Myocardium proteome remodelling after nutritional deprivation of methyl donors

Methyl donor deficiency in H9c2 cardiomyoblasts induces ER stress as an important part of the proteome response

“…4). The same profile was observed for the mRNA level of prohibitin (Phb), a mitochondrial protein with chaperone activity previously found to be upregulated in the myocardium of MD-deficient rat pups (Martinez et al, 2013). It is noticeable that the magnitude of the variations was globally higher after MD deficiency than after folate deficiency.…”

“…Concurrently increased protein carbonylation owing to oxidative stress could account for the decreased abundance of many of these proteins (Martinez et al, 2013). In the present study we demonstrated that altered proteomes of FD and MDD H9c2 cells include proteins involved in protein synthesis, folding and degradation, cell structure and energy metabolism, as discussed below.…”

“…H9c2 cells from the clonal myoblastic cell line, derived from embryonic rat heart (ATCC, LGC Standards, Molsheim, France), were cultured as previously described (Martinez et al, 2013). Folateand MD-deficient (FD and MDD) media were made in-house from synthetic MCDB 131 medium lacking folic acid or folic acid, vitamin B12 and choline, respectively.…”

“…Alternatively, modified proteins can aggregate, contributing to cytoskeleton disorganization and further cell functional impairment (Castro et al, 2012). Our earlier results also demonstrated that the proteome of myocardium of rat pups was dramatically altered after maternal MD deprivation (Martinez et al, 2013). Especially, marked changes were observed in the abundance of several heat shock proteins (Hsps).…”

“…Recently, MD deficiency was related to ventricular hypertrophy in rat pups concurrently with impaired lipid and energy metabolism (Garcia et al, 2011) and we further showed that total protein carbonylation was increased in the myocardium of these animals (Martinez et al, 2013). Carbonylation is an irreversible oxidative post-translational modification (PTM) leading to nonfunctional conformation of proteins (Brioschi et al, 2012).…”