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Sci Rep. 2014 Oct 30;4:6836. doi: 10.1038/srep06836.

Identification of a mammalian vesicular polyamine transporter.

Author information

1
Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8530, JAPAN.
2
Advanced Science Research Center, Okayama University, Okayama 700-8530, JAPAN.
3
Faculty of Bioscience, Nagahama Institute of Bio-science and Technology, Nagahama 526-0829, JAPAN.
4
1] Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama 700-8530, JAPAN [2] Advanced Science Research Center, Okayama University, Okayama 700-8530, JAPAN.

Abstract

Spermine and spermidine act as neuromodulators upon binding to the extracellular site(s) of various ionotropic receptors, such as N-methyl-d-aspartate receptors. To gain access to the receptors, polyamines synthesized in neurons and astrocytes are stored in secretory vesicles and released upon depolarization. Although vesicular storage is mediated in an ATP-dependent, reserpine-sensitive fashion, the transporter responsible for this process remains unknown. SLC18B1 is the fourth member of the SLC18 transporter family, which includes vesicular monoamine transporters and vesicular acetylcholine transporter. Proteoliposomes containing purified human SLC18B1 protein actively transport spermine and spermidine by exchange of H(+). SLC18B1 protein is predominantly expressed in the hippocampus and is associated with vesicles in astrocytes. SLC18B1 gene knockdown decreased both SLC18B1 protein and spermine/spermidine contents in astrocytes. These results indicated that SLC18B1 encodes a vesicular polyamine transporter (VPAT).

PMID:
25355561
PMCID:
PMC4213795
DOI:
10.1038/srep06836
[Indexed for MEDLINE]
Free PMC Article

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