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Mitofusin-2 Determines Mitochondrial Network Architecture and Mitochondrial Metabolism
It is shown that Mfn2 (mitofusin 2), a mitochondrial membrane protein that participates in mitochondrial fusion in mammalian cells, is induced during myogenesis and contributes to the maintenance and operation of the mitochondrial network.
Prolonged increase in insulin-stimulated glucose transport in muscle after exercise.
- G. Cartee, D. Young, M. Sleeper, J. Zierath, H. Wallberg-Henriksson, J. Holloszy
- Biology, MedicineThe American journal of physiology
- 1 April 1989
The persistent increase in insulin sensitivity after exercise in carbohydrate-deprived rats was unrelated to caloric intake, as muscles of fasted and fat-fed rats behaved similarly.
Insulin action and insulin resistance in human skeletal muscle
Current understanding of the molecular mechanisms regulating insulin action and the factors contributing to insulin resistance in human skeletal muscle are focused on.
Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients.
In skeletal muscle from type 2 diabetic subjects, IRS-1 phosphorylation, PI 3-kinase activity, and glucose transport activity were impaired, whereas insulin receptor tyrosine phosphorylations, MAP kinase phosphorylated, and glycogen synthase activity were normal.
Expression of Mfn2, the Charcot-Marie-Tooth neuropathy type 2A gene, in human skeletal muscle: effects of type 2 diabetes, obesity, weight loss, and the regulatory role of tumor necrosis factor alpha…
In vivo modulation of Mfn2 mRNA levels is an additional level of regulation for the control of muscle metabolism and could provide a molecular mechanism for alterations in mitochondrial function in obesity or type 2 diabetes.
Exercise-induced changes in expression and activity of proteins involved in insulin signal transduction in skeletal muscle: differential effects on insulin-receptor substrates 1 and 2.
Increased insulin-stimulated glucose transport after exercise is not limited to increased GLUT4 expression, and the differential response of IRS-1 and IRS-2 to exercise suggests that these molecules have specialized, rather than redundant, roles in insulin signaling in skeletal muscle.
Divergent effects of exercise on metabolic and mitogenic signaling pathways in human skeletal muscle
The data do not support a role of Akt or PYK2 in exercise/contraction‐induced signaling in human skeletal muscle, and exercise has divergent effects on parallel MAP kinase pathways, of which only p38 demonstrated a systemic response.
Insulin-Stimulated Akt Kinase Activity Is Reduced in Skeletal Muscle From NIDDM Subjects
- A. Krook, R. Roth, X. Jiang, J. Zierath, H. Wallberg-Henriksson
- Medicine, BiologyDiabetes
- 1 August 1998
Parallel defects in insulin-stimulated Akt Kinase activity and glucose transport in diabetic skeletal muscle suggest that reduced Akt kinase activity may play a role in the development of insulin resistance in NIDDM.
Insulin action on glucose transport and plasma membrane GLUT4 content in skeletal muscle from patients with NIDDM
- J. Zierath, L. He, A. Gumà, E. Wahlström, A. Klip, H. Wallberg-Henriksson
- Medicine, BiologyDiabetologia
- 1 October 1996
The results suggest that insulin-stimulated glucose transport in skeletal muscle from patients with NIDDM is down-regulated in the presence of hyperglycaemia, which may result in resistance to any further insulin-induced gain of GLUT4 at the level of the plasma membrane.