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A tissue-specific variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase with substrate specificity

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dc.contributor.authorLee, Jae-Eun-
dc.contributor.authorKim, Youngho-
dc.date.available2021-02-22T15:17:23Z-
dc.date.created2020-09-01-
dc.date.issued2006-12-08-
dc.identifier.issn0021-9258-
dc.identifier.urihttps://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/14997-
dc.description.abstractThe human lysyl oxidase-like 3 (LOXL3) encodes a member of the emerging family of lysyl oxidase (LOX) that functions as a copper-dependent amine oxidase. The LOXL3 protein contains four scavenger receptor cysteine-rich domains in the N terminus in addition to the C-terminal characteristic domains of the LOX family, such as a copper binding domain, a cytokine receptor-like domain and residues for the lysyl-tyrosyl quinone cofactor. Using BLASTN searches, we identified a LOXL3 variant LOXL3-sv1 that lacked the sequences corresponding to exons 1, 2, 3, and 5 of LOXL3. LOXL3-sv1 showed an exon-intron structure distinct from LOXL3, additionally containing an 80-bp sequence corresponding to intron 3 of LOXL3 in the 5'-UTR and a 561-bp sequence corresponding to the 3'-flanking genomic region of exon 14 in the 3'-UTR. LOXL3-sv1 was predicted to encode a polypeptide of 392 amino acids that contains the C-terminal domains required for amine oxidase activity but lacks the N-terminal SRCR domains 1, 2, and 3. The recombinant LOXL3-sv1 protein showed a beta-amino-propionitrile-inhibitable amine oxidase activity toward elastin and collagen with substrate specificity. In RT-PCR assays with various human tissues, LOXL3-sv1 and LOXL3 showed distinct expression patterns. Further, luciferase reporter assays revealed a strong promoter element in intron 3 that probably functions as a regulatory region for the expression of LOXL3-sv1. These findings strongly indicate that LOXL3 encodes two variants, LOXL3 and LOXL3-sv1, both of which function as amine oxidases with distinct tissue and substrate specificities from one another.-
dc.language영어-
dc.language.isoen-
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC-
dc.subjectCYSTEINE-RICH DOMAIN-
dc.subjectLIVER FIBROSIS-
dc.subjectCUTIS LAXA-
dc.subjectGENE-
dc.subjectCOLLAGEN-
dc.subjectEXPRESSION-
dc.subjectSEQUENCE-
dc.subjectELASTIN-
dc.subjectCLONING-
dc.subjectENZYME-
dc.titleA tissue-specific variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase with substrate specificity-
dc.typeArticle-
dc.contributor.affiliatedAuthorLee, Jae-Eun-
dc.identifier.doi10.1074/jbc.M600977200-
dc.identifier.scopusid2-s2.0-33846013585-
dc.identifier.wosid000242477100005-
dc.identifier.bibliographicCitationJOURNAL OF BIOLOGICAL CHEMISTRY, v.281, no.49, pp.37282 - 37290-
dc.relation.isPartOfJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.citation.titleJOURNAL OF BIOLOGICAL CHEMISTRY-
dc.citation.volume281-
dc.citation.number49-
dc.citation.startPage37282-
dc.citation.endPage37290-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.subject.keywordPlusCYSTEINE-RICH DOMAIN-
dc.subject.keywordPlusLIVER FIBROSIS-
dc.subject.keywordPlusCUTIS LAXA-
dc.subject.keywordPlusGENE-
dc.subject.keywordPlusCOLLAGEN-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusSEQUENCE-
dc.subject.keywordPlusELASTIN-
dc.subject.keywordPlusCLONING-
dc.subject.keywordPlusENZYME-
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