An amino acid mixture enhances insulin-stimulated glucose uptake in isolated rat epitrochlearis muscle
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An amino acid mixture enhances insulin-stimulated glucose uptake in isolated rat epitrochlearis muscle. / Kleinert, Maximilian; Liao, Yi Hung; Nelson, Jeffrey L; Bernard, Jeffrey R; Wang, Wanyi; Ivy, John L.
I: Journal of Applied Physiology, Bind 111, Nr. 1, 2011, s. 163-169.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - An amino acid mixture enhances insulin-stimulated glucose uptake in isolated rat epitrochlearis muscle
AU - Kleinert, Maximilian
AU - Liao, Yi Hung
AU - Nelson, Jeffrey L
AU - Bernard, Jeffrey R
AU - Wang, Wanyi
AU - Ivy, John L
N1 - (Ekstern)
PY - 2011
Y1 - 2011
N2 - Protein and certain amino acids (AA) have been found to lower blood glucose. Although these glucose-lowering AA are important modulators of skeletal muscle metabolism, their impact on muscle glucose uptake remains unclear. We therefore examined how an AA mixture consisting of 2 mM isoleucine, 0.012 mM cysteine, 0.006 mM methionine, 0.0016 mM valine, and 0.014 mM leucine impacts skeletal muscle glucose uptake in the absence or presence of a submaximal (sINS) or maximal insulin (mINS) concentration. The AA mixture, sINS, and mINS significantly increased 2-[3H]deoxyglucose (2-DG) uptake by 63, 79, and 298% above basal, respectively. When the AA mixture was combined with sINS and mINS, 2-DG uptake was further increased significantly by 26% (P = 0.028) and 14% (P = 0.032), respectively. Western blotting analysis revealed that the AA mixture increased basal and sINS Akt substrate of 160 kDa (AS160) phosphorylation, while AA mixture did not change phosphorylation of Akt or mammalian target of rapamycin (mTOR) under these conditions. Interestingly, addition of the AA mixture to mINS increased phosphorylation of mTOR, Akt as well as AS160, compared with mINS alone. These data suggest that certain AA increase glucose uptake in the absence of insulin and augment insulin-stimulated glucose uptake in an additive manner. Furthermore, these effects appear to be mediated via a pathway that is independent from the canonical insulin cascade and therefore may prove effective as an alternative therapeutic treatment for insulin resistance.
AB - Protein and certain amino acids (AA) have been found to lower blood glucose. Although these glucose-lowering AA are important modulators of skeletal muscle metabolism, their impact on muscle glucose uptake remains unclear. We therefore examined how an AA mixture consisting of 2 mM isoleucine, 0.012 mM cysteine, 0.006 mM methionine, 0.0016 mM valine, and 0.014 mM leucine impacts skeletal muscle glucose uptake in the absence or presence of a submaximal (sINS) or maximal insulin (mINS) concentration. The AA mixture, sINS, and mINS significantly increased 2-[3H]deoxyglucose (2-DG) uptake by 63, 79, and 298% above basal, respectively. When the AA mixture was combined with sINS and mINS, 2-DG uptake was further increased significantly by 26% (P = 0.028) and 14% (P = 0.032), respectively. Western blotting analysis revealed that the AA mixture increased basal and sINS Akt substrate of 160 kDa (AS160) phosphorylation, while AA mixture did not change phosphorylation of Akt or mammalian target of rapamycin (mTOR) under these conditions. Interestingly, addition of the AA mixture to mINS increased phosphorylation of mTOR, Akt as well as AS160, compared with mINS alone. These data suggest that certain AA increase glucose uptake in the absence of insulin and augment insulin-stimulated glucose uptake in an additive manner. Furthermore, these effects appear to be mediated via a pathway that is independent from the canonical insulin cascade and therefore may prove effective as an alternative therapeutic treatment for insulin resistance.
KW - Akt substrate of 160 kDa
KW - Isoleucine
KW - Skeletal muscle
UR - http://www.scopus.com/inward/record.url?scp=79960264780&partnerID=8YFLogxK
U2 - 10.1152/japplphysiol.01368.2010
DO - 10.1152/japplphysiol.01368.2010
M3 - Journal article
C2 - 21527668
AN - SCOPUS:79960264780
VL - 111
SP - 163
EP - 169
JO - Journal of Applied Physiology
JF - Journal of Applied Physiology
SN - 8750-7587
IS - 1
ER -
ID: 241155892