Dataset Information

Rozi2003_GlycogenPhosphorylase_Activation

ABSTRACT: The model reproduces the temporal evolution of Glycogen phosphorylase for a vale of Vm5=30 as depicted in Fig 1a of the paper. The model makes use of calcium oscillations from the Borghans model to stimulate the activation of glycogen phosphorylase. Hence, this is a simple extension of the Borghans model. The model was succesfully tested on MathSBML and Jarnac. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

SUBMITTER: Harish Dharuri

PROVIDER: BIOMD0000000100 | BioModels | 2007-03-22

REPOSITORIES: BioModels

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Publications

A theoretical study of effects of cytosolic Ca2+ oscillations on activation of glycogen phosphorylase.

Rozi Anvar A Jia Ya Y

Biophysical chemistry 20031201 3

Taking into account the Ca(2+)-stimulated degradation of inositol 1,4,5-trisphosphate (IP(3)) by a 3-kinase, we have theoretically explored the effects of both simple and complex Ca(2+) oscillations on the regulation of a phosphorylation-dephosphorylation cycle process involved in glycogen degradation by glycogen phosphorylase a-form, respectively. For the case of simple Ca(2+) oscillations, the roles of cytosolic Ca(2+) oscillations in the regulation of active phosphorylase depend upon the maxi ...[more]

PMID: 14556891

Publication: 1/3

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Project description:The transcriptional coactivator peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1Î±) is a chief activator of the mitochondrial and metatolic program in skeletal muscle (skm) and prevents atrophy. Here we tested whether PGC-1Î± overexpression could restructure the transcriptome and metabolism of cultured human skeletal myotubes, which display an athropic phenotype. An oligonucleotide microarray analysis was used to reveal PGC-1Î± effects on the whole transcriptome, and the possible impact on fuel metabolism reprogramming was examined. Fifty-three different genes displayed changed expression levels in response to PGC-1Î±: 42 upregulated and 11 downregulated. Main associations of gene ontologies (GO) for the upregulated genes were mitochondrial components and processes and this correlated with an increase in COX activity, an indicator of mitochondrial content. Palmitate and lactate oxidation to CO2 was enhanced, but not glucose oxidation. The other most significant GO associations of upregulated genes were chemotaxis and cytokine activity, and accordingly, several cytokines, including IL8, CXCL6, CCL5 and CCL8, were within top induced genes. Among the most regulated genes were also potential metabolic regulators of fatty acid and glucose storage. FITM1/FIT1 induction was associated with an increased number of lipid droplets with smaller area, while triglyceride levels were modestly increased in oleate-incubated cells. Downregulation of CALM1, the calcium-modulated Î´ subunit of phosphorylase kinase, was linked to inactivation of glycogen phosphorylase and greater accumulation of glycogen. The most upregulated gene was PVALB, which is also related to calcium signaling. In conclusion, only the deficient mitochondrial transcriptional program of cultured myotubes is rescued by PGC-1Î±. New PGC-1Î± gene targets and pathways arise, some of which may mediate its activating effects in processes such as lipid and carbohydrate storage and angiogenesis. 6 samples from 3 different skeletal muscle cell cultures were used: 3 were transfected with adenovirus containing PGC-1aplha and 3 with adenovirus containing GFP (control). The 3 PGC-1alpha samples were compared against the control samples.

Dataset Information

Rozi2003_GlycogenPhosphorylase_Activation

Publications

A theoretical study of effects of cytosolic Ca2+ oscillations on activation of glycogen phosphorylase.

Similar Datasets

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