Differential activation of AKT isoforms by growth factors in human myotubes

AKT signaling plays a crucial role in muscle physiology, and is activated by stimuli, including insulin, growth factors, and exercise. Three AKT isoforms have been identified in mammals, and they possess both distinct and redundant functions. However, it is currently unknown what the predominant AKT...

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Bibliographic Details
Published in:Physiological reports 2023-10, Vol.11 (20), p.e15805-n/a
Main Authors: Roberts, Brandon M., Geddis, Alyssa V., Matheny, Ronald W.
Format: Article
Language:English
Subjects:
AKT protein
AKT1 protein
AKT2 protein
anabolic
Antibodies
Cell culture
Cell cycle
Chromatography
Glucose
Growth factors
Insulin
Insulin-like growth factor I
Insulin-like growth factors
Isoforms
Kinases
Liquid chromatography
Lysates
Mass spectrometry
Mass spectroscopy
Metabolism
Musculoskeletal system
myosin
Myotubes
Original
Phosphorylation
Physiology
PKB
protein synthesis
Proteins
Scientific imaging
Skeletal muscle
White people
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Summary:AKT signaling plays a crucial role in muscle physiology, and is activated by stimuli, including insulin, growth factors, and exercise. Three AKT isoforms have been identified in mammals, and they possess both distinct and redundant functions. However, it is currently unknown what the predominant AKT isoform is in primary human skeletal myotubes, and very little is known regarding the effects of insulin and insulin‐like growth factor‐I (IGF‐I) on AKT isoforms activation in human myotubes. Thus, we sought to determine the abundances of each AKT isoform in primary human skeletal myotubes and their responses to insulin or IGF‐I. Analysis of protein lysates by liquid chromatography‐parallel reaction monitoring/mass spectrometry revealed that AKT1 was the most abundant AKT isoform and AKT3 was the least‐abundant isoform. Next, myotubes were treated with either 100 nM insulin or 10 nM IGF‐I for 5, 20, 45, or 60 min. In response to insulin, there was a significant treatment effect on phosphorylation of AKT1 and AKT2, but not AKT3 (p 
ISSN:2051-817X
DOI:10.14814/phy2.15805