Disease relevance of LOC503698

• The width of cell layers surviving the infarction was measured and their viability after 60 minutes of coronary reocclusion was assessed by intracellular glycogen staining [1].
• Morphologically, clumping of the nuclear chromatin, mitochondrial swelling and decrease in glycogen were milder in V group at 20 min ischemia [2].
• No differences were noted in diaphragmatic muscle tissue ATP, phosphocreatine, or glycogen between control and IRL animals or between control and IRL plus hypoxemia animals [3].
• On cultured Zajdela hepatoma cells (ZHC cells), P95 Ab also mimicked insulin action on the incorporation of [U-14C]glucose into glycogen (158 and 207% of the control value for antibody- and insulin-treated cells, respectively) [4].
• It is possible that the chlamydiae seen ultrastructurally within intracytoplasmic vacuoles containing glycogen in conjunctival cells were Chlamydia trachomatis [5].

High impact information on LOC503698

• The PICM-19 cells contained large oval nuclei, numerous oval to elongate mitochondria with flat cristae, extensive rough and smooth endoplasmic reticulum, Golgi complexes, lipid vacuoles, and glycogen granules [6].
• The oxfenicine group had significantly lower lactate output integrals (1.11+/-0.23 vs. 0.60+/-0.11 mmol) and glycogen depletion (66+/-6 vs. 43+/-8%), and higher anterior wall power index (0.95+/-0.17 vs. 1.30+/-0.11%) and anterior wall energy efficiency index (91+/-17 vs. 129+/-10%) [7].
• Regulation of glycogen utilization, but not glucose utilization, by precontraction glycogen levels in vascular smooth muscle [8].
• Prior to and after isometric contraction, measurements were made of tissue glycogen content and superfusate glucose and lactate concentrations [8].
• These experiments were designed to determine whether glycogenolysis was influenced by the glycogen concentration of vascular smooth muscle [8].

Chemical compound and disease context of LOC503698

• In conclusion, this novel mechanistic model effectively predicted the rapid activation of glycogen breakdown and lactate production at the onset of ischemia and supports the concept of localization of glycolysis to a subdomain of the cytosol [9].
• Incubation at hypoxia resulted in increased lactate concentrations, whereas ATP, glucose, and glycogen concentrations were decreased, especially in the mid media, where concentrations of these metabolites were close to zero [10].

Biological context of LOC503698

• The extent of glycogen utilization during a 3 h isometric contraction varied linearly with the precontraction glycogen concentration (R2 = 0.727) [8].
• It is concluded that the rate of glycogenolysis is determined by the content of glycogen during prolonged contractions [8].
• The addition of a subdomain for glycolysis resulted in simulations showing faster rates of glycogen breakdown and lactate production that closely matched in vivo experimental data [9].
• This indicated that, in control conditions, glycosyl units from glycogen sustain cellular metabolism, and hence 3H-2-deoxyglucose phosphorylation [11].
• Muscle glycogen content increased (P less than .01) from 70 to 110 d of gestation [12].

Anatomical context of LOC503698

• Segments of hog carotid artery smooth muscle were allowed to synthesize variable amounts of 1-[13C]glucosyl units of glycogen [8].
• The naturally occurring R225Q mutation in the gamma3-subunit in pigs is associated with abnormally high glycogen content in skeletal muscle [13].
• Scanning electron microscopy revealed flattening of Clara cells in the terminal bronchioles of HFJV animals due to loss of glycogen and secretory granules [14].
• In addition, exercise-induced increases in glucose uptake for the hindlimbs (133%) and glucose incorporation into glycogen for the plantaris (8.4-fold), extensor digitorum longus (5.4-fold), and white gastrocnemius (4.8-fold) muscles were greater for the SUS-E rats than for the CC-E rats (39% and 1.9-, 1.9-, and 3.0-fold, respectively) [15].
• The outer hair cells were found to contain strongly stained particles which, presumably, consisted of glycogen [16].

Associations of LOC503698 with chemical compounds

• In addition, precontraction glycogen levels influence the pathway for glycogen utilization but not the pathway for glucose utilization [8].
• In the continual absence of glucose, glycogen content decreased with time and this decrease was slowed by 36% in the presence of iodoacetate [11].
• Diaphragmatic muscle samples were obtained after study completion and immediately frozen in liquid nitrogen for determination of tissue ATP, phosphocreatine, lactate, and glycogen levels [3].
• Phosphorylase limit dextrin from glycogen is debranched by cooperation of the two activities [17].
• However, no difference in the activities of glycogen phosphorylase and pyruvate kinase, rate-controlling enzymes in glycogenolysis and glycolysis, respectively, was detected between PSE and normal pork loins [18].

Other interactions of LOC503698

• A dominant mutation, denoted RN(-), in the porcine PRKAG3 gene, encoding the regulatory gamma3 subunit of AMPK, results in hyperaccumulation of glycogen in glycolytic skeletal muscle cells [19].
• Cells, once enzymatically isolated and purified, were identified by morphological criteria, positive vimentin immunoreactivity, and histochemical staining for glycogen [11].
• Growth hormone injections resulted in a diabetogenic state in gestating sows and led to improved traits related to baby pig blood glucose homeostasis, including increased blood glucose, increased body lipids and a tendency toward increased liver glycogen concentrations [20].
• The major finding of the proteome analysis was that the key enzyme in the synthesis of glycogen, UDP-glucose pyrophosphorylase, was significantly up-regulated in RN(-) carriers [19].

Analytical, diagnostic and therapeutic context of LOC503698

• Effect of hypophysectomy on tissue glycogen concentrations in the fetal pig [21].
• Measurements of tissue levels of high energy phosphates and glycogen utilization indicated a higher metabolic requirement in guinea pig than in rat hearts in order to oppose the hypothermia-induced calcium load [22].
• Electron microscopy revealed vacuolated sarcoplasmic reticula, enlarged lipid droplets, decreased glycogen and mitochondrial abnormalities in the skeletal muscle samples from the ethanol-exposed newborn guinea pigs [23].
• Improvements in glycogen protection and faster restoration of aerobic metabolism during preservation and reperfusion time seem to be necessary in order to improve liver preservation protocols per se [24].

References