MS-based proteomic analysis of cardiac response to hypoxia in the goldfish (Carassius auratus).
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
12 12 2019
12 12 2019
Historique:
received:
29
07
2019
accepted:
25
10
2019
entrez:
14
12
2019
pubmed:
14
12
2019
medline:
4
11
2020
Statut:
epublish
Résumé
The exceptional hypoxia tolerance of the goldfish heart may be achieved through the activation of an alternative mechanism recruiting the first product of the anaerobic glycolysis (i.e. piruvate). This hypothesis led to design a classical mass spectrometry based proteomic study to identify in the goldfish cardiac proteins that may be associated with maintaining heart function under normoxia and hypoxia. A selective protein solubilization, SDS PAGE, trypsin digestion and MALDI MS/MS analysis allowed the identification of the 12 most stable hypoxia-regulated proteins. Among these proteins, five are enzymes catalyzing reversible steps of the glycolysis/gluconeogenesis network. Protein composition reveals the presence of fructose-1,6-bisphosphate aldolase B as a specific hypoxia-regulated protein. This work indicated that the key enzyme of reversible steps of the glycolysis/gluconeogenesis network is fructose-1,6-bisphosphate, aldolase B, suggesting a role of gluconeogenesis in the mechanisms involved in the goldfish heart response to hypoxia.
Identifiants
pubmed: 31831848
doi: 10.1038/s41598-019-55497-w
pii: 10.1038/s41598-019-55497-w
pmc: PMC6908699
doi:
Substances chimiques
Fish Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
18953Références
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