glycogen and Disease

Reversible protein phosphorylation is an important mode of regulation of cellular processes. While earlier studies focused on protein kinases, it is now apparent that protein phosphatases play an equally integral role in the control of cellular phosphoproteins. This review examines the role played by endogenous inhibitors of three major protein serine/threonine phosphatases, PP1, PP2A and PP2B in the control of cell physiology. The discussion highlights novel paradigms for signal transduction by protein phosphatase inhibitors that provide important avenues for signal amplification, the timing of physiological responses and cross-talk between distinct signal transduction pathways. New evidence also points to genetic abnormalities or altered expression of phosphatase inhibitors as potential mechanisms for human disease.Together, the data emphasize the physiological importance of protein phosphatase inhibitors and establish phosphatase regulation as a key feature of hormone signaling.

Topics: Animals; Calcineurin; Calcineurin Inhibitors; Carrier Proteins; Cell Division; Disease; Dopamine and cAMP-Regulated Phosphoprotein 32; Endoribonucleases; Enzyme Inhibitors; Glycogen; Humans; Intracellular Signaling Peptides and Proteins; Muscle Contraction; Nerve Tissue Proteins; Neuronal Plasticity; Phosphoprotein Phosphatases; Phosphoproteins; Phosphorylation; Proteins; RNA-Binding Proteins

Two formulas were derived to estimate the energy content of the human body which use only body mass, total body water by 3H2O dilution space and body minerals assessed by anthropometry. The formulas were tested in a body composition database of 561 patients and 151 normal volunteers using established metabolizable energy values for protein, fat and glycogen. Total body protein was determined by in vivo neutron activation analysis (IVNAA), body water by dilution of tritium and body minerals from skeletal frame size. Body glycogen was assumed to be 14.6% of the mineral component. Body fat was obtained by difference, body mass less the sum of water, protein, minerals and glycogen. The standard deviation in the estimate of body energy content was 30 MJ or 4.1% of the energy content of reference man. Two formulas for body energy content were derived by regression with body mass, total body water and body minerals or height. Two formulas for energy density and formulas for percentage body fat were similarly derived.

Topics: Adolescent; Adult; Aged; Aged, 80 and over; Body Composition; Body Water; Body Weight; Disease; Energy Metabolism; Female; Glycogen; Humans; Lipid Metabolism; Male; Middle Aged; Minerals; Proteins; Regression Analysis

Changes in hepatic and muscle high-energy phosphates in varying degrees of resting hypermetabolism were studied. Fourteen severely injured and five critically ill patients with normal blood pressure were investigated: the results were compared with 14 normal controls. ATP and ADP levels in the muscle were significantly changed in acutely severe injury: lactate and pyruvate levels in the liver and muscle increased; glycogen level in the liver decreased. Meanwhile, high-energy phosphates in both liver and muscle were not significantly changed in ongoing severe injury. Lactate level increased and glycogen level decreased in both tissues. In critical illness, hepatic and muscle ATP and ADP decreased significantly. The energy charge potential dropped. AMP, lactate, and the lactate-to-pyruvate ratio increased. Hepatic, but not muscle, glycogen dropped markedly. The correlation coefficient between hepatic and muscle ATP was 0.61; between hepatic ATP and hepatic glycogen was 0.60. Alteration in the ATP-ADP-AMP system in the liver and muscle suggests a low-energy charge in acute, severe injury and critical illness. This indicates a decreased capacity for biosynthetic reactions and production of storage compounds. The changes in high-energy phosphate in the liver always paralleled similar changes in muscle.

Topics: Adult; Aged; Amino Acids; Disease; Energy Metabolism; Female; Glycogen; Humans; Lactates; Liver; Male; Middle Aged; Muscles; Phosphates; Pyruvates; Wounds and Injuries

Topics: Cardiomyopathies; Disease; Glycogen; Glycogen Storage Disease; Heart Diseases; Heart Ventricles; Humans; Myocardium

Topics: Blood Glucose; Blood Proteins; Cattle Diseases; Disease; Fetal Diseases; Fetus; Glycogen; Glycogenolysis; Lactates; Pituitary Gland; Pituitary Gland, Anterior; Pyruvates

Topics: Disease; Female; Glycogen; Humans; Vomiting; Vulvar Lichen Sclerosus

Topics: Carbohydrate Metabolism; Disease; Glucose; Glycogen; Humans; Intestinal Absorption; Intestines; Muscles; Muscular Diseases

Topics: Disease; Diuretics; Glycogen; Kidney; Mersalyl; Organomercury Compounds; Pancreas; Pancreatic Diseases

Topics: Disease; Glycogen; Glycogenolysis; Hemoglobinuria; Humans; Muscles; Muscular Diseases; Myoglobinuria

Topics: Disease; Glycogen; Humans; Pancreas; Pancreatic Diseases

Topics: Animals; Disease; Glycogen; Glycogen Phosphorylase, Muscle Form; Mice; Muscle, Skeletal; Muscles; Muscular Diseases; Phosphorylases

Topics: Disease; Endometrial Hyperplasia; Endometrium; Female; Glycogen; Glycogenolysis; Humans; Uterine Diseases

Topics: Disease; Glycogen; Glycogen Storage Disease; Humans; Muscle, Skeletal; Muscles; Muscular Diseases

Topics: Disease; Glycogen; Hydrogen-Ion Concentration; Periodontal Diseases; Periodontal Pocket; Periodontium

Topics: Disease; Glycogen; Glycogen Storage Disease; Humans; Liver; Muscle, Skeletal; Muscles; Muscular Diseases

Topics: Disease; Glycogen; Glycogen Storage Disease; Humans; Muscle, Skeletal; Muscles; Muscular Diseases; Neuromuscular Diseases

Topics: Adenocarcinoma; Disease; Endometrium; Female; Glycogen; Humans; Hyperplasia; Uterine Neoplasms