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Updated: Dec 29, 2025

A Plate-Based Assay for the Measurement of Endogenous Monoamine Release in Acute Brain Slices
Published on: August 11, 2021
Vesicular polyamine transporter as a novel player in amine-mediated chemical transmission
Yoshinori Moriyama1, Ryo Hatano2, Satomi Moriyama3
1Department of Biochemistry, Matsumoto Dental University, Shiojiri 399-0781, Japan; Division of Endocrinology and Metabolism, Department of Internal Medicine, Kurume University School of Medicine, Kurume 830-0011, Japan; CYRIC Tohoku University, Sendai 980-8578, Japan.
Abstract:
The solute carrier 18B1 (SLC18B1) is the most recently identified gene of the vesicular amine transporter family and is conserved in the animal kingdom from insects to humans. Proteoliposomes containing the purified human SLC18B1 protein transport not only monoamines, but also polyamines, such as spermidine (Spd) and spermine (Spm), using an electrochemical gradient of H+ established by vacuolar H+-ATPase (V-ATPase) as the driving force. SLC18B1 gene knockdown abolished the exocytosis of polyamines from mast cells, which affected the secretion of histamine. SLC18B1 gene knockout decreased polyamine levels by ~20% in the brain, and impaired short- and long-term memory. Thus, the SLC18B1 protein is responsible for the vesicular storage and release of polyamines, and functions as a vesicular polyamine transporter (VPAT). VPAT may define when, where, and how polyamine-mediated chemical transmission occurs, providing insights into the more versatile and complex features of amine-mediated chemical transmission than currently considered.
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