ArticleInternational journal of molecular sciences2022
Transport Turnover Rates for Human OCT2 and MATE1 Expressed in Chinese Hamster Ovary Cells.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- CryoEM and computational modeling structural insights into the pH regulator NBCn1.Nature communications · 2025Article
- Determination of metal ion transport rate of human ZIP4 using stable zinc isotopes.The Journal of biological chemistry · 2024Article
- Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.Nature communications · 2024Article
- Exploring Amino Acid Transporters as Therapeutic Targets for Cancer: An Examination of Inhibitor Structures, Selectivity Issues, and Discovery Approaches.Pharmaceutics · 2024Review
- Applying new approach methodologies to assess next-generation tobacco and nicotine products.Frontiers in toxicology · 2024Review
- On the substrate turnover rate of NBCe1 and AE1 SLC4 transporters: structure-function considerations.Frontiers in physiology · 2024Article
- Anion Pathways in the NarK Nitrate/Nitrite Exchanger.Journal of chemical information and modeling · 2023Article
- Novel method for kinetic analysis applied to transport by the uniporter OCT2.American journal of physiology. Renal physiology · 2022Article
- Physiology, Biochemistry and Pharmacology of Transporters for Organic Cations 2.0.International journal of molecular sciences · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
MATE1 (multidrug and toxin extruder 1) and OCT2 (organic cation transporter 2) play critical roles in organic cation excretion by the human kidney. The transporter turnover rate (TOR) is relevant to understanding both their transport mechanisms and interpreting the in vitro-in vivo extrapolation (IVIVE) required for physiologically-based pharmacokinetic (PBPK) modeling. Here, we use a quantitative western blot method to determine TORs for MATE1 and OCT2 proteins expressed in CHO cells. MATE1 and OCT2, each with a C-terminal V-5 epitope tag, were cell surface biotinylated and the amount of cell surface MATE1 and OCT2 protein was quantified by western analysis, using standard curves for the V5 epitope. Cell surface MATE1 and OCT2 protein represented 25% and 24%, respectively, of the total expression of these proteins in CHO cells. The number of cell surface transporters was ~55 fmol cm
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.