有哪些信誉好的足球投注网站amp-activated protein kinase (ampk) mediates nutrient regulation of thioredoxin-interacting protein (txnip) in pancreatic beta-cells活化蛋白激酶(ampk)介导thioredoxin-interacting蛋白质的营养调控胰岛细胞(txnip).pdfVIP
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amp-activated protein kinase (ampk) mediates nutrient regulation of thioredoxin-interacting protein (txnip) in pancreatic beta-cells活化蛋白激酶(ampk)介导thioredoxin-interacting蛋白质的营养调控胰岛细胞(txnip)
AMP-Activated Protein Kinase (AMPK) Mediates Nutrient
Regulation of Thioredoxin-Interacting Protein (TXNIP) in
Pancreatic Beta-Cells
. .
Maayan Shaked , Mali Ketzinel-Gilad , Erol Cerasi, Nurit Kaiser, Gil Leibowitz*
Endocrinology and Metabolism Service, Department of Medicine, Hadassah - Hebrew University Medical Center, Jerusalem, Israel
Abstract
Thioredoxin-interacting protein (TXNIP) regulates critical biological processes including inflammation, stress and apoptosis.
TXNIP is upregulated by glucose and is a critical mediator of hyperglycemia-induced beta-cell apoptosis in diabetes. In
contrast, the saturated long-chain fatty acid palmitate, although toxic to the beta-cell, inhibits TXNIP expression. The
mechanisms involved in the opposing effects of glucose and fatty acids on TXNIP expression are unknown. We found that
both palmitate and oleate inhibited TXNIP in a rat beta-cell line and islets. Palmitate inhibition of TXNIP was independent of
fatty acid beta-oxidation or esterification. AMP-activated protein kinase (AMPK) has an important role in cellular energy
sensing and control of metabolic homeostasis; therefore we investigated its involvement in nutrient regulation of TXNIP. As
expected, glucose inhibited whereas palmitate stimulated AMPK. Pharmacologic activators of AMPK mimicked fatty acids by
inhibiting TXNIP. AMPK knockdown increased TXNIP expression in presence of high glucose with and without palmitate,
indicating that nutrient (glucose and fatty acids) effects on TXNIP are mediated in part via modulation of AMPK activity.
TXNIP is transcriptionally regulated by carbohydrate response element-binding protein (ChREBP). Palmitate inhibited
glucose-stimulated ChREBP nuclear entry and recruitment to the Txni
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