5′-AMP-Activated protein kinase in avian biology

Proszkowiec‐Weglarz, Monika; Richards, Mark

doi:10.3184/147020607x314294

Cited by 10 publications

(14 citation statements)

References 92 publications

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“…This indicates a developmental pattern for expression of the AMPK γ-3 subunit. In fact, we observed that the mRNA expression of γ-3 increased by 48 h posthatch, and from this point forward, it became the predominant AMPK γ subunit expressed by the breast muscle in chickens (Proszkowiec-Weglarz and Richards, 2007). However, in the heart, no dramatic increase in γ-3 subunit expression occurred posthatch as observed in the breast muscle.…”

Section: Discussionmentioning

confidence: 43%

“…However, very few of these studies have involved embryos or embryonic cells at different stages of development. Although there have been several recent reports of the expression of LKB1 and AMPK in chicken tissues and cultured cells (for references, see Proszkowiec-Weglarz and Richards, 2007), there have been no reports concerning the occurrence or functioning of this important energy-responsive regulatory pathway in the developing avian embryo. Therefore, the objective of this study was to characterize the expression of the AMPK pathway in selected tissues from chicken embryos during the latter half of incubation and at hatch.…”

Section: Introductionmentioning

confidence: 97%

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Expression and activity of the 5′-adenosine monophosphate-activated protein kinase pathway in selected tissues during chicken embryonic development

Proszkowiec‐Weglarz

Richards

2009

Poultry Science

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The 5'-adenosine monophosphate-activated protein kinase (AMPK) is a highly conserved serine-threonine protein kinase and a key part of a kinase-signaling cascade that senses cellular energy status (adenosine monophosphate:adenosine triphosphate ratio) and acts to maintain energy homeostasis by coordinately regulating energy-consuming and energy-generating metabolic pathways. The objective of this study was to investigate aspects of the AMPK pathway in the liver, brain, breast muscle, and heart from d 12 of incubation through hatch in chickens. We first determined mRNA and protein expression profiles for a major upstream AMPK kinase, LKB1, which is known to activate (phosphorylate) AMPK in response to increases in the adenosine monophosphate:adenosine triphosphate ratio. Expression of LKB1 protein was greatest in the brain, which demonstrated tissue-specific patterns for phosphorylation. Next, AMPK subunit mRNA and protein expression profiles were determined. Significant changes in AMPK subunit mRNA expression occurred in all tissues from d 12 of incubation to hatch. Differences in the levels of active (phosphorylated) AMPK as well as alpha and beta subunit proteins were observed in all 4 tissues during embryonic development. Finally, we determined the protein level and phosphorylation status of an important downstream target for AMPK, acetyl-coenzyme A carboxylase. The expression of acetyl-co-enzyme A carboxylase and phosphorylated acetyl-coenzyme A was greater in the brain than the liver, but was undetectable by Western blotting in the breast muscle and heart throughout the period of study. Together, our results are the first to demonstrate the expression and activity of the AMPK pathway in key tissues during the transition from embryonic to posthatch development in chickens.

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Section: Discussionmentioning

confidence: 43%

Section: Introductionmentioning

confidence: 97%

Expression and activity of the 5′-adenosine monophosphate-activated protein kinase pathway in selected tissues during chicken embryonic development

Proszkowiec‐Weglarz

Richards

2009

Poultry Science

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“…A subset of AMPK-associated phosphorylation events were found to be significantly altered over the time course of the study. This enzyme functions as part of the energy homeostasis system in cells [13]. AMPK is activated by increased levels of AMP, which is a signal of low energy levels in the cell.…”

Section: Resultsmentioning

confidence: 99%

“…The 5'-adenosine monophosphate-activated protein kinase (AMPK) enzyme is a key metabolic energy homeostasis regulator in avian species [13]. One of its roles is to monitor the ratio of AMP:ATP and alter metabolic processes accordingly.…”

Section: Introductionmentioning

confidence: 99%

Salmonella enterica Typhimurium infection causes metabolic changes in chicken muscle involving AMPK, fatty acid and insulin/mTOR signaling

Arsenault

Napper

Kogut

2013

Vet Res

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Salmonella enterica serovar Typhimurium (Salmonella Typhimurium) infection of chickens that are more than a few days old results in asymptomatic cecal colonization with persistent shedding of bacteria. We hypothesized that while the bacterium colonizes and persists locally in the cecum it has systemic effects, including changes to metabolic pathways of skeletal muscle, influencing the physiology of the avian host. Using species-specific peptide arrays to perform kinome analysis on metabolic signaling pathways in skeletal muscle of Salmonella Typhimurium infected chickens, we have observed key metabolic changes that affected fatty acid and glucose metabolism through the 5'-adenosine monophosphate-activated protein kinase (AMPK) and the insulin/mammalian target of rapamycin (mTOR) signaling pathway. Over a three week time course of infection, we observed changes in the phosphorylation state of the AMPK protein, and proteins up and down the pathway. In addition, changes to a large subset of the protein intermediates of the insulin/mTOR pathway in the skeletal muscle were altered by infection. These changes occur in pathways with direct effects on fatty acid and glucose metabolism. This is the first report of significant cellular metabolic changes occurring systemically in chicken due to a Salmonella infection. These results have implications not only for animal production and health but also for the understanding of how Salmonella infection in the intestine can have widespread, systemic effects on the metabolism of chickens without disease-like symptoms.

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“…RNA polymerase II polypeptide E (POLR2E) was used as a housekeeping gene (Table1). We measured the mRNA levels of AMPK subunits 1, 2 and 1 in liver and of AMPK subunits 2, 2 and 3 in skeletal muscle, because these genes are expressed predominantly in those tissues, respectively (Proszkowiec-Weglarz and Richards, 2007;Proszkowiec-Weglarz and Richards, 2009). Real-time PCR reactions with dual-labelled probes contained 1ϫImmomix (Bioline, London, UK), 4.5mmoll -1 MgCl 2 , 50-900nmoll -1 primer and probe, 1ϫROX reference dye (Invitrogen, USA), and ~50ng cDNA.…”

Section: Mrna Concentrationsmentioning

confidence: 99%

AMP-activated protein kinase controls metabolism and heat production during embryonic development in birds

Walter

Hegarty

Seebacher

2010

Journal of Experimental Biology

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SUMMARYDuring embryonic and early juvenile development, endotherms must balance energy allocation between growth and heat production. Failure to either match the ATP demand of growing tissue or produce heat at the correct developmental stage will lead to damage of the organism. We tested the hypothesis that AMP-activated protein kinase (AMPK) is involved in the regulation of energy metabolism and heat production during development in the chicken (Gallus gallus). We show that mRNA concentrations of regulatory and catalytic AMPK subunits, AMPK total protein, and AMPK phosphorylation increase during development [3days (-3days) and one day (-1day) before hatching, and +1day and +8days after hatching] in liver, and to a lesser extent in skeletal muscle. Chronic stimulation with 5-aminoimidazole-4-carboxamide-1--D-ribofuranoside (AICAR) significantly increases AMPK phosphorylation in skeletal muscle and in liver. This increase was paralleled by significant increases in heat production, glucose utilization, and liver and skeletal muscle mitochondrial capacity (citrate synthase activity). The effects of AMPK are likely to be mediated by inhibition of acetyl CoA carboxylase (ACC) after hatching, when ACC protein concentration increases significantly, and by a significant AMPK-induced increase in PGC-1 mRNA concentration (at +1day), but not in NRF-1 mRNA concentration. AMPK phosphorylation is under the control of thyroid hormone, and AMPK phosphorylation decreases significantly following the induction of hypothyroidism. We propose AMPK as a principal regulatory mechanism during the transition from ectothermy to endothermy in birds, and show that AMPK function in birds is similar to that observed in mammals.

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5′-AMP-Activated protein kinase in avian biology

Cited by 10 publications

References 92 publications

Expression and activity of the 5′-adenosine monophosphate-activated protein kinase pathway in selected tissues during chicken embryonic development

Expression and activity of the 5′-adenosine monophosphate-activated protein kinase pathway in selected tissues during chicken embryonic development

Salmonella enterica Typhimurium infection causes metabolic changes in chicken muscle involving AMPK, fatty acid and insulin/mTOR signaling

AMP-activated protein kinase controls metabolism and heat production during embryonic development in birds

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