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Functional characterization of vesicular excitatory amino acid transport by human sialin.
MedLine Citation:
PMID:  21781115     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Sialin, the protein coded by SLC17A5, is responsible for membrane potential (Δψ)-driven aspartate and glutamate transport into synaptic vesicles as well as H(+) /sialic acid co-transport in lysosomes. Rodent sialin mutants harboring the mutations associated with Salla disease in humans did not transport aspartate and glutamate whereas H(+) /sialic acid co-transport activity was about one-third of the wild type protein. Here we investigate the effects of various mutations on the transport activities of human sialin. Proteoliposomes containing purified heterologously expressed human sialin exhibited both Δψ-driven aspartate and glutamate transport activity and H(+) /sialic acid co-transport activity. Aspartate and glutamate transport was not detected in the R39C and K136E mutant forms of SLC17A5 protein associated with Salla disease, while H(+) /sialic acid co-transport activity corresponded to 30-50% of the recombinant wild type protein. In contrast, SLC17A5 protein harboring the mutations associated with infantile sialic acid storage disease (ISSD), H183R and Δ268SSLRN272 still showed normal levels of Δψ-driven aspartate and glutamate transport even though H(+) /sialic acid co-transport activity was absent. Human sialin carrying the G328E mutation that causes both phenotypes, and P334R and G378V mutations that cause ISSD showed no transport activity. These results support the idea that people suffering from Salla disease have been defective in aspartergic and glutamatergic neurotransmissions.
Authors:
Takaaki Miyaji; Hiroshi Omote; Yoshinori Moriyama
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-7-22
Journal Detail:
Title:  Journal of neurochemistry     Volume:  -     ISSN:  1471-4159     ISO Abbreviation:  -     Publication Date:  2011 Jul 
Date Detail:
Created Date:  2011-7-25     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Journal of Neurochemistry © 2011 International Society for Neurochemistry.
Affiliation:
Advanced Science Research Center, Okayama University, Okayama 700-8530, JAPAN. TEL/FAX: 086-251-7260 Department of Membrane Biochemistry, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, JAPAN. TEL/FAX: 086-251-7933.
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