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PPP1R3C, a novel hypermethylated gene in colorectal cancer, may play a critical role in cancer cell growth in association with glucose levels.
detection of methylation of PPP1R3C alone or in combination with EFHD1 (zeige EFHD1 Proteine) in plasma DNA showed high sensitivity and specificity in CRC (zeige CALR Proteine) detection, and may be useful detection method for CRC (zeige CALR Proteine), especially for early-stage CRCs.
Findings suggest that variations in PTG may condition the course of Lafora disease and establish PTG as a potential target for pharmacogenetic and therapeutic approaches.
Results demonstrated that HIF1 (zeige HIF1A Proteine) promotes glycogen (zeige GYS1 Proteine) accumulation through regulating PPP1R3C expression under hypoxia, which revealed a novel metabolic adaptation of cells to hypoxia.
phosphorylation of R5/PTG at Ser (zeige SIGLEC1 Proteine)-8 by AMPK (zeige PRKAA1 Proteine) accelerates its laforin (zeige EPM2A Proteine)/malin (zeige NHLRC1 Proteine)-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity.
metabolic crosstalk is due to decreased mTORC1 and SREBP activity in PTG (zeige LPCAT3 Proteine) knockout mice or knockdown cells, suggesting a positive feedback loop in which once accumulated, glycogen (zeige GYS1 Proteine) stimulates the mTORC1/SREBP1 (zeige SREBF1 Proteine) pathway to shift energy storage to lipogenesis.
removing PTG (zeige LPCAT3 Proteine), a glycogen (zeige GYS1 Proteine) synthesis activator protein, nearly completely eliminates Lafora bodies and rescues the neurodegeneration, myoclonus,seizure susceptibility, and behavioral abnormality.
Laforin (zeige EPM2A Proteine)-deficient mice lacking PTG (zeige LPCAT3 Proteine) have greatly decreased Lafora bodies and normal glycogen (zeige GYS1 Proteine) levels.
These data suggest that PTG (zeige LPCAT3 Proteine) plays a critical role in glycogen (zeige GYS1 Proteine) synthesis and is necessary to maintain the appropriate metabolic balance for the partitioning of fuel substrates between glycogen (zeige GYS1 Proteine) and lipid.
PTG (zeige LPCAT3 Proteine) overexpression in 3T3-L1 adipocytes discretely stimulates PP1 (zeige PPP1CC Proteine) activity against glycogen synthase and phosphorylase, resulting in a marked and specific increase in glucose uptake and storage as glycogen (zeige GYS1 Proteine).
These data indicate that disruption of PTG (zeige LPCAT3 Proteine) expression resulted in the uncoupling of PP1 (zeige PPP1CC Proteine) activity from glycogen (zeige GYS1 Proteine) metabolizing enzymes, the enhancement of glycogenolysis, and a dramatic decrease in cellular glycogen (zeige GYS1 Proteine) levels.
mouse protein targeting to glycogen (PTG) promoter is regulated by the FoxA2 (zeige FOXA2 Proteine) forkhead protein (zeige FOXO4 Proteine) and by 3',5'-cyclic adenosine 5'-monophosphate in H4IIE hepatoma cells
This gene encodes a regulatory subunit of protein phosphatase-1 (PP1). PP1 catalyzes reversible protein phosphorylation, which is important in a wide range of cellular activities: neuronal, muscular, RNA splicing, protein synthesis, cell death, and glycogen metabolism, to name just a few. By interacting with different regulatory subunits, PP1 is directed to different parts of the cell, to different substrates, or to respond to extracellular signals.
PP1 subunit R5
, Phosphatase 1, regulatory inhibitor subunit 5
, protein phosphatase 1 regulatory subunit 3C
, protein phosphatase 1 regulatory subunit 5
, protein phosphatase 1, regulatory (inhibitor) subunit 3C
, protein targeting to glycogen
, protein phosphatase 1 binding protein PTG
, protein phosphatase 1, regulatory (inhibitor) subunit 5
, protein targeting to glicogen
, protein phosphatase 1 regulatory subunit 3C-B