Matches in Nanopublications for { ?s ?p "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." ?g. }
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- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.
- _4 value "Resistin causes defective AMPK activation in response to insulin. Since AMPK signaling affects insulin-sensitive glucose metabolism (19 22) and since AMPK can act upstream of Akt signaling (23, 24), we assessed whether resistin overexpression alters AMPK activity. As demonstrated in Figure 7, AMPK phosphorylation (Thr172) was reduced by 60%, 35%, and 64% (P 0.01) in the skeletal muscle, adipose tissue, and liver of rats injected with Adv-resistin, respectively, while AMPK protein content remained unchanged." provenance.