established as essential for functional centrosomes, the major MTOCs in animal cells. We show that CnnT is expressed exclusively in testes by alternative splicing and localizes to giant mitochondria in spermatids. In cell culture, CnnT targets to the mitochondrial surface, recruits the MT nucleator γ-tubulin ring complex (γ-TuRC), and is sufficient to convert mitochondria to MTOCs independent of core pericentriolar proteins that regulate MT assembly at centrosomes. We mapped two separate domains in CnnT: one that is necessary and sufficient to target it to mitochondria and another that is necessary and sufficient to recruit γ-TuRCs and nucleate MTs. In elongating spermatids, CnnT forms speckles on the giant mitochondria that are required to recruit γ-TuRCs to organize MTs and support spermiogenesis. This molecular characterization of the mitochondrial MTOC defines a minimal molecular requirement for MTOC generation and implicates the potent role of Cnn (or its related) proteins in the direct regulation of MT assembly and organization of non-centrosomal MTOCs.