Vesicular polyamine transporter as a novel player in amine-mediated chemical transmission.
Biochim Biophys Acta Biomembr
; 1862(12): 183208, 2020 12 01.
Article
in En
| MEDLINE
| ID: mdl-32004521
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Polyamines
/
Cation Transport Proteins
Limits:
Animals
/
Humans
Language:
En
Journal:
Biochim Biophys Acta Biomembr
Year:
2020
Document type:
Article