Stress-induced changes in theSchizosaccharomyces pombe proteome using two-dimensional difference gel electrophoresis, mass spectrometry and a novel integrated robotics platform

PROTEOMICS ◽  
2005 ◽  
Vol 5 (6) ◽  
pp. 1669-1685 ◽  
Author(s):  
Mark E. Weeks ◽  
John Sinclair ◽  
Richard J. Jacob ◽  
Malcolm J. Saxton ◽  
Susan Kirby ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Difference Gel Electrophoresis ◽  
Induced Changes

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 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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