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10/01/2018 · Glycogen Synthesis 2 ..

What may cause this higher Akt-mTOR-S6k signaling? IGF-1 and insulin are known activators of Akt-mTOR signaling , , , and Akt phosphorylation status was higher in postmortem rectus abdominis muscle biopsies of intensive insulin treated ICU patients compared with surgery patient controls , but no further downstream molecules were measured in that study. Since we in the present study show lower plasma IGF-1 and muscle IGF-1 mRNA in ICU patients (), neither systemic nor local IGF-1 could be the driving force in the activation of Akt-mTOR-S6k signaling. To further examine this question, we estimated the role of exogenous insulin by correlating insulin infusion dose at the time of the biopsy with Akt phosphorylated at T308, our most upstream target. We observed a moderate correlation () demonstrating responsiveness of Akt T308 phosphorylation in an insulin dose dependent fashion. Exogenous insulin dose may, however, be of limited value in the correlation with protein phosphorylation status, as ICU patients display signs of insulin resistance of varying degrees () , and insulin sensitivity apparently increases with insulin therapy in critical illness , . Accordingly, it is currently unclear if insulin therapy activates Akt-mTOR-S6k signaling in ICU patients under the present study conditions, and whether insulin induces muscle protein synthesis in critically ill ICU patients similar to what is seen in ICU burn patients .

opposite effect on glycogen synthesis

To estimate the role of exogenous insulin in the activation of the Akt-mTOR-S6k pathway, we correlated the insulin infusion dose at the time of the biopsy with phosphorylation of Akt at T308, which represents the upstream activation by 3-phosphoinositide dependent protein kinase 1 (PDK1). A moderate correlation (r2=0.36, p).

Glycogen Biosynthesis; Glycogen Breakdown - Oregon …

Glycogen Synthesis

The patients had high CRP and IL-6 levels and low serum albumin levels (), which are part of the suggested diagnostic criteria for cachexia , acknowledging that CRP and IL-6 mainly are markers of inflammation. Despite these indices on muscle wasting it has to be acknowledged that we do not know if our patients experienced an active muscle loss or more stable state of atrophy at the time of the biopsy. A more stable state of atrophy could fit with our surprising observations of stimulated protein synthesis pathways and somewhat inhibited protein degradation pathways. Indirect evidence for muscle atrophy is the finding of a good agreement between the atrogene profile observed in several murine muscle atrophy models and the transcriptional response of ICU patients similar to our patients , . On the other hand, the ICU patients under the present study conditions recapitulate a signaling pathway activity pattern, which in some animal models , , but not all , is related to the counteraction of disease-related muscle loss.

Finally, the posttranslational regulation of FoxO transcription factors by e.g. phosphorylation should be recognized as a main regulatory event that was not examined in the present study. We could not detect any total or phosphorylated FoxO proteins, which may be due to FoxO protein content below our detection limit, since low endogenous FoxO protein expression is present in mouse and rat muscle cell lines , , and rat skeletal muscle .

that result in protein phosphorylation or ..

Glycogen synthesis and breakdown Flashcards | Quizlet

To study the effect of metabolic inhibition of glycogen phosphorylase by CP-320626 on protein expression, we analyzed cellular protein expression using a newly established method . Protein expression profiles in MIA PaCa-2 cells treated with and without CP-320626 are shown in . Differentially expressed proteins in MIA cells treated with a hierarchical dose of CP-320626 were selected according to a criterion of the intensity of a spot in the gels showing less or greater than 2-fold difference (p, which showed that inhibition of glycogen phosphorylase by CP-320626 significantly affected dynamics of protein expression. Among twenty-two proteins identified, thirteen proteins were significantly suppressed and nine proteins were significantly enhanced ().

Data in figures are presented as individual values and means in scatter plots, whereas data in tables are means ± standard error of the mean (SEM). Muscle mRNA and protein data were log-transformed and are presented as individual values relative to control mean. Statistical differences between groups were determined using unpaired, two-tailed, unequal variance Welch's t-tests or for TNF-α mRNA Mann-Whitney U test. The relationship between insulin infusion dose and phosphorylated Akt was evaluated by linear regression analysis. This is biologically relevant as Akt is part of the canonical insulin-phosphatidylinositol 3-kinase (PI3K) signaling pathway . Results were considered significant when p

Glycogen Synthesis and Metabolism
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2. Glycogen Synthesis (PPT) Flashcards | Quizlet

Spots of interest were excised from the gels and transferred to Eppendorf LoBind tubes (Eppendorf, Hamburg, Germany). Gel pieces were destained with 100mM ammonium bicarbonate in 30% ACN until transparent and dried in a vacuum centrifuge as described by Jiang et al. . Proteins were proteolyzed with 25 ng of modified trypsin (Promega, Madison, WI) in 25 mM ammonium bicarbonate for 20 h or overnight at 37 °C. Supernatant was collected, and peptides were further extracted twice with 0.1% TFA, 60% ACN with vortexing for 45 min at room temperature. Peptides extracts were vacuum-dried.

-this is becoming a common theme for glycogen synthesis/breakdown ..

The synthesis rates of the differential proteins were calculated according to our in-house algorithms , . The synthesis rate of each protein is the average of three to four fragments. One-way ANOVA with the Tukey’s adjustment was used for multiple comparisons in SPSS 13.0 (SPSS Inc., Chicago, IL).

glycogen synthesis and breakdown ..

Five hundred micrograms of proteins were mixed with a rehydration solution containing 7 M urea, 2 M thiourea, 4% CHAPS, 50 mM DTT, 0.2% biolyte 3–10, 0.1% biolyte 4–6, and 0.1% biolyte 5–8, and a trace of bromophenol blue to a total volume of 300 μL. The mixtures were pipetted into IPG strip holder channels. After 14 h of rehydration, the strips were transferred to an isoelectric focusing (IEF) cell (Bio-Rad, Hercules, CA). Prefocusing and focusing were performed on a Protean IEF cell (500 V hold 2.5 h, linear 500–1000 V increase 1 h, 1000 V hold 1 h, linear 1000–8000V increase 1.5 h, and 8000 V hold 60,000 KV h). Following IEF separation, the equilibration was done by incubating with equilibration buffer I and II (37.5 mM Tris-Cl, pH 8.8, 20% glycerol, 2% SDS, 6 M urea, with 2% DTT in buffer I and 2.5% iodoacetamide in buffer II, respectively). The second dimension electrophoresis was run on 8–16% Tris-HCl gel in a Protean Plus Dodeca cell (Bio-Rad, Hercules, CA) until the bromophenol blue reached the bottom of the gels. After 2-DE, the gels were stained with SYPRO-Ruby (Molecular Probes, Eugene, OR) or visualized with the Coomassie Brilliant Blue R-250 (Merck, Germany). The phosphorylated proteins were stained with Pro-Q Diamond , . Following 2-DE and protein staining, gels were then scanned with a Pharox FX molecular imager (Bio-Rad, Hercules, CA) with a 532 nm laser excitation and a 580 nm band-pass emission filter. The differential protein spots were identified using PDQuest (8.1.0.0) 2-DE analysis software (Bio-Rad, Hercules, CA). The intensity of each protein spot was normalized to the total intensity of the entire gel image.

Glycogen synthesis and breakdown govern availability of ..

FoxO1 mRNA was 310% higher in ICU patients compared with controls (p left), whereas FoxO3 and 4 mRNA were 62 and 83% lower compared with controls (p middle and right). FoxO6 mRNA was below the detection limit. Unfortunately, we could not detect Foxo1, 3 and 4 proteins or any phosphorylation hereof. In ICU patients atrogin1 mRNA was 43% lower than controls (p left). MuRF1 mRNA was similar to controls (−16%, p=0.6, right), whereas MuRF1 protein was 44% lower compared with controls (p=0.05, ).

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