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ALDOAAldolase A
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Previous studies have reported that fructose-bisphosphate aldolase A (ALDOA) mRNA increases during in vitro myogenesis (Colbert and Ciejek-Baez, 1988) are responsible for significant activation during the differentiation of primary myoblasts, therefore playing important roles in muscle gene transcription (Walsh et al., 1980; Hidaka et al., 1993; Ren et al., 2011).
As expected, proteins belonging to the same pathway (e.g., glycolysis) show overall good correlation (Figure S1.D, red CV% <35%), reflecting their regulated coexpression, but they also show quantitatively stable expression with other functional pathways: for example, the molar expression level of the Krebs cycle enzyme malate dehydrogenase 2 (MDH2) is relatively stable not only towards enzymes of the upstream glycolysis (ALDOA, TPI1, GAPDH, and PGK1), but also to the amount of downstream mitochondrial F0F1 ATPase (ATP5A1), and even to unrelated functional pathways such as proteins synthesis/turnover (ubiquitin C, UBC, and heat shock protein A8, HSPA8), cytoskeleton (profilin 1, PFN1), and cell signaling (calmodulin 1, CALM1).
Activity months old of PK and GAPDH (hippocampus, diminished cortex, striatum, and cerebellum) Hypotalamus and eEF-2, ALDOA, GSTA, [96] hypophysis from CKB, PPIA, PK, male Wistar GADPH, INA, CFL1 rats from 3,12 to 24 months old treated with an antioxidant MSC cultures Several proteins as [97] from the tibial members of the and femoral BM actin-binding of 83-week-and protein family of 12-month-old calponins, galectin- Sprague-Dawley 3 rats Retina Fisher 344- Increased: CD46, [98] Brown Norway FI GABA2, DJ-1, EBP50, rats from 3-4 Ezrin, Cathepsin D.