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Conference Paper: Sedlin and prostaglandin E2 dehydrogenase - interactions and implications for spondyloepiphyseal dysplasia tarda

TitleSedlin and prostaglandin E2 dehydrogenase - interactions and implications for spondyloepiphyseal dysplasia tarda
Authors
Issue Date2012
PublisherThe RE(ACT) Congress 2012.
Citation
The 1st International Congress on Research of Rare and Orphan Diseases (RE(ACT) 2012), Basel, Switzerland, 29 February-2 March 2012. In Brochure of RE(ACT)® 2012, 2012, p. 112 How to Cite?
AbstractSpondyloepiphyseal dysplasia tarda (SEDT) is a rare X-linked, late-onset skeletal disease. Affected individuals develop phenotypes in their early childhood, displaying barrel-shaped chests, vertebral bodies malformation, flattened disc spaces and premature osteoarthritis in weight-bearing joints. The disease was found linked to the gene SEDL coding for the protein sedlin. Sedlin is one of the subunits of the TRAPP (Transport Protein Particle) complex, which is responsible for vesicle tethering during endoplasmic reticulum-to-golgi transport. Although sedlin is known to function in intracellular trafficking, the reason why mutations in a trafficking protein lead to a skeletal disease remains unknown. To address this, four missense mutations (D47Y, S73L, F83S and V130D) of sedlin observed in SEDT patients were studied. Except D47Y, the other three mutations cause proteosomal degradation of sedlin in cultured cells, whereas the D47Y mutation had a minor effect on Bet3 binding to sedlin. Pull-down assay was performed to identify novel sedlin interacting partners. 15-hydroxyprostaglandin dehydrogenase (PGDH) was pulled down and the interaction was confirmed in cell culture system. Sedlin activates PGDH activity in vitro. By confocal microscopy, sedlin was also found to colocalize with PGDH in the cytosol. PGDH catalyzes the degradation of prostaglandin E2, which affects cartilage and bone growth. Further investigation is ongoing to understand the function of sedlin and the mechanism of disease for SEDT.
DescriptionIn Brochure of RE(ACT)® 2012, 2012, p. 112
Session D - Genomic Disorders: abstract no. D020
Persistent Identifierhttp://hdl.handle.net/10722/146945

 

DC FieldValueLanguage
dc.contributor.authorChan, CWLen_US
dc.contributor.authorChoi, MMYen_US
dc.contributor.authorChan, CCYen_US
dc.contributor.authorChan, Den_US
dc.contributor.authorYu, SSBen_US
dc.contributor.authorCheah, KSEen_US
dc.contributor.authorTanner, JAen_US
dc.date.accessioned2012-05-23T05:50:58Z-
dc.date.available2012-05-23T05:50:58Z-
dc.date.issued2012en_US
dc.identifier.citationThe 1st International Congress on Research of Rare and Orphan Diseases (RE(ACT) 2012), Basel, Switzerland, 29 February-2 March 2012. In Brochure of RE(ACT)® 2012, 2012, p. 112en_US
dc.identifier.urihttp://hdl.handle.net/10722/146945-
dc.descriptionIn Brochure of RE(ACT)® 2012, 2012, p. 112-
dc.descriptionSession D - Genomic Disorders: abstract no. D020-
dc.description.abstractSpondyloepiphyseal dysplasia tarda (SEDT) is a rare X-linked, late-onset skeletal disease. Affected individuals develop phenotypes in their early childhood, displaying barrel-shaped chests, vertebral bodies malformation, flattened disc spaces and premature osteoarthritis in weight-bearing joints. The disease was found linked to the gene SEDL coding for the protein sedlin. Sedlin is one of the subunits of the TRAPP (Transport Protein Particle) complex, which is responsible for vesicle tethering during endoplasmic reticulum-to-golgi transport. Although sedlin is known to function in intracellular trafficking, the reason why mutations in a trafficking protein lead to a skeletal disease remains unknown. To address this, four missense mutations (D47Y, S73L, F83S and V130D) of sedlin observed in SEDT patients were studied. Except D47Y, the other three mutations cause proteosomal degradation of sedlin in cultured cells, whereas the D47Y mutation had a minor effect on Bet3 binding to sedlin. Pull-down assay was performed to identify novel sedlin interacting partners. 15-hydroxyprostaglandin dehydrogenase (PGDH) was pulled down and the interaction was confirmed in cell culture system. Sedlin activates PGDH activity in vitro. By confocal microscopy, sedlin was also found to colocalize with PGDH in the cytosol. PGDH catalyzes the degradation of prostaglandin E2, which affects cartilage and bone growth. Further investigation is ongoing to understand the function of sedlin and the mechanism of disease for SEDT.-
dc.languageengen_US
dc.publisherThe RE(ACT) Congress 2012.-
dc.relation.ispartofBrochure of RE(ACT)® 2012en_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titleSedlin and prostaglandin E2 dehydrogenase - interactions and implications for spondyloepiphyseal dysplasia tardaen_US
dc.typeConference_Paperen_US
dc.identifier.emailChan, CWL: ceccwl@hku.hken_US
dc.identifier.emailChoi, MMY: meiychoi@hku.hken_US
dc.identifier.emailChan, CCY: calebccy@hku.hken_US
dc.identifier.emailChan, D: chand@hku.hken_US
dc.identifier.emailCheah, KSE: hrmbdkc@hku.hken_US
dc.identifier.emailTanner, JA: jatanner@hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.identifier.authorityCheah, KSE=rp00342en_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.description.naturepostprint-
dc.identifier.hkuros199721en_US
dc.identifier.hkuros200861-
dc.identifier.spage112-
dc.identifier.epage112-
dc.publisher.placeSwitzerland-
dc.description.otherThe 1st International Congress on Research of Rare and Orphan Diseases (RE(ACT) 2012), Basel, Switzerland, 29 February-2 March 2012. In Brochure of RE(ACT)® 2012, 2012, p. 112-

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