New alterations of serum glycoproteins in alcoholic and cirrhotic patients revealed by high resolution two-dimensional gel electrophoresis

Details

Serval ID
serval:BIB_E0CA53854AA0
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
New alterations of serum glycoproteins in alcoholic and cirrhotic patients revealed by high resolution two-dimensional gel electrophoresis
Journal
Biochemical and Biophysical Research Communications
Author(s)
Gravel  P., Walzer  C., Aubry  C., Balant  L. P., Yersin  B., Hochstrasser  D. F., Guimon  J.
ISSN
0006-291X (Print)
Publication state
Published
Issued date
03/1996
Volume
220
Number
1
Pages
78-85
Notes
Comparative Study
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Mar 7
Abstract
Plasma protein are synthesized and secreted by the liver. Several reports have shown that excessive consumption of ethanol interferes with the hepatic protein synthesis and/or secretion. This study was undertaken to identify the plasma/serum proteins altered in two groups of patients with different alcohol-related diseases: actively drinking alcoholic patients group without liver disease and alcohol cirrhotic patients group. Two-dimensional gel electrophoresis was used to separate proteins with high resolution. Proteins were detected by silver staining and glycoproteins were specifically visualized and analyzed after lectin blotting followed by chemiluminescence detection. Different protein alterations were identified in each group of patients. In the alcoholic group, two new glycosylation modifications of serum proteins were identified. An abnormal microheterogeneity of haptoglobin and alpha1-antitrypsin was detected in the serum of all alcoholic patients. We also characterized by two-dimensional gel electrophoresis the carbohydrate deficient transferrin. The modifications of haptoglobin, alpha1-antitrypsin and transferrin present a similar change of charge and molecular weight in the two-dimensional gel electrophoresis pattern. These qualitative estimations support the hypothesis of a general mechanism of liver glycosylation alteration of serum proteins induced by excessive alcohol consumption. The immunoglobulin alterations were easily visualized and identified for the cirrhotic and the alcoholic patients. And finally, the decrease of haptoglobin and albumin spots for cirrhotic patients was confirmed.
Keywords
Alcoholism/*blood Blood Protein Electrophoresis Carbohydrate Sequence Case-Control Studies Electrophoresis, Gel, Two-Dimensional Female Glycoproteins/*blood/chemistry/isolation & purification Haptoglobins/chemistry/isolation & purification Humans Immunoglobulin A/blood/isolation & purification Liver Cirrhosis, Alcoholic/*blood Male Molecular Sequence Data Oligosaccharides/chemistry Transferrin/chemistry/isolation & purification alpha 1-Antitrypsin/chemistry/isolation & purification
Pubmed
Web of science
Create date
24/01/2008 16:31
Last modification date
20/08/2019 16:05
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