Genetic defects of glycogen metabolism and its control

F. Huijing

Research output: Contribution to journalArticle

Abstract

Genetic defects of glycogen metabolism are known in man, dog, mouse and in bacteria. In 2 of the human glycogen storage diseases the symptoms are related to the glycogen accumulation itself (lysosomal α glucosidase and branching enzyme deficiency). All other human glycogen diseases are primarily triggered by a shortage of glucose or glycolytic intermediates (deficiencies of glucose 6 phosphatase liver or muscle phosphorylase, phosphorylase kinase or debranching enzyme). Three of the defects should in fact be considered inborn errors in control of metabolism, since they are not defects of enzymes of glycogen metabolism itself. These defects are deficiency of phosphorylase kinase, glucose 6 phosphatase and phosphofructokinase. In the latter 2 the glycogen accumulation is secondary and caused by increased availability of substrate (glucose 1 phosphate) as well as stimulatory action of elevated glucose 6 phosphate concentrations on the glycogen synthase system. Phosphorylase kinase deficiency may be caused by an increase of the Km of the enzyme for its macromolecular substrate or by a decrease in the total amount of enzyme present. A large proportion of heterozygotes of this X linked deficiency show some signs of their defect especially at an early age.

Original languageEnglish
Pages (from-to)290-302
Number of pages13
JournalAnnals of the New York Academy of Sciences
VolumeVol. 210
StatePublished - Dec 1 1973
Externally publishedYes

Fingerprint

Glycogen
Metabolism
Phosphorylase Kinase
Defects
Enzymes
Glucose-6-Phosphatase
Glycogen Storage Disease Type I
1,4-alpha-Glucan Branching Enzyme
Phosphofructokinase-1
Glucosidases
Glycogen Storage Disease
Glycogen Synthase
Phosphorylases
Glucose-6-Phosphate
Phosphofructokinases
Heterozygote
Substrates
Liver
Muscle
Dogs

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Genetic defects of glycogen metabolism and its control. / Huijing, F.

In: Annals of the New York Academy of Sciences, Vol. Vol. 210, 01.12.1973, p. 290-302.

Research output: Contribution to journalArticle

@article{555a7fe8a4b44533944f58bdd5ac1092,
title = "Genetic defects of glycogen metabolism and its control",
abstract = "Genetic defects of glycogen metabolism are known in man, dog, mouse and in bacteria. In 2 of the human glycogen storage diseases the symptoms are related to the glycogen accumulation itself (lysosomal α glucosidase and branching enzyme deficiency). All other human glycogen diseases are primarily triggered by a shortage of glucose or glycolytic intermediates (deficiencies of glucose 6 phosphatase liver or muscle phosphorylase, phosphorylase kinase or debranching enzyme). Three of the defects should in fact be considered inborn errors in control of metabolism, since they are not defects of enzymes of glycogen metabolism itself. These defects are deficiency of phosphorylase kinase, glucose 6 phosphatase and phosphofructokinase. In the latter 2 the glycogen accumulation is secondary and caused by increased availability of substrate (glucose 1 phosphate) as well as stimulatory action of elevated glucose 6 phosphate concentrations on the glycogen synthase system. Phosphorylase kinase deficiency may be caused by an increase of the Km of the enzyme for its macromolecular substrate or by a decrease in the total amount of enzyme present. A large proportion of heterozygotes of this X linked deficiency show some signs of their defect especially at an early age.",
author = "F. Huijing",
year = "1973",
month = "12",
day = "1",
language = "English",
volume = "Vol. 210",
pages = "290--302",
journal = "Annals of the New York Academy of Sciences",
issn = "0077-8923",
publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Genetic defects of glycogen metabolism and its control

AU - Huijing, F.

PY - 1973/12/1

Y1 - 1973/12/1

N2 - Genetic defects of glycogen metabolism are known in man, dog, mouse and in bacteria. In 2 of the human glycogen storage diseases the symptoms are related to the glycogen accumulation itself (lysosomal α glucosidase and branching enzyme deficiency). All other human glycogen diseases are primarily triggered by a shortage of glucose or glycolytic intermediates (deficiencies of glucose 6 phosphatase liver or muscle phosphorylase, phosphorylase kinase or debranching enzyme). Three of the defects should in fact be considered inborn errors in control of metabolism, since they are not defects of enzymes of glycogen metabolism itself. These defects are deficiency of phosphorylase kinase, glucose 6 phosphatase and phosphofructokinase. In the latter 2 the glycogen accumulation is secondary and caused by increased availability of substrate (glucose 1 phosphate) as well as stimulatory action of elevated glucose 6 phosphate concentrations on the glycogen synthase system. Phosphorylase kinase deficiency may be caused by an increase of the Km of the enzyme for its macromolecular substrate or by a decrease in the total amount of enzyme present. A large proportion of heterozygotes of this X linked deficiency show some signs of their defect especially at an early age.

AB - Genetic defects of glycogen metabolism are known in man, dog, mouse and in bacteria. In 2 of the human glycogen storage diseases the symptoms are related to the glycogen accumulation itself (lysosomal α glucosidase and branching enzyme deficiency). All other human glycogen diseases are primarily triggered by a shortage of glucose or glycolytic intermediates (deficiencies of glucose 6 phosphatase liver or muscle phosphorylase, phosphorylase kinase or debranching enzyme). Three of the defects should in fact be considered inborn errors in control of metabolism, since they are not defects of enzymes of glycogen metabolism itself. These defects are deficiency of phosphorylase kinase, glucose 6 phosphatase and phosphofructokinase. In the latter 2 the glycogen accumulation is secondary and caused by increased availability of substrate (glucose 1 phosphate) as well as stimulatory action of elevated glucose 6 phosphate concentrations on the glycogen synthase system. Phosphorylase kinase deficiency may be caused by an increase of the Km of the enzyme for its macromolecular substrate or by a decrease in the total amount of enzyme present. A large proportion of heterozygotes of this X linked deficiency show some signs of their defect especially at an early age.

UR - http://www.scopus.com/inward/record.url?scp=0015782153&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0015782153&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0015782153

VL - Vol. 210

SP - 290

EP - 302

JO - Annals of the New York Academy of Sciences

JF - Annals of the New York Academy of Sciences

SN - 0077-8923

ER -