ABCC10 Membrane Protein Introduction

Introduction of ABCC10

ABCC10, also known as MRP1, is a member of the superfamily of ATP-binding cassette (ABC) transporters which transport various molecules across extra- and intracellular membranes. There are seven subfamilies in ABC superfamily named as ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White, respectively. ABCC10 protein belongs to MRP subfamily. It has 1492 amino acids with three membrane-spanning domains that contain 17 transmembrane helixes, and two nucleotide binding domains.

Basic Information of ABCC10
Protein Name	Multidrug resistance-associated protein 7
Gene Name	ABCC10
Aliases	MRP7, SIMRP7, EST182763
Organism	Homo sapiens (Human)
UniProt ID	Q5T3U5
Transmembrane Times	17
Length (aa)	1492
Sequence	MERLLAQLCGSSAAWPLPLWEGDTTGHCFTQLVLSALPHALLAVLSACYLGTPRSPDYILPCSPGWRLRLAASFLLSVFPLLDLLPVALPPGAGPGPIGLEVLAGCVAAVAWISHSLALWVLAHSPHGHSRGPLALALVALLPAPALVLTVLWHCQRGTLLPPLLPGPMARLCLLILQLAALLAYALGWAAPGGPREPWAQEPLLPEDQEPEVAEDGESWLSRFSYAWLAPLLARGACGELRQPQDICRLPHRLQPTYLARVFQAHWQEGARLWRALYGAFGRCYLALGLLKLVGTMLGFSGPLLLSLLVGFLEEGQEPLSHGLLYALGLAGGAVLGAVLQNQYGYEVYKVTLQARGAVLNILYCKALQLGPSRPPTGEALNLLGTDSERLLNFAGSFHEAWGLPLQLAITLYLLYQQVGVAFVGGLILALLLVPVNKVIATRIMASNQEMLQHKDARVKLVTELLSGIRVIKFCGWEQALGARVEACRARELGRLRVIKYLDAACVYLWAALPVVISIVIFITYVLMGHQLTATKVFTALALVRMLILPLNNFPWVINGLLEAKVSLDRIQLFLDLPNHNPQAYYSPDPPAEPSTVLELHGALFSWDPVGTSLETFISHLEVKKGMLVGIVGKVGCGKSSLLAAIAGELHRLRGHVAVRGLSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGRLLQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMGLFSPQLLLFSPGNLYIPVFPLPKAAPNGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQPHSLFQQLLQSSQQGVPASLGGP

Function of ABCC10 Membrane Protein

ABCC10 has been shown the capacity to transport lipophilic anions and its substrates selectivity is relatively limited including glucuronate conjugates 17β-estradiol-(17-β-d-glucuronide) and glutathione S-conjugates (leukotriene C4). In view of the characteristics of its substrates, ABCC10 plays a very important role in cellular detoxification and multi-drug resistance, including nucleoside-based agents and a range of natural product anticancer agents such as docetaxel, paclitaxel, daunorubicin, etoposide and epothilone B. Unlike other MRPs, MRP7 is an essential factor for regulating taxanes resistance. MRP7-transfected HEK293 cells have the highest levels of resistance against docetaxel (9-13-fold), and lower levels of resistance toward paclitaxel (3-fold), vincristine (3-fold), and vinblastine (3-4-fold). A recent study has been also revealed that the ABCC10 expression is significantly associated with overall survival of colorectal cancer patients and provided a possible prognostic marker in colorectal cancer. Now the physiological functions of MRP7 are not exactly clear, but it has been indicated that MRP7 may play a potential role in suppression of natural killer (NK)-mediated lysis.

ABCC10 Membrane Protein Introduction Fig.1 The topography and localization of ABCB1, ABCG2, short-(ABCC4, ABCC5, ABCC11) and long-(ABCC1, ABCC2, ABCC3, ABCC6, ABCC10) forms of ABCCs. (Wang, 2014)

Application of ABCC10 Membrane Protein in Literature

Fang L., et al. Systematic analysis reveals a lncRNA-mRNA co-expression network associated with platinum resistance in high-grade serous ovarian cancer. Investigational New Drugs. 2018, 36(2): 187-194. PubMed ID: 29082457

The study shows that lncRNA RP5-1120P11.1 and ABCC10 are both down-regulated in platinum-resistant high-grade serous ovarian cancer (HGS-OvCa) patients. This suggests lncRNA is involved in drug resistance.
Dabrowska M and Sirotnak F.M. E2F site in the essential promoter region does not confer Sphase-specific transcription of the ABCC10 gene in human prostate cancer cells. Acta Biochimica Polonica. 2017, 64(2): 371-374. PubMed ID: 28612064

The study indicates that the ABCC10 expression in human prostate cancer cells is primarily associated with cell proliferation, not be specific to S phase.
Zhang H., et al. The BTK inhibitor, ibrutinib (PCI-32765) overcomes paclitaxel resistance in ABCB1 and ABCC10 overexpressing cells and tumors. Molecular Cancer Therapeutics. 2017, 16(6): 1021-1030. PubMed ID: 28265007

The study shows that the combination of paclitaxel and ibrutinib can effectively inhibit the paclitaxel resistance mediated by ABCB1 and ABCC10.
Salvaggio S.E., et al. Clinical and genetic factors associated with kidney tubular dysfunction in a real-life single centre cohort of HIV-positive patients. Bmc Infectious Diseases. 2017, 17(1): 396. PubMed ID: 28583112

The study shows that ABCC4 rs1751034 may be associated with kidney tubular dysfunction (KTD). But the further studies need to prove the value of genetic factors in the KTD personalization therapy.
Hegyi M., et al. Pharmacogenetic analysis of high-dose methotrexate treatment in children with osteosarcoma. Oncotarget. 2017, 8(6): 9388-9398. PubMed ID: 27566582

The authors analyze the correlations between polymorphisms in transporters genes (ABCB1, ABCC1, ABCC2, ABCC3, ABCC10, ABCG2, GGH, SLC19A1 and NR1I2 genes) and pharmacokinetic parameters and the occurrence of hepato- and myelotoxicity.

ABCC10 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-ABCC10 antibody development services.

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Reference

Wang Y J, et al. (2014). Repositioning of tyrosine kinase inhibitors as antagonists of ATP-binding cassette transporters in anticancer drug resistance. Cancers. 6(4):1925-52.

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