Changes of Carbohydrate-Deficient Transferrin in Chronic Alcoholism

König, P; Niederhofer, Helmut; Steurer, H.; Haller, Reinhard; Wölfle, Roland; Fritzsche, H; Weiss, Pamela

doi:10.1159/000119235

Cited by 4 publications

(3 citation statements)

References 14 publications

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“…Remaining 15% of transferrin molecules are penta-or trisialylated, while the proportion of less sialylated molecules is negligible [78]. The transferrin of lowered sialylation is called carbohydrate-deficient transferrin, and since its appearance reflect disturbances in glycosylation machinery it is already being routinely used to diagnose chronic alcoholism [79,80] and congenital disorders of glycosylation [71].…”

Section: Transferrinmentioning

confidence: 99%

Glycosylation of Serum Proteins in Inflammatory Diseases

2008

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Inflammatory diseases are accompanied by numerous changes at the site of inflammation as well as many systemic physiological and biochemical changes. In the past two decades more and more attention is being paid to changes in glycosylation and in this review we describe some of the changes found on main serum proteins (α1-acid glycoprotein, immunoglobulin G, immunoglobulin A, transferrin, haptoglobin, α2-macroglobulin, C-reactive protein, and others). Molecular background and physiological importance of most of these changes are yet to be discovered, but it is evident that glycosylation plays an important role in the inflammatory response. Maybe the greatest value of these changes currently lays in their potential diagnostic and prognostic usage, either in combination with current diagnostic markers or on their own. However, determining glycan structures is still technically too complex for most clinical laboratories and further efforts have to be made to develop simple analytical tools to study changes in glycosylation.

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Section: Transferrinmentioning

confidence: 99%

Glycosylation of Serum Proteins in Inflammatory Diseases

2008

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“…Changes in transferrin sialylation were found in many pathological conditions [19] and carbohydrate-deficient transferrin (CDT) is already being used to diagnose chronic alcoholism [20,21] and congenital disorders of glycosylation [22].…”

Section: Introductionmentioning

confidence: 99%

Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis

Gornik

Gašparović

et al. 2008

Clinical Biochemistry

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“…Gene mutations can cause defects in glycosylation resulting in inborn errors of metabolism, characterized by deficient or reduced glycosylation and known as congenital disorders of glycosylation (CDGs) [ 7 ]. Change of sialylation has also been linked to alcoholism and many pathological states [ 8 , 9 ]. Nowadays, the analysis of glycosylation change is used as a diagnostic tool for alcoholism and congenital disorders of glycosylation [ 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Low-pressure chromatographic separation and UV/Vis spectrophotometric characterization of the native and desialylated human apo-transferrin

Friganović¹,

Tomašić²,

Šeba³

et al. 2021

Heliyon

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Low-pressure pH gradient ion exchange separation provides a fast, simple and cost-effective method for preparative purification of native and desialylated apo-transferrin. The method enables easy monitoring of the extent of the desialylation reaction and also the efficient separation and purification of protein fractions after desialylation. The N -glycan analysis shows that the modified desialylation protocol successfully reduces the content of the sialylated fractions relative to the native apo-transferrin. In the optimized protocol, the desialylation capacity is increased by 150 %, compared to the original protocol provided by the manufacturer. The molar absorption coefficients in the near-UV region for the native and desialylated apo-transferrin differ by several percent, suggesting a subtle dependence of the glycoprotein absorbance on the variable sialic acid content. The method can easily be modified for other glycoproteins and is particularly appropriate for quick testing of sialic acid content in the protein glycosylation patterns prior to further verification by mass spectrometry.

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Changes of Carbohydrate-Deficient Transferrin in Chronic Alcoholism

Cited by 4 publications

References 14 publications

Glycosylation of Serum Proteins in Inflammatory Diseases

Glycosylation of Serum Proteins in Inflammatory Diseases

Change in transferrin sialylation is a potential prognostic marker for severity of acute pancreatitis

Low-pressure chromatographic separation and UV/Vis spectrophotometric characterization of the native and desialylated human apo-transferrin

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