2. БЕЛКИ-ТРАНСПОРТЕРЫ ОРГАНИЧЕСКИХ АНИОНОВ СЕМЕЙСТВА SLC21/SLCO.

Лев Павлович Смирнов, Ирина Викторовна Суховская, Екатерина Витальевна Борвинская, Lev Smirnov, Irina Sukhovskaya, Ekaterina Borvinskaya

Аннотация


Белки суперсемейства SLC21/SLCO (по классификации HUGO Gene Nomenclature Commitee) представляют собой транспортеры органических анионов. OATР (organic anion transporting peptides) входят в состав Na-независимой транспортной системы и при физиологических значениях рН осуществляют перенос через плазматические мембраны различных органов и тканей эукариотических организмов большого числа как эндогенных (желчные кислоты, эйкозаноиды, стероидные и тиреоидные гормоны, и др.), так и экзогенных (анионные олигопептиды, органические красители, различные токсины, лекарственные препараты и др.) амфифильных органических анионов с молекулярными массами больше 350 Da. Эти транспортеры являются неотъемлемой частью системы биотрансформации ксенобиотиков и играют важную роль в ее функционировании через тесную взаимосвязь с ферментами фаз I и II, которая может осуществляться через изменение метаболических путей за счет одновременной альтерации активности ферментов и транспортеров. Препараты, мишенями которых являются ферменты фаз I и II, зачастую могут быть субстратами или ингибиторами транспортеров. В настоящее время расшифровано полностью или частично строение около 300 полипептидов из почти 40 видов животных. На основании сходства по аминокислотной последовательности белки разделяются на семейства (до 40% идентичности) и подсемейства (до 60 % сходства). Филогения ОАТР4В1 указывает на очень близкие эволюционные дистанции по этому белку между млекопитающими и другими видами. Транспортеры подсемейства ОАТР1С считаются эволюционно наиболее древними, поскольку обнаружены у всех исследованных видов. У растений, дрожжей и бактерий гомологи OATP не найдены.

 


Ключевые слова


транспортеры органических анионов; биотрансформация ксенобиотиков

Полный текст:

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Литература


Смирнов Л. П., Суховская И. В., Борвинская Е. В.

Транспортеры органических анионов (ОАТ). Молекулярное разнообразие, структура, функция, участие в функционировании системы биотрансформации ксенобиотиков у животных // Труды КарНЦ РАН. 2017. № 12. С. 28–42. doi: 10.17076/eb622

Ballatori N., Hammond C. L., Cunningham J. B., Krance S. M., Marchan R. Molecular mechanisms of reduced glutathione transport: role of theMRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins // Toxicology and Applied Pharmacology. 2005. Vol. 204. P. 238–255. doi:10.1016/j.taap.2004.09.008.

Cai S. Y., Wang W., Soroka C. J. Ballatori N., Boyer J. L. An evolutionary ancient Oatp: insights into conserved functional domains of these proteins // Am J Physiol: Gastrointest Liver Physiol. 2002. Vol. 282. P. G702 – G710. doi: 10.1152/ajpgi.00458.2001.

Chang A. B., Lin R., Studley W. K., Tran C. V., Saier M. H., Jr. Phylogeny as a guide to structure and function of membrane transport proteins (Review) // Mol. Membr. Biol. 2004. Vol. 21. P. 171-181. doi:10.1080/09687680410001720830.

Evers R., Chu X.Y. Role of the murine organic anion-transporting polypeptide 1b2 (Oatp1b2) in drug disposition and hepatotoxicity // Mol. Pharmacol. 2008. Vol. 74. P. 309–311.

Fenner K.S., Jones H.M., Ullah M., Kempshall S., Dickins M., Lai Y., et al. The evolution of the OATPhepatic uptake transport protein family in DMPK sciences: from obscure liver transporters to key determinants of hepatobiliary clearance // Xenobiotica. 2012. Vol. 42,#1. P. 28–45. doi: 10.3109/00498254.2011.626464.

Fischer A., Hoeger S.J., Stemmer K., Feurstein D.J., Knobeloch D., Nussler A., Dietrich D.R. The role of organic anion transporting polypeptides (OATPs/SLCOs) in the toxicity of different microcystin congeners in vitro: A comparison of primary human hepatocytes and OATP-transfected HEK293 cells// Toxicology and Applied Pharmacology. 2010. Vol. 245 P. 9–20. doi: 10.1016/j.taap.2010.02.006.

Froschauer A., Braasch I., Volff J. Fish genomes, comparativegenomics and vertebrate evolution //Curr. Genomics.2006. Vol. 7. P. 43–57.

Glaeser H., Mandery K., Sticht H., Fromm M.F., Konig J. Relevance of conserved lysine and arginine residues in transmembrane helices for the transport activity of organic anion transporting polypeptide 1B3 //Br J Pharmacol. 2010. Vol. 159, #3. P. 698–708. doi: 10.1111/j.1476-5381.2009.00568.x.

Gui C., Hagenbuch B. Molecular determinants for substrate selectivity of OATP-1B3 // FASEB J. 2008. Vol. 151. P. 393–399.

Gui C., Hagenbuch B. Cloning/characterization of the canine organic anion transporting polypeptide 1b4 (Oatp1b4) and classification of the canine OATP/SLCO members // Comp Biochem Physiol C Toxicol Pharmacol. 2010. Vol. 151. P. 393–399. doi: 10.1016/j.cbpc.2010.01.005.

Hagenbuch B., Meier P.J. The superfamily of organic anion transporting polypeptides // Biochimica et Biophysica Acta. 2003. Vol. 1609. P. 1–18.

Hagenbuch B., Meier P. J. Organic anion transporting polypeptides of the OATP/SLC21 family: phylogenic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties // Pflugers Arch. 2004. Vol. 447. P. 653-665.

Hagenbuch B., Gui C. Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family // Xenobiotica. 2008. Vol. 38. P. 778–801. doi: 10.1080/00498250801986951.

Hagenbuch B., Stieger B. The SLCO (former SLC21) superfamily of transporters // Molecular Aspects of Medicine. 2013. Vol. 34. P. 396–412. doi: 10.1016/j.mam.2012.10.009.

Hӓnggi E., Grundschober A.F., Leuthold S., Meier P.J., St-Pierre M.V. Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1 // Molecular Pharmacology. 2006. Vol.70. P. 806–817. doi:10.1124/mol.105.019547.

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Hung AY, Sheng M. PDZ domains: Structural modules for protein complex assembly // J Biol Chem. 2002. Vol. 277 P. 5699–5702.

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Kim E., Sheng M. PDZ domain proteins of synapses // Nat Rev Neurosci. 2004. Vol. 5. P. 771–781. doi:10.1038/nrn1517.

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Kusuhara H, Sugiyama Y. In vitro-in vivo extrapolation of transporter-mediated clearance in the liver and kidney //Drug Metab Pharmacokinet. 2009. Vol. 24, #1. P. 37–52.

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Li L., Lee T. K., MeierP. J., Ballatori N. Identification of glutathione as a driving force and leukotriene C4 as a substrate for oatp1, the hepatic sinusoidal organic solute transporter // J. Biol. Chem. 1998. Vol. 273, No. 26. P. 16184–16191.

Li L., Meier P. J., Ballatori N. Oatp2 mediates bidirectional organic solute transport: a role for intracellular glutathione // Molecular Pharmacology. 2000. Vol. 58 P. 335–340.

Mandery K., Sticht H., Bujok K., Schmidt I., Fahrmayr C., Balk B., Fromm M.F., Glaeser H. Functional and structural relevance of conserved positively charged lysine residues in organic anion transporting polypeptide 1B3 // Mol Pharmacol. 2011. Vol. 80, #3. P. 400–406. doi: 10.1124/mol.111.071282.

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Meier-Abt F., Mokrab Y., Mizuguchi K. Organic anion transporting polypeptides of the OATP/SLCO superfamily: identification of new members in nonmammalian species, comparative modeling anda potential transport mode // J Membr Biol. 2005.Vol. 208. P. 213–227. doi:10.1007/s00232-005-7004-x.

Meier-Abt F., Hammann-Hänni A., Stieger B., Ballatori N., Boyer J.L. The organic anion transport polypeptide 1d1 (Oatp1d1) mediates hepatocellular uptake of phalloidin and microcystin into skate liver// Toxicology and Applied Pharmacology. 2007. Vol. 218. P. 274–279. doi:10.1016/j.taap.2006.11.015.

Niemi M., Backman J.T., Neuvonen M., Neuvonen P.J. Effects of gemfibrozil, itraconazole, and their combination on the pharmacokinetics and pharmacodynamics of repaglinide: Potentially hazardous interaction between gemfibrozil and repaglinide // Diabetologia. 2003. Vol. 46. P. 347–351. doi:10.1007/s00125-003-1034-7.

Pizzagalli F., Hagenbuch B., Stieger B., Klenk U., Folkers G., Meier P.J. Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter // Mol. Endocrinol. 2002. Vol. 16. P. 2283–2296. doi:10.1210/me.2001-0309.

Popovic M., Zaja R., Smital T. Organic anion transporting polypeptides (OATP) in zebrafish (Danio rerio): Phylogenetic analysis and tissue distribution // Comparative Biochemistry and Physiology, Part A. 2010. Vol. 155. P. 327–335. doi: 10.1016/j.cbpa.2009.11.011.

Popovic M., Zaja R., Fent K., Smital T. Molecular Characterization of Zebrafish Oatp1d1 (Slco1d1), a Novel Organic Anion-transporting Polypeptide// J. Biol. Chem. 2013. Vol. 288. P. 33894–33911. doi: 10.1074/jbc.M113.518506.

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References in English

Smirnov L. P., Sukhovskaya I. V., Borvinskaya E. V.

Transportery organicheskikh anionov (OAT). Molekulyarnoe

raznoobrazie, struktura, funktsiya, uchastie v funktsionirovanii sistemy biotransformatsii ksenobiotikov u zhivotnykh [1. Organic anion transporters. Molecular diversity, structure, contribution to the functioning of the xenobiotic biotransformation system in animals (a rewiew)]. Trudy KarNTs RAN [Trans. of KarRC of RAS]. 2017. No. 12. P. 28–42. doi: 10.17076/eb622

Ballatori N., Hammond C. L., Cunningham J. B., Krance S. M., Marchan R. Molecular mechanisms of reduced glutathione transport: role of the MRP/CFTR/ABCC and OATP/SLC21A families of membrane proteins //Toxicology and Applied Pharmacology. 2005. Vol. 204. P. 238–255. doi:10.1016/j.taap.2004.09.008.

Cai S. Y., Wang W., Soroka C. J. Ballatori N., Boyer J. L. An evolutionary ancient Oatp: insights into conserved functional domains of these proteins // Am J Physiol: Gastrointest Liver Physiol. 2002. Vol. 282. P. G702 – G710. doi: 10.1152/ajpgi.00458.2001.

Chang A. B., Lin R., Studley W. K., Tran C. V., Saier M. H., Jr. Phylogeny as a guide to structure and function of membrane transport proteins (Review) // Mol. Membr. Biol. 2004. Vol. 21 P. 171-181. doi:10.1080/09687680410001720830.

Evers R., Chu X.Y. Role of the murine organic anion-transporting polypeptide 1b2 (Oatp1b2) in drug disposition and hepatotoxicity // Mol. Pharmacol. 2008. Vol. 74. P. 309–311.

Fenner K.S., Jones H.M., Ullah M., Kempshall S., Dickins M., Lai Y., et al. The evolution of the OATPhepatic uptake transport protein family in DMPK sciences: from obscure liver transporters to key determinants of hepatobiliary clearance // Xenobiotica. 2012. Vol. 42, #1. P. 28–45. doi: 10.3109/00498254.2011.626464.

Fischer A., Hoeger S.J., Stemmer K., Feurstein D.J., Knobeloch D., Nussler A., Dietrich D.R. The role of organic anion transporting polypeptides (OATPs/SLCOs) in the toxicity ofdifferent microcystin congeners in vitro: A comparison of primary humanhepatocytes and OATP-transfected HEK293 cells // Toxicology and Applied Pharmacology. 2010. Vol. 245 P. 9–20. doi: 10.1016/j.taap.2010.02.006.

Froschauer A., Braasch I., Volff J. Fish genomes, comparative genomics and vertebrate evolution //Curr. Genomics. 2006. Vol. 7. P. 43–57.

Glaeser H., Mandery K., Sticht H., Fromm M.F., Konig J. Relevance of conserved lysine and arginine residues in transmembrane helices for the transport activity of organic anion transporting polypeptide 1B3 // Br J Pharmacol. 2010. Vol.159, # 3. P. 698–708. doi: 10.1111/j.1476-5381.2009.00568.x.

Gui C., Hagenbuch B. Molecular determinants for substrate selectivity of OATP-1B3 // FASEB J. 2008. Vol. 151. P. 393–399.

Gui C., Hagenbuch B. Cloning/characterization of the canine organic anion transporting polypeptide 1b4 (Oatp1b4) and classification of the canine OATP/SLCO members // Comp Biochem Physiol C Toxicol Pharmacol. 2010. Vol. 151. P. 393–399. doi: 10.1016/j.cbpc.2010.01.005.

Hagenbuch B., Meier P.J. The superfamily of organic anion transporting polypeptides // Biochimica et Biophysica Acta. 2003.Vol. 1609. P. 1–18.

Hagenbuch B., Meier P. J. Organic anion transporting polypeptides of the OATP/SLC21 family: phylogenic classification as OATP/SLCO superfamily, new nomenclature and molecular/functional properties // Pflugers Arch. 2004. Vol. 447. P. 653-665.

Hagenbuch B., Gui C. Xenobiotic transporters of the human organic anion transporting polypeptides (OATP) family // Xenobiotica. 2008. Vol. 38. P. 778–801. doi: 10.1080/00498250801986951.

Hagenbuch B., Stieger B. The SLCO (former SLC21) superfamily of transporters // Molecular Aspects of Medicine. 2013. Vol. 34. P. 396–412. doi: 10.1016/j.mam.2012.10.009.

Hӓnggi E., Grundschober A.F., Leuthold S., Meier P.J., St-Pierre M.V. Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1 // Molecular Pharmacology. 2006. Vol.70. P. 806–817. doi:10.1124/mol.105.019547.

Hediger M. A., Romero M. F.,Peng J.-B., Rolfs A., Takanaga H., Bruford E. A. The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteins // Pflugers Arch - Eur J Physiol. 2004. Vol. 447. P. 465–468. doi: 10.1007/s00424-003-1192-y.

Hediger M. A., Clémençon B., Burrier R. E., Bruford E. A. The ABCs of membrane transporters in health and disease (SLC series): Introduction // Molecular Aspects of Medicine 2013. Vol. 34. P. 95–107. doi: 10.1016/j.mam.2012.12.009.

Hung AY, Sheng M. PDZ domains: Structural modules for protein complex assembly // J Biol Chem. 2002. Vol. 277 P. 5699–5702.

Katz D.A., Carr R., Grimm D.R., Xiong H., Holley-Shanks R., Mueller T., Leake B., Wang Q., Han L., Wang P.G., Edeki T., Sahelijo L., Doan T.,Allen A., Spear B.B., Kim R.B. Organic anion transporting polypeptide 1B1 activity classified by SLCO1B1 genotype influences atrasentan pharmacokinetics // Clin Pharmacol Ther. 2006. Vol. 79. P. 186–196. doi:10.1016/j.clpt.2005.11.003.

Kim E., Sheng M. PDZ domain proteins of synapses // Nat Rev Neurosci. 2004. Vol. 5. P. 771–781. doi:10.1038/nrn1517.

Kӧnig J., Cui Y., Nies A.T., Keppler D. Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide // J Biol Chem 2000. Vol. 275. P. 23161–23168.

Kӧnig J. Uptake transporters of the human OATP family. Molecular characteristics, substrates, their role in drug-drug interactions, and functional consequences of polymorphisms. // Handb Exp Pharmacol. 2011. Vol. 201. P. 1–28. doi: 10.1007/978-3-642-14541-4_1.

Kusuhara H, Sugiyama Y. In vitro-in vivo extrapolation of transporter-mediated clearance in the liver and kidney // Drug Metab Pharmacokinet. 2009. Vol. 24(1). P. 37–52.

Leuthold S., Hagenbuch B., Mohebbi N., Wagner C.A., Meier P.J., Stieger B. Mechanisms of pH-gradient driven transport mediated by organic anion polypeptide transporters // Am J Physiol Cell Physiol.2009. Vol. 296, #3. P. 570–582. doi: 10.1152/ajpcell.00436.2008.

Li L., Lee T. K., MeierP. J., Ballatori N. Identification of glutathione as a driving force and leukotriene C4 as a substrate for oatp1, the hepatic sinusoidal organic solute transporter //J Biol Chem. 1998. Vol. 273, # 26. P. 16184–16191.

Li L., Meier P. J., Ballatori N. Oatp2 mediates bidirectional organic solute transport: a role for intracellular glutathione // Molecular Pharmacology. 2000. Vol. 58 P. 335–340.

Mandery K., Sticht H., Bujok K., Schmidt I., Fahrmayr C., Balk B., Fromm M. F., Glaeser H. Functional and structural relevance of conserved positively charged lysine residues in organic anion transporting polypeptide 1B3 // Mol Pharmacol. 2011. Vol. 80, #3. P. 400–406. doi: 10.1124/mol.111.071282.

Meier-Abt F., Faulstich H., Hagenbuch B. Identification of phalloidin uptake systems of rat and human liver // Biochim. Biophys. Acta. 2004. Vol. 1664. P. 64–69. doi: 10.1016/j.bbamem.2004.04.004.

Meier-Abt F., Mokrab Y., Mizuguchi K. Organic anion transporting polypeptides of the OATP/SLCO superfamily: identification of new members in nonmammalian species, comparative modeling and a potential transport mode //J Membr Biol. 2005.Vol. 208. P. 213–227. doi:10.1007/s00232-005-7004-x.

Meier-Abt F., Hammann-Hänni A., Stieger B., Ballatori N., Boyer J.L.The organic anion transport polypeptide 1d1 (Oatp1d1) mediates hepatocellular uptake of phalloidin and microcystin into skate liver// Toxicology and Applied Pharmacology. 2007. Vol. 218. P. 274–279. doi:10.1016/j.taap.2006.11.015.

Niemi M., Backman J.T., Neuvonen M., Neuvonen P.J. Effects of gemfibrozil, itraconazole, and their combination on the pharmacokinetics and pharmacodynamics of repaglinide: Potentially hazardous interaction between gemfibrozil and repaglinide // Diabetologia. 2003. Vol. 46. P. 347–351. doi:10.1007/s00125-003-1034-7.

Pizzagalli F., Hagenbuch B., Stieger B., Klenk U., Folkers G., Meier P.J. Identification of a novel human organic anion transporting polypeptide as a high affinity thyroxine transporter // Mol. Endocrinol. 2002. Vol. 16. P. 2283–2296. doi:10.1210/me.2001-0309.

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DOI: http://dx.doi.org/10.17076/eb629

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