Linked Life Data

21520340

Source:http://linkedlifedata.com/resource/pubmed/id/21520340

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pubmed-article:21520340pubmed:issue7lld:pubmed
pubmed-article:21520340pubmed:dateCreated2011-6-28lld:pubmed
pubmed-article:21520340pubmed:abstractText?-Galactosidase deficiency is a group of lysosomal lipid storage disorders with an autosomal recessive trait. It causes two clinically different diseases, G(M1) -gangliosidosis and Morquio B disease. It is caused by heterogeneous mutations in the GLB1 gene coding for the lysosomal acid ?-galactosidase. We have previously reported the chaperone effect of N-octyl-4-epi-?-valienamine (NOEV) on mutant ?-galactosidase proteins. In this study, we performed genotype analyses of patients with ?-galactosidase deficiency and identified 46 mutation alleles including 9 novel mutations. We then examined the NOEV effect on mutant ?-galactosidase proteins by using six strains of patient-derived skin fibroblast. We also performed mutagenesis to identify ?-galactosidase mutants that were responsive to NOEV and found that 22 out of 94 mutants were responsive. Computational structural analysis revealed the mode of interaction between human ?-galactosidase and NOEV. Moreover, we confirmed that NOEV reduced G(M1) accumulation and ameliorated the impairments of lipid trafficking and protein degradation in ?-galactosidase deficient cells. These results provided further evidence to NOEV as a promising chaperone compound for ?-galactosidase deficiency.lld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:MatsudaJunich...lld:pubmed
pubmed-article:21520340pubmed:authorpubmed-author:SuzukiYoshiyu...lld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:YamamotoKoich...lld:pubmed
pubmed-article:21520340pubmed:authorpubmed-author:NinomiyaHarua...lld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:HigakiKatsumi...lld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:TakaiTomokoTlld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:IidaMasamiMlld:pubmed
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pubmed-article:21520340pubmed:authorpubmed-author:LiLinjingLlld:pubmed
pubmed-article:21520340pubmed:authorpubmed-author:OkuzawaSoichi...lld:pubmed
pubmed-article:21520340pubmed:authorpubmed-author:TakamuramAyum...lld:pubmed
pubmed-article:21520340pubmed:authorpubmed-author:IkehataHiroki...lld:pubmed
pubmed-article:21520340pubmed:copyrightInfo© 2011 Wiley-Liss, Inc.lld:pubmed
pubmed-article:21520340pubmed:issnTypeElectroniclld:pubmed
pubmed-article:21520340pubmed:volume32lld:pubmed
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pubmed-article:21520340pubmed:year2011lld:pubmed
pubmed-article:21520340pubmed:articleTitleChemical chaperone therapy: chaperone effect on mutant enzyme and cellular pathophysiology in ?-galactosidase deficiency.lld:pubmed
pubmed-article:21520340pubmed:affiliationDivision of Functional Genomics, Research Center for Bioscience and Technology, Tottori University, 86 Nishi-cho, Yonago, Japan. kh4060@med.tottori-u.ac.jplld:pubmed
pubmed-article:21520340pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:21520340pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed