Effect of a singlein ovo injection of 2,3,7,8-tetrachlorodibenzo-p-dioxin on protein expression in liver and ovary of the one-day-old chick analyzed by fluorescent two-dimensional difference gel electrophoresis and mass spectrometry

PROTEOMICS ◽  
2006 ◽  
Vol 6 (8) ◽  
pp. 2576-2585 ◽  
Author(s):  
Veerle Bruggeman ◽  
Gert Van den Bergh ◽  
Stefan Clerens ◽  
Linn Dumez ◽  
Okanlawon Onagbesan ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Expression ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Difference Gel Electrophoresis ◽  
Tetrachlorodibenzo P Dioxin ◽  
The One

Proteome analysis of human hepatocellular carcinoma tissues by two-dimensional difference gel electrophoresis and mass spectrometry

PROTEOMICS ◽  
2005 ◽  
Vol 5 (8) ◽  
pp. 2258-2271 ◽  
Author(s):  
Cynthia R. M. Y. Liang ◽  
Chon Kar Leow ◽  
Jason C. H. Neo ◽  
Gek San Tan ◽  
Siaw Ling Lo ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Hepatocellular Carcinoma ◽  
Gel Electrophoresis ◽  
Proteome Analysis ◽  
Human Hepatocellular Carcinoma ◽  
Two Dimensional ◽  
Difference Gel Electrophoresis

scholarly journals Fluorescence two-dimensional difference gel electrophoresis for biomaterial applications

2009 ◽  
Vol 7 (suppl_1) ◽  
Author(s):  
Laura E. McNamara ◽  
Matthew J. Dalby ◽  
Mathis O. Riehle ◽  
Richard Burchmore
Keyword(s):  
Protein Expression ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Expression Levels ◽  
Powerful Technique ◽  
Difference Gel Electrophoresis

Fluorescence two-dimensional difference gel electrophoresis (DiGE) is rapidly becoming established as a powerful technique for the characterization of differences in protein expression levels between two or more conditions. In this review, we consider the application of DiGE—both minimal and saturation labelling—to biomaterials research, considering the challenges and rewards of this approach.

scholarly journals Impaired Lysosomal Trimming of N-Linked Oligosaccharides Leads to Hyperglycosylation of Native Lysosomal Proteins in Mice with α-Mannosidosis

2009 ◽  
Vol 30 (1) ◽  
pp. 273-283 ◽  
Author(s):  
Markus Damme ◽  
Willy Morelle ◽  
Bernhard Schmidt ◽  
Claes Andersson ◽  
Jens Fogh ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gel Electrophoresis ◽  
Cathepsin B ◽  
Genetic Defect ◽  
Two Dimensional ◽  
Difference Gel Electrophoresis ◽  
Free Oligosaccharides ◽  
Lysosomal Proteins

ABSTRACT α-Mannosidosis is caused by the genetic defect of the lysosomal α-d-mannosidase (LAMAN), which is involved in the breakdown of free α-linked mannose-containing oligosaccharides originating from glycoproteins with N-linked glycans, and thus manifests itself in an extensive storage of mannose-containing oligosaccharides. Here we demonstrate in a model of mice with α-mannosidosis that native lysosomal proteins exhibit elongated N-linked oligosaccharides as shown by two-dimensional difference gel electrophoresis, deglycosylation assays, and mass spectrometry. The analysis of cathepsin B-derived oligosaccharides revealed a hypermannosylation of glycoproteins in mice with α-mannosidosis as indicated by the predominance of extended Man3GlcNAc2 oligosaccharides. Treatment with recombinant human α-mannosidase partially corrected the hyperglycosylation of lysosomal proteins in vivo and in vitro. These data clearly demonstrate that LAMAN is involved not only in the lysosomal catabolism of free oligosaccharides but also in the trimming of asparagine-linked oligosaccharides on native lysosomal proteins.

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