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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...
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Proteoglycans01:05

Proteoglycans

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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,...
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Protein Glycosylation

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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.
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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.
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Lesson: Translation
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Expanded Clinical Spectrum of Autosomal-Dominant STT3A-CDG.

Hamdan Al-Shahrani1, Evelin Szabó2, Caroline Staccone1

  • 1Department of Genetics and Genomic Sciences, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.

Biomolecules
|March 28, 2026
PubMed
Summary

Dominant STT3A-CDG, a distinct disorder from recessive forms, presents with varied symptoms including developmental delays and skeletal issues. New cases reveal additional features like obesity and bleeding disorders, expanding the known clinical spectrum.

Keywords:
STT3Acongenital disorder of glycosylationdominant-negativegenotype–phenotype correlationoligosaccharyltransferase

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Area of Science:

  • Biochemistry
  • Genetics
  • Clinical Medicine

Background:

  • The STT3A gene encodes the catalytic subunit of the oligosaccharyltransferase A (OST-A) complex.
  • Mutations in STT3A are classically associated with severe autosomal-recessive congenital disorder of glycosylation (CDG).
  • The distinct clinical features and inheritance pattern of autosomal-dominant STT3A-CDG remain incompletely defined.

Purpose of the Study:

  • To delineate the distinct clinical and biochemical characteristics of autosomal-dominant STT3A-CDG.
  • To integrate published data with new patient information to expand the understanding of the disorder's spectrum.
  • To investigate the genetic basis and mutational patterns in dominant STT3A-CDG.

Main Methods:

  • Systematic review of all published cases of dominant STT3A-CDG.
  • Integration of three previously unpublished individuals from a CDG natural history study.
  • Analysis of clinical phenotypes, biochemical signatures (transferrin glycosylation), and genetic variants.

Main Results:

  • Abnormal transferrin glycosylation (20/21) and facial dysmorphism (18/21) were common in 21 individuals.
  • Frequent neurodevelopmental (motor/speech delay, learning difficulties, intellectual disability) and musculoskeletal (skeletal abnormalities, short stature, osteoarthritis) issues were observed.
  • New cases revealed anorectal malformation, morbid obesity, and bleeding diathesis (von Willebrand factor/factor VIII deficiency), expanding the phenotype. Recurrent p.Arg405 variants suggest a mutational hotspot and dominant-negative mechanism.

Conclusions:

  • Dominant STT3A-CDG is a distinct entity with a broad clinical spectrum, including newly identified features.
  • Transferrin glycosylation patterns can be variable, and near-normal results do not exclude the diagnosis.
  • Genetic variants in conserved catalytic regions, particularly p.Arg405, are implicated in the dominant-negative mechanism of STT3A-CDG.