Liver Glycogenosis Research Articles

Mapping of the gene for X-linked liver glycogenosis due to phosphorylase kinase deficiency to human chromosome region Xp22

X-linked liver glycogenosis (XLG) is a glycogenosis due to deficient activity of phosphorylase kinase (PHK) in liver. PHK consists of four different subunits, α, β, γ, and δ. Although it is unknown whether liver and muscle PHK subunits are encoded by the same genes, the muscle α subunit (PHKA) gene was a likely candidate gene for the mutation responsible for this X-linked liver glycogenosis as it was assigned to the X chromosome at q12–q13. Linkage analysis with X-chromosomal polymorphic DNA markers was performed in two families segregating XLG. First, multipoint linkage analysis excluded the muscle PHKA region as the site of the XLG mutation. Second, evidence was obtained for linkage between the XLG locus and DXS197, DXS43, DXS16, and DXS9 with two-point peak lod scores Z max = 6.64, 3.75, 1.30, and 0.88, all at θ max = 0.00, respectively. Multipoint linkage results and analysis of recombinational events indicated that the mutation responsible for XLG is located in Xp22 between DXS143 and DXS41.

Families with X‐linked liver glycogenosis due to phosphorylase kinase deficiency

American Journal of Medical GeneticsVolume 37, Issue 3 p. 441-441 Letter to the Editor Families with X-linked liver glycogenosis due to phosphorylase kinase deficiency Patrick Willems, Patrick Willems Department of Medical Genetics, University of Antwerp Antwerp, BelgiumSearch for more papers by this author Patrick Willems, Patrick Willems Department of Medical Genetics, University of Antwerp Antwerp, BelgiumSearch for more papers by this author First published: November 1990 https://doi.org/10.1002/ajmg.1320370336Citations: 1AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article.Citing Literature Volume37, Issue3November 1990Pages 441-441 RelatedInformation

Families with X linked liver glycogenosis owing to phosphorylase kinase deficiency

Families with X linked liver glycogenosis owing to phosphorylase kinase deficiency

Families with X‐linked liver glycogenosis due to phosphorylase kinase deficiency

Clinical GeneticsVolume 38, Issue 1 p. 80-80 Families with X-linked liver glycogenosis due to phosphorylase kinase deficiency Patrick Willems MD, Corresponding Author Patrick Willems MDDepartment of Medical Genetics University of Antwerp - U.I.A. Universiteitsplein, 1 2610 Wilrijk/Antwerp Belgium Telephone: 32-3-8202584 Telefax: 32-3-8202248Search for more papers by this author Patrick Willems MD, Corresponding Author Patrick Willems MDDepartment of Medical Genetics University of Antwerp - U.I.A. Universiteitsplein, 1 2610 Wilrijk/Antwerp Belgium Telephone: 32-3-8202584 Telefax: 32-3-8202248Search for more papers by this author First published: July 1990 https://doi.org/10.1111/j.1399-0004.1990.tb03552.xCitations: 1AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article.Citing Literature Volume38, Issue1July 1990Pages 80-80 RelatedInformation

The natural history of liver glycogenosis due to phosphorylase kinase deficiency: A longitudinal study of 41 patients

We report a longitudinal study of 41 patients with liver glycogenosis due to phosphorylase kinase deficiency. In their youth, patients displayed hepatomegaly (92%), growth retardation (68%), delayed motor development (52%), hypercholesterolaemia (76%), hypertriglyceridaemia (70%), elevation of glutamate pyruvate transaminase (56%) and fasting hyperketosis (44%). With age, these clinical and biochemical abnormalities gradually disappeared and most adult patients were asymptomatic.

Effect of intravenous caffeine on liver glycogenosis during prolonged exercise

Ingestion of caffeine has been reported to enhance performance during prolonged endurance exercise. This effect on performance has been attributed to a caffeine-induced enhancement of lipid oxidation, thereby sparing muscle glycogen. The purpose of this experiment was to determine the effect of caffeine on the rate of liver glycogenolysis during exercise. Adult male rats were given an intravenous injection of caffeine (5 mg X kg-1) or of 0.9% NaCl. One h later they were run on a motor driven treadmill at 28 m X min-1 up a 15% grade for 45 or 90 min. Liver and muscles were frozen, and blood was collected for analysis. No significant differences were found between caffeine- and saline-injected rats in liver or muscle glycogen, plasma free fatty acid, insulin, glucagon, blood glucose, or blood glycerol. Liver adenosine 3',5'-cyclic monophosphate was essentially the same in caffeine- and saline-injected rats after 90 min of exercise. In a separate study, injection of 5 or 25 mg caffeine per kg body weight immediately prior to a 60-min bout of exercise had no effect on the rate of liver muscle glycogenolysis or on any of the hormones and metabolites studied. We conclude that in the rat, blood levels of caffeine in the range of 3.7 to 29 micrograms X ml-1 have no effect on liver adenosine 3',5'-cyclic monophosphate or the rate of liver glycogenolysis during prolonged treadmill running.

Ketosis in hepatic glycogenosis.

The occurrence of ketosis in 41 patients with liver glycogenosis and a control group of 22 children was investigated. Fasting ketosis was present in children with a deficiency of the debranching enzyme system and in young children with a deficiency of the phosphorylase system, but never in patients with a glucose-6-phosphatase deficiency. Oral tolerance tests on a patient deficient in debranching enzyme showed that the blood levels of glucose and ketone bodies changed in the opposite direction. It is argued that, for biochemical reasons, the occurrence of ketosis in patients with a glucose-6-phosphatase deficiency is improbable.

The inhibitory effect of sulphonylurea derivatives on liver glycogenolysis increased by catecholamines.

Abstract Hypoglycaemic sulphonylureas inhibit the increased glycogenosis and glucose release of the rat perfused liver produced by β-adrenergic agonists. The β-receptor antagonist propranolol exerted a similar effect. Dichloroisoprenaline increases the hypoglycaemic effect of chlorpropamide given in doses ineffective in the intact rat. Hypoglycaemic sulphonylureas have no effect on the catecholamine sensitivity of the nictitating membrane and heart auricle of the cat, indicating that their ability to inhibit glycogenosis induced by β-receptor agonists is not due to a β-receptor antagonist activity as is the action of propranolol.

HEXOSE AND PROTEIN TOLERANCE TESTS IN CHILDREN WITH LIVER GLYCOGENOSIS CAUSED BY A DEFICIENCY OF THE DEBRANCHING ENZYME SYSTEM

Galactose and fructose, administered orally to five children with liver glycogenosis due to deficiency of the debranching enzyme system, were found to be rapidly converted into glucose. A fluctuating glucose curve and a significant rise of blood lactate were observed during oral hexose challenge. Some proteins and amino acid mixtures, administered orally, induced a small and prolonged rise of blood glucose.

Liver phosphorylase: Deactivation in a child with progressive brain disease, increased hepatic glycogen and increased urinary catecholamines

Low activity of hepatic phosphorylase in a girl with degenerative disease of the brain increased to normal after the administration of either glucagon or epinephrine. Hepatic electron micrographs showed increased glycogen in a normal pattern and strikingly different from that in generalized glycogenosis. The surprising finding of a two- to eightfold increase in the excretion of urinary catecholamines led to the study of the effect of continuous epinephrine infusion in dogs. Their activities of liver phosphorylase responded with an initial increase and then with a decline to pre-infusion values or below. Reserpine administered to the child produced a maximal rise in urinary catecholamines which was followed by the lowest phosphorylase measurement recorded. The patient's low activity of hepatic phosphorylase did not seem to be the consequence of a deficiency in this enzyme, or of any of the enzymes involved in the phosphorylase system, since proper hormonal activation could be obtained. The low activity might be the expression of a deranged control over the degree of activation of liver phosphorylase. The resulting liver glycogenosis seems unimportant clinically. The implication of a defective control mechanism, however, might have significance in view of the deterioration of the patient's central nervous system. A recent biopsy of the patient's brain disclosed increased glycogen of unusual electron microscopic appearance [14].

Glycogen stores in glucagon-treated rats. I. Time factors.

1. Effects of epinephrine and various doses of glucagon on liver and muscle glycogen and on adrenal ascorbic acid were studied. 2. Twenty minutes after injection of epinephrine a decrease in liver and muscle glycogen, and in adrenal ascorbic acid were observed. Two hours after injection, liver glycogen was significantly higher than in controls, while muscle glycogen and adrenal ascorbic acid were still below normal. 3. Glucagon caused immediate decrease in liver glycogen. When large doses were used this decrease was followed by secondary increase to values greater than normal. 4. The glycostatic effect of large doses of glucagon in the liver was probably associated with an earlier decrease in adrenal ascorbic acid. 5. Glucagon caused an occasional slight increase of muscle glycogen. 6. It is suggested that the primary effect of epinephrine and of glucagon in all doses is an acceleration of liver glycogenosis and that their glycostatic effects are due to secondary increases in secretion of insulin and/or adrenal cortical hormones.