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Following the oral administration of [<jats:sup>14<\/jats:sup>C]teneligliptin to Sprague\u2013Dawley rats, it was predominantly distributed to the kidney and liver, followed by the lung, spleen and pituitary gland. The elimination half\u2010life (<jats:italic>t<\/jats:italic><jats:sub>1\/2<\/jats:sub>) of [<jats:sup>14<\/jats:sup>C]teneligliptin was 68.3 and 69.0 h in the kidney and liver, respectively; these values were about 10 times greater than the plasma <jats:italic>t<\/jats:italic><jats:sub>1\/2<\/jats:sub>. Of note, the elimination of [<jats:sup>14<\/jats:sup>C]teneligliptin from tissues with high DPP\u20104 activity (kidney, liver and lung) was slower in wild\u2010type rats than in DPP\u20104\u2010deficient rats, especially in the kidney. By contrast, in the heart and pancreas, which weakly express DPP\u20104, no difference was observed in [<jats:sup>14<\/jats:sup>C]teneligliptin concentrations between the two animal strains. In the kidney, most radioactivity was attributable to unchanged teneligliptin from 0.5 to 72 h after administration. The marked difference in the distribution of [<jats:sup>14<\/jats:sup>C]teneligliptin between the two strains suggests that the high binding affinity of teneligliptin for DPP\u20104 is involved in its tissue distribution. The currently marketed DPP\u20104 inhibitors are highly distributed to the liver, kidney and lung, but the extent of tissue distribution varies greatly among the drugs. The differences in the tissue distributions of DPP\u20104 inhibitors might be related to differences in their pleiotropic effects.  \u00a9 2016 The Authors Biopharmaceutics &amp; Drug Disposition Published by John Wiley &amp; Sons Ltd.<\/jats:p>","DOI":"10.1002\/bdd.2003","type":"journal-article","created":{"date-parts":[[2016,1,10]],"date-time":"2016-01-10T15:29:58Z","timestamp":1452439798000},"page":"142-155","source":"Crossref","is-referenced-by-count":16,"title":["Tissue distribution of teneligliptin in rats and comparisons with data reported for other dipeptidyl peptidase\u20104 inhibitors"],"prefix":"10.1002","volume":"37","author":[{"given":"Yoshinobu","family":"Nakamaru","sequence":"first","affiliation":[{"name":"Clinical Pharmacology Department, Development Division Mitsubishi Tanabe Pharma Co  <i>Chuo\u2010ku<\/i> Tokyo Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fumihiko","family":"Akahoshi","sequence":"additional","affiliation":[{"name":"Research Unit C, Research Division Mitsubishi Tanabe Pharma Co  Toda Saitama Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroaki","family":"Iijima","sequence":"additional","affiliation":[{"name":"Medical Affairs Department Mitsubishi Tanabe Pharma Co  <i>Chuo\u2010ku<\/i> Tokyo Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Noriko","family":"Hisanaga","sequence":"additional","affiliation":[{"name":"DMPK Research Laboratories, Research Division Mitsubishi Tanabe Pharma Co  Kisarazu Chiba Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Toshiyuki","family":"Kume","sequence":"additional","affiliation":[{"name":"DMPK Research Laboratories, Research Division Mitsubishi Tanabe Pharma Co  Kisarazu Chiba Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2016,4,24]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI30076"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmc.2011.09.043"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm050261p"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bmc.2012.08.012"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm030091l"},{"key":"e_1_2_7_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm070104l"},{"key":"e_1_2_7_8_1","doi-asserted-by":"crossref","first-page":"6450","DOI":"10.1021\/jm701280z","article-title":"8\u2010(3\u2010I\u2010aminopiperidin\u20101\u2010yl)\u20107\u2010but\u20102\u2010ynyl\u20103\u2010methyl\u20101\u2010(4\u2010methyl\u2010quinazolin\u20102\u2010ylmethyl)\u20103,7\u2010dihydropurine\u20102,6\u2010dione (BI 1356), a highly potent, selective, long\u2010acting, and orally bioavailable DPP\u20104 inhibitor for the treatment of type 2 diabetes","volume":"50","author":"Eckhardt M","year":"2007","journal-title":"J Med Chem"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm0493156"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1021\/jm00073a001"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2013.03.010"},{"key":"e_1_2_7_12_1","first-page":"9","article-title":"Teneligliptin, a novel selective dipeptidyl peptidase\u20104 inhibitor, improves postprandial hyperglycemia in a model of type 2 diabetes, Zucker diabetic fatty rats","volume":"49","author":"Kimata H","year":"2012","journal-title":"Med Consult New Remedies"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.2165\/11632930-000000000-00000"},{"key":"e_1_2_7_14_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1463-1326.2010.01212.x"},{"key":"e_1_2_7_15_1","doi-asserted-by":"publisher","DOI":"10.1358\/dot.2013.49.10.2035882"},{"key":"e_1_2_7_16_1","doi-asserted-by":"publisher","DOI":"10.1517\/14656566.2015.1000301"},{"key":"e_1_2_7_17_1","doi-asserted-by":"publisher","DOI":"10.3109\/00498254.2013.816891"},{"key":"e_1_2_7_18_1","doi-asserted-by":"publisher","DOI":"10.1002\/cpdd.29"},{"key":"e_1_2_7_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/cpdd.89"},{"key":"e_1_2_7_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/j"},{"key":"e_1_2_7_21_1","doi-asserted-by":"publisher","DOI":"10.1124\/dmd.108.026088"},{"key":"e_1_2_7_22_1","doi-asserted-by":"publisher","DOI":"10.1007\/s13318-013-0119-z"},{"key":"e_1_2_7_23_1","unstructured":"Nesina\u00ae (alogliptin) Common Technical Document.Takeda Pharmaceutical Company2010. 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