Related Experiment Video
Updated: May 26, 2026
08:51
Profiling of Permethylated Mucin O-glycans Using Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry
Published on: June 20, 2025
Source document verification in the Mucopolysaccharidosis Type I Registry.
Karien Verhulst1, Laura Artiles-Carloni, Michael Beck
1Genzyme Europe BV, Naarden, the Netherlands.
Pharmacoepidemiology and Drug Safety
|December 16, 2011
Summary
The Mucopolysaccharidosis Type I (MPS I) Registry shows high data accuracy, with error rates below 4% after source document verification. This confirms the reliability of this important registry for MPS I research.
Area of Science:
- Rare diseases
- Genetic disorders
- Data management in clinical research
Background:
- The Mucopolysaccharidosis Type I (MPS I) Registry collects natural history and treatment outcome data.
- Established post-laronidase approval, it's a voluntary, consent-based international observational database.
- Rigorous data checks include queries, monthly reviews, and electronic audits.
Purpose of the Study:
- To assess the overall data accuracy of the MPS I Registry.
- To validate the integrity of collected patient data through source document verification (SDV).
Main Methods:
- Two phases of source document verification (SDV) were conducted.
- Registry data were compared against source documents across European, Latin American, and North American sites.
- Key MPS I parameters were examined for randomly selected patients on laronidase therapy.
Main Results:
- Phase 1 showed a 2.7% source-to-database error rate (95% CI [2.2%, 3.5%]).
- Phase 2 indicated a 3.7% source-to-database error rate (95% CI [2.9%, 4.7%]).
- No systematic errors were identified in either phase.
Conclusions:
- The MPS I Registry demonstrates acceptable data accuracy for the assessed fields.
- Source document verification confirms the reliability of the registry data for MPS I research.
Related Concept Videos
01:22Lysosomal 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,...
01:24Oligosaccharide 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...
Multiple sugar molecules that may or may...
01:05Proteoglycans
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,...