Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.

Polyamine (putrescine, spermidine and spermine) and agmatine uptake by the human organic cation transporter 2 (hOCT2) was studied using HEK293 cells transfected with pCMV6-XL4/hOCT2. The Km values for putrescine and spermidine were 7.50 and 6.76 mM, and the Vmax values were 4.71 and 2.34 nmol/min/mg...

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Autores principales:	Kyohei Higashi, Masataka Imamura, Satoshi Fudo, Takeshi Uemura, Ryotaro Saiki, Tyuji Hoshino, Toshihiko Toida, Keiko Kashiwagi, Kazuei Igarashi
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/167099fd587e430ab52a376e61992d78
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spelling	oai:doaj.org-article:167099fd587e430ab52a376e61992d782021-11-25T06:08:37ZIdentification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.1932-620310.1371/journal.pone.0102234https://doaj.org/article/167099fd587e430ab52a376e61992d782014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25019617/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Polyamine (putrescine, spermidine and spermine) and agmatine uptake by the human organic cation transporter 2 (hOCT2) was studied using HEK293 cells transfected with pCMV6-XL4/hOCT2. The Km values for putrescine and spermidine were 7.50 and 6.76 mM, and the Vmax values were 4.71 and 2.34 nmol/min/mg protein, respectively. Spermine uptake by hOCT2 was not observed at pH 7.4, although it inhibited both putrescine and spermidine uptake. Agmatine was also taken up by hOCT2, with Km value: 3.27 mM and a Vmax value of 3.14 nmol/min/mg protein. Amino acid residues involved in putrescine, agmatine and spermidine uptake by hOCT2 were Asp427, Glu448, Glu456, Asp475, and Glu516. In addition, Glu524 and Glu530 were involved in putrescine and spermidine uptake activity, and Glu528 and Glu540 were weakly involved in putrescine uptake activity. Furthermore, Asp551 was also involved in the recognition of spermidine. These results indicate that the recognition sites for putrescine, agmatine and spermidine on hOCT2 strongly overlap, consistent with the observation that the three amines are transported with similar affinity and velocity. A model of spermidine binding to hOCT2 was constructed based on the functional amino acid residues.Kyohei HigashiMasataka ImamuraSatoshi FudoTakeshi UemuraRyotaro SaikiTyuji HoshinoToshihiko ToidaKeiko KashiwagiKazuei IgarashiPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e102234 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kyohei Higashi Masataka Imamura Satoshi Fudo Takeshi Uemura Ryotaro Saiki Tyuji Hoshino Toshihiko Toida Keiko Kashiwagi Kazuei Igarashi Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
description	Polyamine (putrescine, spermidine and spermine) and agmatine uptake by the human organic cation transporter 2 (hOCT2) was studied using HEK293 cells transfected with pCMV6-XL4/hOCT2. The Km values for putrescine and spermidine were 7.50 and 6.76 mM, and the Vmax values were 4.71 and 2.34 nmol/min/mg protein, respectively. Spermine uptake by hOCT2 was not observed at pH 7.4, although it inhibited both putrescine and spermidine uptake. Agmatine was also taken up by hOCT2, with Km value: 3.27 mM and a Vmax value of 3.14 nmol/min/mg protein. Amino acid residues involved in putrescine, agmatine and spermidine uptake by hOCT2 were Asp427, Glu448, Glu456, Asp475, and Glu516. In addition, Glu524 and Glu530 were involved in putrescine and spermidine uptake activity, and Glu528 and Glu540 were weakly involved in putrescine uptake activity. Furthermore, Asp551 was also involved in the recognition of spermidine. These results indicate that the recognition sites for putrescine, agmatine and spermidine on hOCT2 strongly overlap, consistent with the observation that the three amines are transported with similar affinity and velocity. A model of spermidine binding to hOCT2 was constructed based on the functional amino acid residues.
format	article
author	Kyohei Higashi Masataka Imamura Satoshi Fudo Takeshi Uemura Ryotaro Saiki Tyuji Hoshino Toshihiko Toida Keiko Kashiwagi Kazuei Igarashi
author_facet	Kyohei Higashi Masataka Imamura Satoshi Fudo Takeshi Uemura Ryotaro Saiki Tyuji Hoshino Toshihiko Toida Keiko Kashiwagi Kazuei Igarashi
author_sort	Kyohei Higashi
title	Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
title_short	Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
title_full	Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
title_fullStr	Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
title_full_unstemmed	Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
title_sort	identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/167099fd587e430ab52a376e61992d78
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_version_	1718414089364963328

Identification of functional amino acid residues involved in polyamine and agmatine transport by human organic cation transporter 2.

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