dc.contributor.author | Mueller, Stefan | |
dc.contributor.author | Pekmez, Murat | |
dc.contributor.author | Hanisch, Franz-Georg | |
dc.contributor.author | Staubach, Simon | |
dc.date.accessioned | 2021-03-04T11:34:36Z | |
dc.date.available | 2021-03-04T11:34:36Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Staubach S., Mueller S., Pekmez M., Hanisch F., "Classical Galactosemia: Insight into Molecular Pathomechanisms by Differential Membrane Proteomics of Fibroblasts under Galactose Stress", JOURNAL OF PROTEOME RESEARCH, cilt.16, sa.2, ss.516-527, 2017 | |
dc.identifier.issn | 1535-3893 | |
dc.identifier.other | av_72fe2dcf-b33b-465a-aad8-21d57b261ba6 | |
dc.identifier.other | vv_1032021 | |
dc.identifier.uri | http://hdl.handle.net/20.500.12627/79121 | |
dc.identifier.uri | https://doi.org/10.1021/acs.jproteome.6b00658 | |
dc.description.abstract | Classical galactosemia, a hereditary metabolic disease caused by the deficiency of galactose-1-phosphate uridyltransferase (GALT; EC 2.7.712), results in an impaired galactose metabolism and serious long-term developmental affection of the CNS and ovaries, potentially related in part to endogenous galactose-induced protein dysglycosylation. In search for galactose-induced changes in membrane raft proteomes of GALT-deficient cells, we performed differential analyses of lipid rafts from patient-derived (Q) and sex- and age-matched control fibroblasts (H) in the presence or absence of the stressor. Label based proteomics revealed of the total 454 (female) or 678 (male) proteins a proportion of similar to 12% in at least one of four relevant ratios as fold-changed. GALT(-) cell-specific effects in the absence of stressor revealed cell-model-dependent affection of biological processes related to protein targeting to the plasma membrane (female) or to cellular migration (male). However, a series of common galactose-induced effects were observed, among them the strongly increased ER-stress marker GRP78 and calreticulin involved in N-glycoprotein quality control. The membrane-anchored N-glycoprotein receptor CD109 was concertedly decreased under galactose-stress together with cadherin-13, GLIPR1, glypican-1, and semaphorin-7A. A series of proteins showed opposite fold-changes in the two cell models, whereas others fluctuated in only one of the two models. | |
dc.language.iso | eng | |
dc.subject | Biyokimya | |
dc.subject | Yaşam Bilimleri | |
dc.subject | Moleküler Biyoloji ve Genetik | |
dc.subject | Sitogenetik | |
dc.subject | Temel Bilimler | |
dc.subject | Sağlık Bilimleri | |
dc.subject | Temel Tıp Bilimleri | |
dc.subject | Tıp | |
dc.subject | Moleküler Biyoloji ve Genetik | |
dc.subject | BİYOKİMYA VE MOLEKÜLER BİYOLOJİ | |
dc.subject | Yaşam Bilimleri (LIFE) | |
dc.subject | Biyoloji ve Biyokimya | |
dc.subject | BİYOKİMYASAL ARAŞTIRMA YÖNTEMLERİ | |
dc.title | Classical Galactosemia: Insight into Molecular Pathomechanisms by Differential Membrane Proteomics of Fibroblasts under Galactose Stress | |
dc.type | Makale | |
dc.relation.journal | JOURNAL OF PROTEOME RESEARCH | |
dc.contributor.department | University of Cologne , , | |
dc.identifier.volume | 16 | |
dc.identifier.issue | 2 | |
dc.identifier.startpage | 516 | |
dc.identifier.endpage | 527 | |
dc.contributor.firstauthorID | 240562 | |