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Title

A tandem mass tag (TMT) proteomic analysis during the early phase of experimental pancreatitis reveals new insights in the disease pathogenesis

Authors
García-Hernández, Violeta
Sánchez-Bernal, Carmen
Calvo, José J
Sánchez-Yagüe, Jesús
Published in Journal of Proteomics. 2018, vol. 181, p. 190-200
Abstract Changes in the protein expression occurring within the initiation phase of acute pancreatitis (AP) might be vital in the development of this complex disease. However, the exact mechanisms involved in the onset of AP remains elusive and most of our knowledge about the pathobiology of AP comes from animal models. We performed in a rat pancreatitic model a high-throughput shotgun proteomic profiling of the soluble and whole membrane fractions from the pancreas during the early phase of cerulein (Cer)-induced AP. We identified 997 proteins, of which 353 were significantly different (22, 276 or 55 in both, the soluble or the membrane fractions, respectively). Gene Ontology and KEGG PATHWAY analyses revealed that these proteins were implicated in molecular mechanisms relevant to AP pathogenesis, including vesicle-mediated and protein transport, lysosomal and mitochondrial impairment or proteolysis. Numerous metabolic processes were downregulated apparently to reduce energy consumption, and a remarkable increase in inflammatory and stress responses was also highlighted. The proteomic data were verified by immunoblotting of 11 and 7 different soluble or membrane-associated proteins, either novel (VPS29 and MCTS1) or known factors in AP. Also, our first observation of the imbalance of some COP proteins during AP early phase deserves further characterization.
Identifiers
PMID: 29678717
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Article (Published version) (1.9 MB) - document accessible for UNIGE members only Limited access to UNIGE
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Research group Groupe de Protéomique biomédicale (635)
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GARCÍA-HERNÁNDEZ, Violeta et al. A tandem mass tag (TMT) proteomic analysis during the early phase of experimental pancreatitis reveals new insights in the disease pathogenesis. In: Journal of Proteomics, 2018, vol. 181, p. 190-200. https://archive-ouverte.unige.ch/unige:114678

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Deposited on : 2019-03-01

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