The DOI matches its Crossref record.
Cellular localization of the multidrug-resistance gene product P-glycoprotein in normal human tissues.
Open accessAbstract
Monoclonal antibody MRK16 was used to determine the location of P-glycoprotein, the product of the multidrug-resistance gene (MDR1), in normal human tissues. The protein was found to be concentrated in a small number of specific sites. Most tissues examined revealed very little P-glycoprotein. However, certain cell types in liver, pancreas, kidney, colon, and jejunum showed specific localization of P-glycoprotein. In liver, P-glycoprotein was found exclusively on the biliary canalicular front of hepatocytes and on the apical surface of epithelial cells in small biliary ductules. In pancreas, P-glycoprotein was found on the apical surface of the epithelial cells of small ductules but not larger pancreatic ducts. In kidney, P-glycoprotein was found concentrated on the apical surface of epithelial cells of the proximal tubules. Colon and jejunum both showed high levels of P-glycoprotein on the apical surfaces of superficial columnar epithelial cells. Adrenal gland showed high levels of P-glycoprotein diffusely distributed on the surface of cells in both the cortex and medulla. These results suggest that the protein has a role in the normal secretion of metabolites and certain anti-cancer drugs into bile, urine, and directly into the lumen of the gastrointestinal tract.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Molecular Basis of Bacterial Outer Membrane Permeability Revisited
Nikaido, H. (2003) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.67.4.593-656.2003 · Cited by 4,316
Targeting multidrug resistance in cancer
Szakács, G., Paterson, J. K., Ludwig, J. A., Booth-Genthe, C., & Gottesman, M. M. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1984 · Cited by 3,609
Self-citationOverexpression of a Transporter Gene in a Multidrug-Resistant Human Lung Cancer Cell Line
Cole, S. P. C., Bhardwaj, G., Gerlach, J. H., Mackie, J. E., Grant, C. E., Almquist, K. C., Stewart, A. J., Kurz, E. U., Duncan, A. M. V., & Deeley, R. G. (1992) · Science · doi:10.1126/science.1360704 · Cited by 3,037
Deeley, R. G., Westlake, C., & Cole, S. P. C. (2006) · Physiological Reviews · doi:10.1152/physrev.00035.2005 · Cited by 761
Transport of drugs from blood vessels to tumour tissue
Dewhirst, M. W., & Secomb, T. W. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.93 · Cited by 749
Structure, function and regulation of P-glycoprotein and its clinical relevance in drug disposition
Zhou, S.-F. (2008) · Xenobiotica · doi:10.1080/00498250701867889 · Cited by 599
Importance of P-glycoprotein at blood–tissue barriers
Fromm, M. F. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.06.002 · Cited by 592
The molecular basis of multidrug resistance in cancer: The early years of P‐glycoprotein research
Gottesman, M. M., & Ling, V. (2006) · FEBS Letters · doi:10.1016/j.febslet.2005.12.060 · Cited by 558
Self-citationThe neurobiology of depression and antidepressant action
Willner, P., Scheel-Krüger, J., & Belzung, C. (2013) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2012.12.007 · Cited by 519
ABC transporters as mediators of drug resistance and contributors to cancer cell biology
Fletcher, J. I., Williams, R. T., Henderson, M. J., Norris, M. D., & Haber, M. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2016.03.001 · Cited by 423
Ishimoto, H., & Jaffe, R. B. (2011) · Endocrine Reviews · doi:10.1210/er.2010-0001 · Cited by 379
(2001) · PubMed · Cited by 350
Modulation of P-glycoprotein efflux pump: induction and activation as a therapeutic strategy
Silva, R., Vilas-Boas, V., Carmo, H., Dinis-Oliveira, R. J., Carvalho, F., de Lourdes Bastos, M., & Remião, F. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.11.013 · Cited by 339
Rostami-Hodjegan, A. (2012) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2012.65 · Cited by 331
Yabuuchi, H., Tamai, I., Nezu, J.-I., Sakamoto, K., Oku, A., Shimane, M., Sai, Y., & Tsuji, A. (1999) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(24)38199-6 · Cited by 316
Intestinal permeability and its relevance for absorption and elimination
Lennernäs, H. (2007) · Xenobiotica · doi:10.1080/00498250701704819 · Cited by 304
Marchetti, S., Mazzanti, R., Beijnen, J. H., & Schellens, J. H. M. (2007) · The Oncologist · doi:10.1634/theoncologist.12-8-927 · Cited by 284
Furuno, T., Landi, M.-T., Ceroni, M., Caporaso, N., Bernucci, I., Nappi, G., Martignoni, E., Schaeffeler, E., Eichelbaum, M., Schwab, M., et al. (2002) · Pharmacogenetics · doi:10.1097/00008571-200210000-00004 · Cited by 178
Role of the hypothalamic–pituitary–adrenal axis in developmental programming of health and disease
Xiong, F., & Zhang, L. (2013) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2012.11.002 · Cited by 177
Apical/Basolateral Surface Expression of Drug Transporters and its Role in Vectorial Drug Transport
Ito, K., Suzuki, H., Horie, T., & Sugiyama, Y. (2005) · Pharmaceutical Research · doi:10.1007/s11095-005-6810-2 · Cited by 174
Role of cellular uptake in the reversal of multidrug resistance by PEG-b-PLA polymeric micelles
Xiao, L., Xiong, X., Sun, X., Zhu, Y., Yang, H., Chen, H., Gan, L., Xu, H., & Yang, X. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.03.071 · Cited by 169
Genovese, I., Ilari, A., Assaraf, Y. G., Fazi, F., & Colotti, G. (2017) · Drug Resistance Updates · doi:10.1016/j.drup.2017.10.003 · Cited by 156
Zhou, S., Zong, Y., Ney, P. A., Nair, G., Stewart, C. F., & Sorrentino, B. P. (2005) · Blood · doi:10.1182/blood-2004-04-1566 · Cited by 157
Dysfunction of ABC transporters at the blood-brain barrier: Role in neurological disorders
Gil-Martins, E., Barbosa, D. J., Silva, V., Remião, F., & Silva, R. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107554 · Cited by 152
P-glycoprotein-mediated transport of berberine across Caco-2 cell monolayers
Maeng, H.-J., Yoo, H.-J., Kim, I.-W., Song, I.-S., Chung, S.-J., & Shim, C.-K. (2002) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.10268 · Cited by 128
Gut bitter taste receptor signalling induces ABCB1 through a mechanism involving CCK
Jeon, T.-I., Seo, Y.-K., & Osborne, T. F. (2011) · Biochemical Journal · doi:10.1042/bj20110009 · Cited by 127
Boyer, J. L. (2013) · Comprehensive Physiology · doi:10.1002/j.2040-4603.2013.tb00519.x · Cited by 124
Relationship Between P-Glycoprotein and Second-Generation Antipsychotics
Moons, T., de Roo, M., Claes, S., & Dom, G. (2011) · Pharmacogenomics · doi:10.2217/pgs.11.55 · Cited by 122
Pharmacogenetics of antidepressants
Crisafulli, C., Fabbri, C., Porcelli, S., Drago, A., Spina, E., De Ronchi, D., & Serretti, A. (2011) · Frontiers in Pharmacology · doi:10.3389/fphar.2011.00006 · Cited by 113
Symposium Article: Molecular and Physical Mechanisms of First-Pass Extraction
Hall, S. D., Thummel, K. E., Watkins, P. B., Lown, K. S., Benet, L. Z., Paine, M. F., Mayo, R. R., Turgeon, D. K., Bailey, D. G., Fontana, R. J., et al. (1999) · Drug Metabolism and Disposition · doi:10.1016/s0090-9556(24)15271-3 · Cited by 109
Fowler, S., Chen, W. L. K., Duignan, D. B., Gupta, A., Hariparsad, N., Kenny, J. R., Lai, W. G., Liras, J., Phillips, J. A., & Gan, J. (2020) · Lab on a Chip · doi:10.1039/c9lc00857h · Cited by 109
Husain, I., Bala, K., Khan, I. A., & Khan, S. I. (2021) · Food Frontiers · doi:10.1002/fft2.110 · Cited by 104
Notch2-positive progenitors with the intrinsic ability to give rise to pancreatic ductal cells
Lee, K. M., Yasuda, H., Hollingsworth, M. A., & Ouellette, M. M. (2005) · Laboratory Investigation · doi:10.1038/labinvest.3700298 · Cited by 88
RLIP76, a Novel Transporter Catalyzing ATP-Dependent Efflux of Xenobiotics
Awasthi, S., Sharma, R., Singhal, S. S., Zimniak, P., & Awasthi, Y. C. (2002) · Drug Metabolism and Disposition · doi:10.1124/dmd.30.12.1300 · Cited by 86
Bexarotene: A promising anticancer agent
Qu, L., & Tang, X. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-1140-4 · Cited by 78
Ibrahim, Y. F., Moussa, R. A., Bayoumi, A. M. A., & Ahmed, A.-S. F. (2020) · Inflammopharmacology · doi:10.1007/s10787-019-00628-y · Cited by 75
Hindle, S. J., Munji, R. N., Dolghih, E., Gaskins, G., Orng, S., Ishimoto, H., Soung, A., DeSalvo, M., Kitamoto, T., Keiser, M. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.026 · Cited by 74
Tabibian, J. H., Masyuk, A. I., Masyuk, T. V., O'Hara, S. P., & LaRusso, N. F. (2013) · Comprehensive Physiology · doi:10.1002/j.2040-4603.2013.tb00495.x · Cited by 52
Yanagishita, M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50119-3 · Cited by 51
Song, Q.-Q., Xie, W.-Y., Tang, Y.-J., Zhang, J., & Liu, J. (2017) · Pharmacogenomics · doi:10.2217/pgs-2016-0151 · Cited by 40
Pérez-Ramírez, C., Cañadas-Garre, M., Alnatsha, A., Villar, E., Delgado, J. R., Faus-Dáder, M. J., & Calleja-Hernández, M. Ÿ. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.08.002 · Cited by 33
Progress in the Molecular Characterization of Hepatobiliary Transporters
Keppler, D. (2017) · Digestive Diseases · doi:10.1159/000450911 · Cited by 33
Structural insights into binding-site access and ligand recognition by human ABCB1
Kurre, D., Dang, P. X., Le, L. T. M., Gadkari, V. V., & Alam, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00361-z · Cited by 25
Wang, Y., Tu, M.-J., & Yu, A.-M. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1423416 · Cited by 21
Heikkinen, A. T., Fowler, S., Gray, L., Li, J., Peng, Y., Yadava, P., Railkar, A., & Parrott, N. (2013) · Molecular Pharmaceutics · doi:10.1021/mp300692k · Cited by 20
Metadata
- Authors
- Thiebaut, F., Tsuruo, T., Hamada, H., Gottesman, M. M., Pastan, I., & Willingham, M. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-11
- Volume
- 84
- Issue
- 21
- Pages
- 7735-7738
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1964470226
- Cited by
- 2,777
- References
- 0
- FWCI
- 16.60
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.