The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Human Multidrug Resistance ABCB and ABCG Transporters: Participation in a Chemoimmunity Defense System
Abstract
In this review we give an overview of the physiological functions of a group of ATP binding cassette (ABC) transporter proteins, which were discovered, and still referred to, as multidrug resistance (MDR) transporters. Although they indeed play an important role in cancer drug resistance, their major physiological function is to provide general protection against hydrophobic xenobiotics. With a highly conserved structure, membrane topology, and mechanism of action, these essential transporters are preserved throughout all living systems, from bacteria to human. We describe the general structural and mechanistic features of the human MDR-ABC transporters and introduce some of the basic methods that can be applied for the analysis of their expression, function, regulation, and modulation. We treat in detail the biochemistry, cell biology, and physiology of the ABCB1 (MDR1/P-glycoprotein) and the ABCG2 (MXR/BCRP) proteins and describe emerging information related to additional ABCB- and ABCG-type transporters with a potential role in drug and xenobiotic resistance. Throughout this review we demonstrate and emphasize the general network characteristics of the MDR-ABC transporters, functioning at the cellular and physiological tissue barriers. In addition, we suggest that multidrug transporters are essential parts of an innate defense system, the “chemoimmunity” network, which has a number of features reminiscent of classical immunology.
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Cites
Targeting multidrug resistance in cancer
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Self-citationZhou, S., Schuetz, J. D., Bunting, K. D., Colapietro, A.-M., Sampath, J., Morris, J. J., Lagutina, I., Grosveld, G. C., Osawa, M., Nakauchi, H., et al. (2001) · Nature Medicine · doi:10.1038/nm0901-1028 · Cited by 2,280
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Deeley, R. G., Westlake, C., & Cole, S. P. C. (2006) · Physiological Reviews · doi:10.1152/physrev.00035.2005 · Cited by 761
Mutant p53 Cooperates with ETS and Selectively Up-regulates Human MDR1 Not MRP1
Sampath, J., Sun, D., Kidd, V. J., Grenet, J., Gandhi, A., Shapiro, L. H., Wang, Q., Zambetti, G. P., & Schuetz, J. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103429200 · Cited by 244
Organic anion transporter (Slc22a) family members as mediators of toxicity
Sweet, D. H. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.10.016 · Cited by 150
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Porter, C. J. H., Trevaskis, N. L., & Charman, W. N. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2197 · Cited by 1,824
Maschmeyer, I., Lorenz, A. K., Schimek, K., Hasenberg, T., Ramme, A. P., Hübner, J., Lindner, M., Drewell, C., Bauer, S., Thomas, A., et al. (2015) · Lab on a Chip · doi:10.1039/c5lc00392j · Cited by 861
Human kidney proximal tubule-on-a-chip for drug transport and nephrotoxicity assessment
Jang, K.-J., Mehr, A. P., Hamilton, G. A., McPartlin, L. A., Chung, S., Suh, K.-Y., & Ingber, D. E. (2013) · Integrative Biology · doi:10.1039/c3ib40049b · Cited by 849
Mechanistic diversity in ATP-binding cassette (ABC) transporters.
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Metadata
- Authors
- Sarkadi, B., Homolya, L., Szakács, G., & Váradi, A.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2006-10
- Volume
- 86
- Issue
- 4
- Pages
- 1179-1236
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2061270171
- Cited by
- 726
- References
- 6
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- closed
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