Related Experiment Video

Updated: Dec 23, 2025

In Vitro Enzyme Measurement to Test Pharmacological Chaperone Responsiveness in Fabry and Pompe Disease
10:16

In Vitro Enzyme Measurement to Test Pharmacological Chaperone Responsiveness in Fabry and Pompe Disease

Published on: December 20, 2017

8.4K

α-Mannosidosis - An underdiagnosed lysosomal storage disease in individuals with an 'MPS-like' phenotype

Thomas Wiesinger1, Markus Schwarz1, Thomas P Mechtler1

  • 1ARCHIMED Life Science GmbH, Leberstraße 20, 1110 Vienna, Austria.

Molecular Genetics and Metabolism
|April 26, 2020
PubMed

Insights

Alpha-Mannosidosis, an ultra-rare disease, shares symptoms with mucopolysaccharidoses (MPS). This study found an unexpectedly high number of alpha-Mannosidosis cases among individuals suspected of having MPS, highlighting the need for better diagnostic awareness.

Area of Science:

  • Biochemistry
  • Genetics
  • Rare Diseases

Background:

  • Alpha-Mannosidosis presents with symptoms overlapping mucopolysaccharidoses (MPS), including respiratory infections and skeletal changes.
  • It is an ultra-rare disorder with historically limited diagnostic testing.
  • Advancements in diagnostics, like tandem mass spectrometry on dried blood spots, offer new avenues for detection and understanding.

Purpose of the Study:

  • To investigate the prevalence of alpha-Mannosidosis in individuals suspected of having MPS.
  • To assess the utility of dried blood spot testing for diagnosing rare lysosomal storage disorders.

Main Methods:

  • Pilot study analyzing 1010 residual dried blood spot samples from individuals with suspected MPS.
  • Biochemical and genetic testing for alpha-mannosidases was performed.

Main Results:

  • 158 out of 1010 individuals were confirmed to have MPS.
  • Four individuals were diagnosed with alpha-Mannosidosis through confirmatory testing.
  • This represents a higher than anticipated prevalence in the studied cohort.

Conclusions:

  • The findings underscore the importance of considering alpha-Mannosidosis in the differential diagnosis of patients suspected of MPS.
  • Improved diagnostic strategies are crucial for identifying this ultra-rare condition.
  • Increased awareness and accessible testing can enhance disease understanding and patient care.
Keywords:
Dried blood spotsLysosomal storage diseaseMucopolysaccharidosisRare diseaseTandem mass spectrometryα-Mannosidosisα-mannosidase

More Related Videos

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

13.2K
Utility of Dissociated Intrinsic Hand Muscle Atrophy in the Diagnosis of Amyotrophic Lateral Sclerosis08:16

Utility of Dissociated Intrinsic Hand Muscle Atrophy in the Diagnosis of Amyotrophic Lateral Sclerosis

Published on: March 4, 2014

33.0K

Related Concept Videos

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,...
4.4K
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...
627
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...
3.4K
Overview of Protein Metabolism01:21

Overview of Protein Metabolism

Proteins are broken down into amino acids during digestion. Unlike fats and carbohydrates, which are stored for later use, proteins are not. Instead, amino acids are either used to produce ATP through oxidation or contribute to the creation of new proteins for the growth and repair of the body. Any surplus amino acids from the diet are converted into glucose or triglycerides rather than excreted.
Amino acids play various roles in the body once they are absorbed into cells. They are restructured...
3.4K
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,...
4.5K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
4.8K