Related Experiment Video

Updated: Jun 22, 2026

Glycan Node Analysis: A Bottom-up Approach to Glycomics
11:36

Glycan Node Analysis: A Bottom-up Approach to Glycomics

Published on: May 22, 2016

Abnormal glycosylation of dystroglycan in human genetic disease

Jane E Hewitt1

  • 1Institute of Genetics, School of Biology, Queen's Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK. jane.hewitt@nottingham.ac.uk

Biochimica Et Biophysica Acta
|June 23, 2009
PubMed

Insights

Dystroglycanopathies are inherited muscular dystrophies caused by faulty alpha-dystroglycan glycosylation. This review covers six genes, their disease relevance, and animal models for studying these complex genetic disorders.

Area of Science:

  • Biochemistry
  • Genetics
  • Neurology

Background:

  • Dystroglycanopathies are inherited muscular dystrophies characterized by hypoglycosylation of alpha-dystroglycan.
  • These disorders often involve central nervous system and ocular defects.
  • Alpha-dystroglycan dysfunction is also implicated in cancer progression.

Purpose of the Study:

  • To review the six identified dystroglycanopathy genes.
  • To discuss their roles in alpha-dystroglycan glycosylation and human disease.
  • To present available animal models for dystroglycanopathy research.

Main Methods:

  • Literature review of dystroglycanopathy genes and associated research.
  • Analysis of known and proposed functions in glycosylation pathways.
  • Compilation of data on human disease manifestations and animal models.

Main Results:

  • Six genes linked to dystroglycanopathies have been identified.
  • These genes play critical roles in the glycosylation of alpha-dystroglycan.
  • Defects lead to muscular dystrophy and potentially other systemic issues.

Conclusions:

  • Understanding dystroglycan glycosylation is key to addressing these inherited disorders.
  • Further research into the identified genes and animal models will advance therapeutic strategies.
  • Dystroglycanopathies represent a significant area for genetic and neurological research.

More Related Videos

Live Imaging and Analysis of Muscle Contractions in Drosophila Embryo07:18

Live Imaging and Analysis of Muscle Contractions in Drosophila Embryo

Published on: July 9, 2019

Related Concept Videos

Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Inborn Errors of Metabolism01:20

Inborn Errors of Metabolism

Phenylketonuria (PKU) is a protein metabolism disorder characterized by high blood levels of the amino acid phenylalanine. This results from a mutation in the gene responsible for phenylalanine hydroxylase, an enzyme that converts phenylalanine into tyrosine. When this enzyme is deficient, phenylalanine builds up in the blood, leading to symptoms such as vomiting, rashes, seizures, growth deficiency, and severe mental retardation. An early diagnosis and a diet restricting phenylalanine intake...
Glucose Transporters01:27

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Lysosomal Hydrolases01:22

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...