Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10803065 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2007 | 7 Pages |
Abstract
A novel organic cation transporter OCTN2 is indispensable for carnitine transport across plasma membrane and subsequent fatty acid metabolism in the mitochondria. Here, we report a novel splice variant of OCTN2 (OCTN2VT), in which a 72-base-pair sequence located in the first intron of OCTN2 gene was spliced between exons 1 and 2 of OCTN2, causing the insertion of 24 amino acids in the first extracellular loop of OCTN2. Despite the similarity between OCTN2 and OCTN2VT regarding primary structure and tissue distribution, their biochemical characteristics were significantly different. OCTN2 was expressed on the plasma membrane with robust N-glycosylation, whereas OCTN2VT was retained in the endoplasmic reticulum (ER) with poor N-glycosylation. In addition, the retention in the ER caused no carnitine uptake into the cells. These results demonstrate that the biochemical and functional characteristics of OCTN2VT are distinct from OCTN2 due to the insertion of 24 amino acids in the first extracellular loop.
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Authors
Satoshi Maekawa, Daisuke Mori, Tadashi Nishiya, Osamu Takikawa, Takahiro Horinouchi, Arata Nishimoto, Emi Kajita, Soichi Miwa,