Expanding the proteome two-dimensional gel electrophoresis reference map of human renal cortex by peptide mass fingerprinting

PROTEOMICS ◽  
2005 ◽  
Vol 5 (3) ◽  
pp. 816-825 ◽  
Author(s):  
Fulvio Magni ◽  
Cecilia Sarto ◽  
Cristina Valsecchi ◽  
Stefano Casellato ◽  
Stefano Ferrero Bogetto ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Renal Cortex ◽  
Peptide Mass Fingerprinting ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Peptide Mass ◽  
Reference Map

scholarly journals Altered Protein Expression of Streptococcus oralis Cultured at Low pH Revealed by Two-Dimensional Gel Electrophoresis

2001 ◽  
Vol 67 (8) ◽  
pp. 3396-3405 ◽  
Author(s):  
Joanna C. Wilkins ◽  
Karen A. Homer ◽  
David Beighton
Keyword(s):  
Gel Electrophoresis ◽  
Peptide Mass Fingerprinting ◽  
Low Ph ◽  
Ionization Mass ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Altered Expression ◽  
Streptococcus Oralis ◽  
Peptide Mass

ABSTRACT Streptococcus oralis is the predominant aciduric nonmutans streptococcus isolated from the human dentition, but the role of this organism in the initiation and progression of dental caries has yet to be established. To identify proteins that are differentially expressed by S. oralis growing under conditions of low pH, soluble cellular proteins extracted from bacteria grown in batch culture at pH 5.2 or 7.0 were analyzed by two-dimensional (2-D) gel electrophoresis. Thirty-nine proteins had altered expression at low pH; these were excised, digested with trypsin using an in-gel protocol, and further analyzed by peptide mass fingerprinting using matrix-assisted laser desorption ionization mass spectrometry. The resulting fingerprints were compared with the genomic database forStreptococcus pneumoniae, an organism that is phylogenetically closely related to S. oralis, and putative functions for the majority of these proteins were determined on the basis of functional homology. Twenty-eight proteins were up-regulated following growth at pH 5.2; these included enzymes of the glycolytic pathway (glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase), the polypeptide chains comprising ATP synthase, and proteins that are considered to play a role in the general stress response of bacteria, including the 60-kDa chaperone, Hsp33, and superoxide dismutase, and three distinct ABC transporters. These data identify, for the first time, gene products that may be important in the survival and proliferation of nonmutans aciduric S. oralis under conditions of low pH that are likely to be encountered by this organism in vivo.

Proteomic analysis defines altered cellular redox pathways and advanced glycation end-product metabolism in glomeruli of db/db diabetic mice

2007 ◽  
Vol 293 (4) ◽  
pp. F1157-F1165 ◽  
Author(s):  
Michelle T. Barati ◽  
Michael L. Merchant ◽  
Angela B. Kain ◽  
Anthony W. Jevans ◽  
Kenneth R. McLeish ◽  
...  
Keyword(s):  
Glutathione Peroxidase ◽  
Proteomic Analysis ◽  
Adaptive Response ◽  
Renal Cortex ◽  
Peptide Mass Fingerprinting ◽  
Glyoxalase I ◽  
Diabetic Mice ◽  
Two Dimensional Gel Electrophoresis ◽  
Peptide Mass

To attain a profile of protein expression during diabetes, we applied proteomic analysis to glomeruli of 160-day-old db/db diabetic and db/m nondiabetic mice. Glomerular proteins were extracted and separated by two-dimensional gel electrophoresis to construct a proteome map. Matrix-assisted laser desorption and ionization-time of flight mass spectrometry and peptide mass fingerprinting were used to identify 190 proteins. Of 105 analyzed spots, expression of 40 proteins, including the antioxidative enzymes peroxiredoxin 1 and 3, glutathione peroxidase 1, and SOD-1, was increased with diabetes, suggesting an adaptive response to oxidative stress associated with this diabetic model. However, activity of glutathione peroxidase and SOD was unaltered in glomeruli of diabetic mice. Expression of glyoxalase I was increased in glomeruli of diabetic mice. Because the cofactor for glyoxalase I, glutathione, is decreased in renal cortex of db/db mice, renal cortical glyoxalase I activity was measured in vitro with fixed amounts of exogenous glutathione. Glyoxalase I activity was decreased in renal cortex of db/db mice. These data indicate that diabetes-induced decreases in glyoxalase I activity are likely to be due to glutathione-dependent and -independent mechanisms and that increased expression of glyoxalase I may represent an insufficient adaptive response to increased methylglyoxal formation.

scholarly journals Proteomic Analysis of Azole Resistance in Candida albicans Clinical Isolates

2004 ◽  
Vol 48 (7) ◽  
pp. 2733-2735 ◽  
Author(s):  
Massoumeh Z. Hooshdaran ◽  
Katherine S. Barker ◽  
George M. Hilliard ◽  
Harald Kusch ◽  
Joachim Morschhäuser ◽  
...  
Keyword(s):  
Candida Albicans ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Peptide Mass Fingerprinting ◽  
Ergosterol Biosynthesis ◽  
Azole Resistance ◽  
Biosynthesis Pathway ◽  
Two Dimensional ◽  
Peptide Mass

ABSTRACT Changes in protein expression within a matched set of Candida albicans isolates representing the acquisition of azole resistance were examined by two-dimensional polyacrylamide gel electrophoresis and peptide mass fingerprinting. Proteins differentially expressed in association with azole resistance included Grp2p, Ifd1p, Ifd4p, Ifd5p, and Erg10p, a protein involved in the ergosterol biosynthesis pathway.

Diversity of Glycoprotein Deficiencies in Glanzmann’s Thrombasthenia

1985 ◽  
Vol 54 (03) ◽  
pp. 626-629 ◽  
Author(s):  
M Meyer ◽  
F H Herrmann
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Type Ii ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Structural Variant ◽  
Glanzmann’S Thrombasthenia ◽  
Crossed Immunoelectrophoresis ◽  
Glanzmann's Thrombasthenia ◽  
Platelet Proteins

SummaryThe platelet proteins of 9 thrombasthenic patients from 7 families were analysed by high resolution two-dimensional gel electrophoresis (HR-2DE) and crossed immunoelectrophoresis (CIE). In 7 patients both glycoproteins (GPs) IIb and Ilia were absent or reduced to roughly the same extent. In two related patients only a trace of GP Ilb-IIIa complex was detected in CIE, but HR-2DE revealed a glycopeptide in the position of GP Ilia in an amount comparable to type II thrombasthenia. This GP Ilia-like component was neither recognized normally by anti-GP Ilb-IIIa antibodies nor labeled by surface iodination. In unreduced-reduced two-dimensional gel electrophoresis two components were observed in the region of GP Ilia. The assumption of a structural variant of GP Ilia in the two related patients is discussed.

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