Preliminary report: The effects of phospholipase C inhibition on insulin-stimulated glucose transport in skeletal muscle

Wright, David C.; Craig, Bruce W.; Fick, Christopher A.; Lim, K

doi:10.1053/meta.2002.30500

Cited by 14 publications

(10 citation statements)

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“…Contreras-Ferrat et al (15) revealed that insulin induces Ca 2+ transient through their release from IP 3 -sensitive sarcoplasmic reticulum stores, which is responsible for glucose uptake via GLUT4 in primary neonatal cardiomyocytes. Insulin activated phospholipase C, resulting in increased glucose uptake in skeletal muscle (36). Our study confirms that insulin-induced Ca 2+ transient and glucose uptake is dependent on IP 3 by showing that XesC completely inhibits insulin-induced Ca 2+ transient and glucose uptake (Figs.…”

Section: Discussionsupporting

confidence: 84%

Exercise Ameliorates Insulin Resistance via Ca2+ Signals Distinct From Those of Insulin for GLUT4 Translocation in Skeletal Muscles

Park

Kim

et al. 2014

Diabetes

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Muscle contraction and insulin induce glucose uptake in skeletal muscle through GLUT4 membrane translocation. Beneficial effects of exercise on glucose homeostasis in insulin-resistant individuals are known to be due to their distinct mechanism between contraction and insulin action on glucose uptake in skeletal muscle. However, the underlying mechanisms are not clear. Here we show that in skeletal muscle, distinct Ca 2+ second messengers regulate GLUT4 translocation by contraction and insulin treatment; D-myo-inositol 1,4,5-trisphosphate/nicotinic acid adenine dinucleotide phosphate (NAADP) and cyclic ADP-ribose/NAADP are main players for insulin-and contraction-induced glucose uptake, respectively. Different patterns of phosphorylation of AMPK and Ca 2+ /calmodulindependent protein kinase II were shown in electrical stimuli (ES)-and insulin-induced glucose uptake pathways. ES-induced Ca 2+ signals and glucose uptake are dependent on glycolysis, which influences formation of NAD(P)-derived signaling messengers, whereas insulininduced signals are not. High-fat diet (HFD) induced a defect in only insulin-mediated, but not ES-mediated, Ca 2+ signaling for glucose uptake, which is related to a specifically lower NAADP formation. Exercise decreases blood glucose levels in HFD-induced insulin resistance mice via NAADP formation. Thus we conclude that different usage of Ca 2+ signaling in contraction/insulin-stimulated glucose uptake in skeletal muscle may account for the mechanism by which exercise ameliorates glucose homeostasis in individuals with type 2 diabetes.Both insulin and contraction induce the translocation of GLUT4 from the interior of the muscle cell to the cell membrane, leading to an increase in glucose uptake into the muscle cell (1,2). However, evidence indicates that contraction-induced GLUT4 translocation uses a mechanism distinct from that of insulin (3,4). This is the basis behind the beneficial effects of exercise in cases where insulin resistance is present, such as type 2 diabetes (5,6). However, the exact mechanisms by which insulin and contraction induce glucose transport are not clear. Ca 2+ plays a versatile role in intracellular signaling (7). Mammalian cells have specific Ca 2+ signals for particular cellular processes. Ca 2+ second messengers control intracellular Ca 2+ levels by mobilizing Ca 2+ from intracellular stores, including the sarcoplasmic reticulum, lysosomes, and mitochondria (8). D-myo-inositol 1,4,5-trisphosphate (IP 3 ), cyclic ADP-ribose (cADPR), and nicotinic acid adenine dinucleotide phosphate (NAADP) are well-characterized Ca 2+ second messengers. IP 3 is produced by phospholipase C, and the latter two by ADP-ribosyl cyclases, including CD38 (9-11). Ca 2+ signals in skeletal muscle mediate a variety of physiological processes, including muscle contraction and cell metabolism

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Section: Discussionsupporting

confidence: 84%

Exercise Ameliorates Insulin Resistance via Ca2+ Signals Distinct From Those of Insulin for GLUT4 Translocation in Skeletal Muscles

Park

Kim

et al. 2014

Diabetes

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“…The specific PKβII inhibitor, CG53353 supports this conclusion. Demonstrating a role for PKCβII in cultured myotubes (both primary and cell line) insulin responsiveness was confirmed by other laboratories [12] including Sampson's lab, Formisano's lab (personal communication) and laboratories working on intact muscle showing a requirement for PKCβII in insulin stimulated glucose uptake [88,89].…”

Section: Pkcβiimentioning

confidence: 75%

Specific protein kinase C isoforms as transducers and modulators of insulin signaling

Sampson

Cooper

2006

Molecular Genetics and Metabolism

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Recent studies implicate specific PKC isoforms in the insulin-signaling cascade. Insulin activates PKCsα, βII, δ and ζ in several cell types. In addition, as will be documented in this review, certain members of the PKC family may also be activated and act upstream of PI3 and MAP kinases. Each of these isoforms has been shown one way or another either to mimic or to modify insulin-stimulated effects in one or all of the insulin-responsive tissues. Moreover, each of the isoforms has been shown to be activated by insulin stimulation or conditions important for effective insulin stimulation. Studies attempting to demonstrate a definitive role for any of the isoforms have been performed on different cells, ranging from appropriate model systems for skeletal muscle, liver and fat, such as primary cultures, and cell lines and even in vivo studies, including transgenic mice with selective deletion of specific PKC isoforms. In addition, studies have been done on certain expression systems such as CHO or HEK293 cells, which are far removed from the tissues themselves and serve mainly as vessels for potential protein-protein interactions. Thus, a clear picture for many of the isoforms remains elusive in spite of over two decades of intensive research. The recent intrusion of transgenic and precise molecular biology technologies into the research armamentarium has opened a wide range of additional possibilities for direct involvement of individual isoforms in the insulin signaling cascade. As we hope to discuss within the context of this review, whereas many of the long soughtafter answers to specific questions are not yet clear, major advances have been made in our understanding of precise roles for individual PKC isoforms in mediation of insulin effects. In this review, in which we shall focus our attention on isoforms in the conventional and novel categories, a clear case will be made to show that these isoforms are not only expressed but are importantly involved in regulation of insulin metabolic effects.

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“…Glucose transport was determined as described previously (Wright et al, 2002). Briefly, clamped muscles were placed in sealed vials containing Krebs Henseleit Buffer (KHB) supplemented with mannitol (18 mM) and pyruvate (2 mM).…”

Section: Glucose Transportmentioning

confidence: 99%

A role for calcium/calmodulin kinase in insulin stimulated glucose transport

et al. 2004

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Preliminary report: The effects of phospholipase C inhibition on insulin-stimulated glucose transport in skeletal muscle

Cited by 14 publications

References 0 publications

Exercise Ameliorates Insulin Resistance via Ca2+ Signals Distinct From Those of Insulin for GLUT4 Translocation in Skeletal Muscles

Exercise Ameliorates Insulin Resistance via Ca2+ Signals Distinct From Those of Insulin for GLUT4 Translocation in Skeletal Muscles

Specific protein kinase C isoforms as transducers and modulators of insulin signaling

A role for calcium/calmodulin kinase in insulin stimulated glucose transport

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