Proteomic identification and characterization of hepatic glyoxalase 1 dysregulation in non-alcoholic fatty liver disease View Full Text


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Article Info

DATE

2018-02-14

AUTHORS

Christos Spanos, Elaina M. Maldonado, Ciarán P. Fisher, Petchpailin Leenutaphong, Ernesto Oviedo-Orta, David Windridge, Francisco J. Salguero, Alexandra Bermúdez-Fajardo, Mark E. Weeks, Caroline Evans, Bernard M. Corfe, Naila Rabbani, Paul J. Thornalley, Michael H. Miller, Huan Wang, John F. Dillon, Alberto Quaglia, Anil Dhawan, Emer Fitzpatrick, J. Bernadette Moore

ABSTRACT

BackgroundNon-alcoholic fatty liver disease (NAFLD) is the most common liver disease worldwide. However, its molecular pathogenesis is incompletely characterized and clinical biomarkers remain scarce. The aims of these experiments were to identify and characterize liver protein alterations in an animal model of early, diet-related, liver injury and to assess novel candidate biomarkers in NAFLD patients.MethodsLiver membrane and cytosolic protein fractions from high fat fed apolipoprotein E knockout (ApoE−/−) animals were analyzed by quantitative proteomics, utilizing isobaric tags for relative and absolute quantitation (iTRAQ) combined with nano-liquid chromatography and tandem mass spectrometry (nLC-MS/MS). Differential protein expression was confirmed independently by immunoblotting and immunohistochemistry in both murine tissue and biopsies from paediatric NAFLD patients. Candidate biomarkers were analyzed by enzyme-linked immunosorbent assay in serum from adult NAFLD patients.ResultsThrough proteomic profiling, we identified decreased expression of hepatic glyoxalase 1 (GLO1) in a murine model. GLO1 protein expression was also found altered in tissue biopsies from paediatric NAFLD patients. In vitro experiments demonstrated that, in response to lipid loading in hepatocytes, GLO1 is first hyperacetylated then ubiquitinated and degraded, leading to an increase in reactive methylglyoxal. In a cohort of 59 biopsy-confirmed adult NAFLD patients, increased serum levels of the primary methylglyoxal-derived advanced glycation endproduct, hydroimidazolone (MG-H1) were significantly correlated with body mass index (r = 0.520, p < 0.0001).ConclusionCollectively these results demonstrate the dysregulation of GLO1 in NAFLD and implicate the acetylation-ubquitination degradation pathway as the functional mechanism. Further investigation of the role of GLO1 in the molecular pathogenesis of NAFLD is warranted. More... »

PAGES

4

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URI

http://scigraph.springernature.com/pub.10.1186/s12953-018-0131-y

DOI

http://dx.doi.org/10.1186/s12953-018-0131-y

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https://app.dimensions.ai/details/publication/pub.1101037316

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29456458


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