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dc.contributor.authorLee, Na-Young-
dc.contributor.authorKim, Yunha-
dc.contributor.authorRyu, Hoon-
dc.contributor.authorKang, Young-Sook-
dc.date.accessioned2024-01-20T02:30:59Z-
dc.date.available2024-01-20T02:30:59Z-
dc.date.created2021-09-01-
dc.date.issued2017-01-29-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/123172-
dc.description.abstractThe alteration of D-serine levels is associated with the pathogenesis of sporadic ALS and mutant SOD1 (G93A) animal model of ALS. However, the exact mechanism of D-serine transport is not known in ALS. To better understand the distribution of D-serine in ALS, we determined the activity and the expression of serine transporter in a motor neuronal cell line model of ALS (NSC-34/hSOD1(G93A) cells). The uptake of [3H] D-serine was significantly lower in NSC-34/hSOD1(G93A) cells than in control NSC-34 and NSC-34/ hSOD1(wt) cells. In contrast, the uptake of [3H] L-serine, precursor of D-serine, was markedly increased in NSC-34/hSOD1(G93A) cells compared to control NSC-34 and NSC-34/hSOD1(wt) cells. Both [3H] D-serine and [3H] L-serine uptake were saturable in these cells. The estimated Michaelis-Menten constant, Km, for Dserine uptakes was higher in NSC-34/hSOD1(G93A) cells than in NSC-34/hSOD1(wt) cells while the Km for Lserine uptake was 2 fold lower in NSC-34/hSOD1(G93A) cells than in control cells. [3H] D-serine and [3H] Lserine uptakes took place in a Na+-dependent manner, and both uptakes were significantly inhibited by system ASC (alanine-serine-cysteine) substrates. As a result of small interfering RNA experiments, we found that ASCT2 (SLC1A5) and ASCT1 (SLC1A4) are involved in [3H] D-serine and [3H] L-serine uptake in NSC-34/hSOD1(G93A) cells, respectively. The level of SLC1A4 mRNA was significantly increased in NSC-34/ hSOD1(G93A) compared to NSC-34 and NSC-34/hSOD1(wt) cells. In contrast, the level of SLC7A10 mRNA was relatively lower in NSC-34/hSOD1(G93A) cells than the control cells. Together, these data suggest that the pathological alteration of D-and L-serine uptakes in ALS is driven by the affinity change of D-and L-serine uptake system. (C) 2016 Elsevier Inc. All rights reserved.-
dc.languageEnglish-
dc.publisherACADEMIC PRESS INC ELSEVIER SCIENCE-
dc.subjectAMINO-ACID TRANSPORTER-
dc.subjectHIGH-AFFINITY-
dc.subjectPRIMARY CULTURE-
dc.subjectMOTOR-NEURONS-
dc.subjectRECEPTOR-
dc.subjectRACEMASE-
dc.subjectCLONING-
dc.subjectASC-1-
dc.subjectEXPRESSION-
dc.subjectOXIDASE-
dc.titleThe alteration of serine transporter activity in a cell line model of amyotrophic lateral sclerosis (ALS)-
dc.typeArticle-
dc.identifier.doi10.1016/j.bbrc.2016.12.178-
dc.description.journalClass1-
dc.identifier.bibliographicCitationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.483, no.1, pp.135 - 141-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume483-
dc.citation.number1-
dc.citation.startPage135-
dc.citation.endPage141-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000397259000021-
dc.identifier.scopusid2-s2.0-85008452889-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiophysics-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaBiophysics-
dc.type.docTypeArticle-
dc.subject.keywordPlusAMINO-ACID TRANSPORTER-
dc.subject.keywordPlusHIGH-AFFINITY-
dc.subject.keywordPlusPRIMARY CULTURE-
dc.subject.keywordPlusMOTOR-NEURONS-
dc.subject.keywordPlusRECEPTOR-
dc.subject.keywordPlusRACEMASE-
dc.subject.keywordPlusCLONING-
dc.subject.keywordPlusASC-1-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusOXIDASE-
dc.subject.keywordAuthorAmyotrophic lateral sclerosis (ALS)-
dc.subject.keywordAuthorMotor neuron disease-
dc.subject.keywordAuthorD-Serine-
dc.subject.keywordAuthorL-Serine-
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