Abstract
Leucine plays important signaling roles in maintaining both skeletal muscle and adipocyte functions. In this study, fully differentiated 3T3‐L1 adipocytes were cultured (top compartment of transwells) over C2C12 myotubes in high glucose Dulbecco's modification of Eagle's medium, in the presence or absence of additional leucine (5mM) for 48 h. The medium was used for secretomics by TMT quantitative proteomic analysis. Leucine enhanced (ratio>1.2) the concentration of 15 proteins (Uniprot_mouse database): including ptotein S100 (P97352), putative uncharacterized protein (Q8BTE9), heterogeneous nuclear ribonucleoprotein D (G5E8GO), corneodesmosin (Q7TPC1), insulin‐like growth factor 1 (Q547V2). In addition, leucine decreased the concentration of 14 proteins (ratio<0.75): including alpha‐1‐antitrypsin (E9PUC6), krt78 protein (A1L0X5), apolipoprotein (P34928), krt2 protein (B2RTP7), deocyhypusine hydroxylase (D3Z7J7). Thus co‐culture influences the secretion of proteins that secreted from myotubes and adipocytes involved primarily in cell growth and structure, RNA stability and cell signaling. The identification of local cross‐talk between myocytes and adipocytes provides insights into possible paracrine effects of altered leucine supply.
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