Screening and diagnosis of congenital disorders of glycosylation

Marklová, E; Albahri, Ziad

doi:10.1016/j.cca.2007.07.002

Cited by 72 publications

(61 citation statements)

References 133 publications

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“…However, transferrin does not detect all N-glycosylation defects (3) and does not pinpoint the defective gene (4). More important, there is currently no corresponding indicator of reduced glycosylation in patient cells.…”

Section: Congenital Disorders Of Glycosylation (Cdg)mentioning

confidence: 99%

Identification of Intercellular Cell Adhesion Molecule 1 (ICAM-1) as a Hypoglycosylation Marker in Congenital Disorders of Glycosylation Cells

He¹,

Ng²,

Losfeld³

et al. 2012

Journal of Biological Chemistry

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Section: Congenital Disorders Of Glycosylation (Cdg)mentioning

confidence: 99%

Identification of Intercellular Cell Adhesion Molecule 1 (ICAM-1) as a Hypoglycosylation Marker in Congenital Disorders of Glycosylation Cells

He¹,

Ng²,

Losfeld³

et al. 2012

Journal of Biological Chemistry

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“…and human disease states (e.g., cancer; congenital disorders of glycosylation; neurodegenerative disorders, etc.). [6][7][8][9][10][11][12][13][14][15][16][17] While protein glycosylation analyses are oen carried out with either a "glycocentric" (i.e., compositional and structural analysis of glycans released from glycoproteins) or a "proteocentric" (i.e., identication of deglycosylated glycoproteins with indirect glycosylation site localization) outlook, the loss of molecular detail imposed by glycan release limits the specicity and potential for biological resolution that can be furnished by such analyses. 18 In order to map specic oligosaccharide structures to their corresponding sites of protein attachment, the analytical scheme must preserve the oligosaccharide-polypeptide connectivity until such a time that the chosen approach can characterize the linkage.…”

Section: Introductionmentioning

confidence: 99%

Energy-resolved collision-induced dissociation pathways of model N-linked glycopeptides: implications for capturing glycan connectivity and peptide sequence in a single experiment

Kolli

Dodds

2014

Analyst

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"Energy-resolved collision-induced dissociation pathways of model N-linked glycopeptides: implications for capturing glycan connectivity and peptide sequence in a single experiment" (2014). Faculty Publications --Chemistry Department. 68. http://digitalcommons.unl.edu/chemfacpub/68Energy-resolved collision-induced dissociation pathways of model N-linked glycopeptides: implications for capturing glycan connectivity and peptide sequence in a single experiment † Venkata Kolli and Eric D. Dodds * Tandem mass spectrometry (MS/MS) of glycopeptides stands among the principal analytical approaches for assessing protein glycosylation in a site-specific manner. The aims of such experiments are often to determine the monosaccharide connectivity of the glycan, the amino acid sequence of the peptide, and the site of glycan attachment. This level of detail is often difficult to achieve using any single ion dissociation method; however, precedent does exist for use of collision-induced dissociation (CID) to establish either the connectivity of the oligosaccharide or the sequence of the polypeptide depending upon the applied collision energy. Unfortunately, the relative energy requirements for glycan and peptide cleavage have not been thoroughly characterized with respect to specific physicochemical characteristics of the precursor ions. This report describes case studies on the energy-resolved CID pathways of model tryptic glycopeptides derived from Erythrina cristagalli lectin and bovine ribonuclease B. While glycopeptide ions having disparate physical and chemical characteristics shared strikingly similar qualitative responses to increasing vibrational energy deposition, the absolute collision energies at which either glycan or peptide fragmentations were accessed varied substantially among the precursor ions examined. Nevertheless, these data suggest that the energy requirements for peptide and glycan cleavage may be somewhat predictable based on characteristics of the precursor ion. The practical usefulness of these observations was demonstrated through implementation of online collision energy modulation such that both glycan and peptide fragmentation were captured in the same spectrum, providing near-exhaustive glycopeptide characterization in a single experiment. Overall, these results highlight the potential to further extend the capabilities of CID in the context of glycoproteomics.

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“…LLO (lipid-linked oligosaccharides) analysis of fibroblasts shows an accumulation of Man9GlcNAc2 (Imbach et al 1999;Burda et al 1998;Marklova and Albahri 2007). A few isolated CDG-ALG6 patients (e.g., patients with the homozygous c.391TT>C, p.Y131H mutation) presented with a normal transferrin and LLO profile (Westphal et al 2003;Miller et al 2011).…”

Section: Introductionmentioning

confidence: 99%