ABCC10
- Known as:
- ABCC10
- Catalog number:
- 000917A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ABCC10
Related genes to: ABCC10
- Gene:
- ABCC10 NIH gene
- Name:
- ATP binding cassette subfamily C member 10
- Previous symbol:
- -
- Synonyms:
- EST182763, MRP7, SIMRP7
- Chromosome:
- 6p21.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-10-26
- Date modifiied:
- 2018-05-03
Related products to: ABCC10
Related articles to: ABCC10
- Bixlozone has significant potential as a pre-emergence and early post-emergence herbicide in wheat production across China. However, its safety when applied to wheat is poor, frequently causing phytotoxicity. This study confirmed the capacity of pyroxsulam to mitigate bixlozone-induced injury without compromising weed control efficacy and examined the underlying processes. Wheat exposed to bixlozone alone developed pronounced chlorosis and significant reductions in tiller formation, ultimately lowering the grain yield. In contrast, co-treatment with pyroxsulam substantially relieved chlorosis and restored both the tiller number and yield performance. Bixlozone reduced chlorophyll and carotenoid levels, impairing the function of photosystem II (PSII), which was mitigated by pyroxsulam application. Transcriptome profiling showed that pyroxsulam strongly activated detoxification-related pathways, especially those associated with glutathione S-transferases (GSTs) and ATP-binding cassette (ABC) transporters, which facilitate the metabolic detoxification or compartmentalization of bixlozone. qRT-PCR further validated the marked induction of key detoxification genes , and following pyroxsulam addition. Collectively, this study provides initial mechanistic insight into how pyroxsulam, though itself a herbicide, can enhance wheat tolerance to bixlozone by stimulating endogenous detoxification systems. These findings offer a framework for the development of safer herbicide mixtures and expand current understanding of crop-herbicide interactions, providing meaningful implications for herbicide management and sustainable agricultural systems. - Source: PubMed
Publication date: 2026/02/22
Geng YalingDong XuWang ChencanLiu ChunhongWei HongliangWang LinghuiXu JingChen DongYuan Libing - Multidrug resistance of cancer cells is attributed to drug-induced alteration of numerous intracellular processes. Using clinically relevant models of triple-negative breast and non-small lung cancer cells we previously showed that these cells respond to repeated paclitaxel exposure by inter alia lysosome enrichment in ABCC3, ABCC5, and ABCC10, which contribute to drug sequestration in these organelles and reduced drug cytotoxicity. In this study, we provide experimental evidence that transcription of the above-mentioned ABCC genes is enabled by BRG1-based SWI/SNF chromatin remodeling complex. Pharmacological inhibition of SWI/SNF with PFI3 or ACBI1, the PROTAC degrader of SMARCA2/4, substantially reduced transcription of ABCC3, ABCC5, and ABCC10. A similar effect was caused by transient silencing of SMARCA4 (BRG1), but not SMARCA2 (BRM). The deficiency of BRG1 led to extralysosomal distribution of anticancer drugs, their deeper penetration of spheroids, and substantial increase in drug cytotoxicity. Interestingly, in BRG1-deficient cell line paclitaxel triggered mutations, which reverted BRG1 truncating deletion in SMARCA4, thereby restoring SWI/SNF ATPase expression in paclitaxel-resistant cells and increasing transcription of ABCC. Acquisition of drug resistance was associated with BRG1 redistribution in the genome, de novo occurrence at the promoters of genes functionally linked to endolysosomal system, and stronger co-occurrence with EP300. Our study indicates possible target--SWI/SNF complex for anticancer combinatorial interventions in paclitaxel-induced multidrug resistant phenotypes. SIGNIFICANCE STATEMENT: This study provides evidence that BRG1 inhibition with PFI3 and degradation of SMARCA4 mRNA substantially declines lysosomal drug sequestration and potentiate drug toxicity. Therefore, BRG1 targeting can be considered as candidate for combinatorial anticancer therapy with some standard chemotherapy drugs. - Source: PubMed
Publication date: 2025/11/10
Gronkowska KarolinaMichlewska SylwiaPłoszaj TomaszStrachowska MagdalenaStępień AdriannaBorowiec MaciejBednarek AndrzejRobaszkiewicz Agnieszka - This study investigated the association between ATP-binding cassette (ABC) transporter gene polymorphisms and Epidermal Growth Factor Receptor (EGFR)- Tyrosine kinase inhibitor (TKI) sensitivity in non-small cell lung cancer (NSCLC). Our goal was to determine if these genetic variations could serve as valuable biomarkers for predicting treatment efficacy. We examined the associations between ABC transporter mRNA expression and EGFR-TKI sensitivity in 16 NSCLC cell lines. Expression of ABCB1, ABCG2, ABCC10, and ABCC11 was quantified by real-time PCR and correlated with IC values of gefitinib and osimertinib. Additionally, associations between transporter gene single nucleotide polymorphisms (SNPs) (ABCB1 C1236T, ABCB1 C3435T, ABCG2 C421A, ABCC10 T2843C, ABCC11 G538A) and EGFR-TKI sensitivity were evaluated. To assess clinical relevance, blood samples from 109 gefitinib/erlotinib- and 54 osimertinib-treated patients were analyzed for these SNPs. While no significant correlation was found between mRNA expression and IC values in cell lines, we did find that specific SNPs significantly correlated with drug cytotoxicity in vitro. Clinically, the ABCB1 C1236T T/T genotype was associated with prolonged PFS in patients on first-generation EGFR-TKIs, while the ABCC10 T2843C T/T genotype was linked to longer PFS with third-generation EGFR-TKIs. These findings suggest that ABC transporter SNPs could be valuable biomarkers for personalized medicine in NSCLC. These findings suggest that ABC transporter SNPs may serve as valuable biomarkers for predicting EGFR-TKI efficacy in NSCLC patients with EGFR mutations, which will contribute to personalized medicine. - Source: PubMed
Publication date: 2025/12/04
Toda-Shiraga SanaeUemura TakehiroKakihara AkihitoHashiba FumitakaTanaka TatsuyaIto ToshiyasuOnuki TomohiroIto KeimaMori YutaFukumitsu KensukeFukuda SatoshiKanemitsu YoshihiroTajiri TomokoOhkubo HirotsuguMaeno KenNiimi AkioOguri Tetsuya - The development of resistance to paclitaxel (PTX), which is a vital anticancer drug treating breast and lung cancers, can cause treatment failure and limit further use of taxanes and similar drugs. As previously documented, PTX-induced irresponsiveness to chemotherapy involves the overexpression of ABCC3, ABCC5, and ABCC10 members of the ATP-binding cassette (ABC) transmembrane proteins, which are enriched in the lysosomes of drug-resistant cells where anticancer drugs are actively trapped. In this paper, the role of HIF1A in a BRG1-p300-dependent overexpression of 3 genes in drug resistant cells was examined. Although motive spacing analysis of BRG1 enriched regions indicated that HIF1A, ISL1, MAF, and ZNF76 could be possible BRG1 co-regulators, co-operation with BRG1 and the contribution to drug resistance was only confirmed for HIF1A. HIF1A deficiency abolished the transcription promoting effect of BRG1 and p300, thereby suggesting that this protein acts as the master regulator of ABCC transcription. Analysis of The Cancer Genome Atlas (TCGA) and The Genotype-Tissue Expression (GTEx) databases confirmed a likely role of HIF1A-BRG1-p300 overexpression in the taxanes resistance of cancer patients and the possible biomarker function of this protein in cancer responses to chemotherapy. Therefore, the complex comprising BRG1-EP300-HIF1A can be considered for further clinical investigation and planning for patient therapy. - Source: PubMed
Publication date: 2025/09/08
Gronkowska KarolinaKołacz-Milewska KingaMichlewska SylwiaPłoszaj TomaszBorowiec MaciejRobaszkiewicz Agnieszka - Mucopolysaccharidosis type I (MPS I) is a rare lysosomal storage disorder resulting from a deficiency in the lysosomal enzyme alpha-L-iduronidase, which degrades heparan sulfate and dermatan sulfate glycosaminoglycans (GAG) within endosome-lysosome compartments. MPS I patients demonstrate respiratory dysfunction with varying symptoms and severity during disease progression, which has been associated primarily with upper airway involvement and the thoracic cavity. However, the involvement of respiratory complications in patient morbidity and mortality suggests that we know relatively little about the pathogenic process in the lung. Using a proteomics approach, we analyzed lung tissues from a murine model of MPS I to identify proteins and molecular pathways contributing to respiratory pathology. A total of 7604 proteins were identified, of which 144 were significantly upregulated, 93 downregulated, and three proteins (GPNMB, SLC39A1, ABCC10) were uniquely detected in MPS I lung tissue compared to control lung tissue. Gene ontology analysis confirmed significant disruptions to lysosomal biogenesis, GAG degradation pathways, and extracellular matrix remodelling. Immunohistochemistry showed elevated LAMP I expression, which was consistent with the proteomic results and endosome-lysosome dysfunction being a key driver of disease pathogenesis in the MPS I lung. Our findings reveal novel proteomic alterations underlying distal lung pathology in MPS I and identify potential biomarkers that may have clinical utility for monitoring disease progression. - Source: PubMed
Publication date: 2025/09/07
Ngai Yuen TYoung CliffordParkinson-Lawrence Emma JWimmer-Kleikamp SabineMittal ParulBeard HelenBriggs Matthew TKlingler-Hoffmann ManuelaBrooks Doug AOrgeig SandraHoffmann Peter