Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model.
Heat induced complications cause an increase in a large number of proteins which play a role in diverse pathways during heat shock. A detailed characterization of these proteins is essential for understanding the molecular mechanisms involved in heat stroke. In this report, the proteins present in rat liver were compared at 37 degrees C (control) and at core temperature (Tc) 42 degrees C (heat stress) by 1D PAGE and MALDI/MS/MS. Among proteins identified in the sample after heat stress are dimethyglycine dehydrogenase, transketolase, carboxylic ester hydrolase, pyruvate kinase, L-type pyruvate kinase, arginosuccinate synthetase; fumarylacetoacetate hydrolase and peptidylpropyl isomerase A. These findings show that analysis of large scale proteins by MALDI/MS/MS provides a better understanding of the molecular mechanisms associated with heat shock. The resolution of proteins examined by 1D-PAGE was less than that obtained with 2D-PAGE. More specifically, 2D-PAGE allows better identification of low molecular weight proteins that can not be resolved by 1D-PAGE.
Rajaseger
Ganapathy
G
Defence Medical and Environmental Research Institute, DSO National Laboratories, Singapore. grajaseg@dso.org.sg
Lim
Chin Leong
CL
Lee
Koon Wui
KW
Arjunan
Pachiappan
P
Jia
Lu
L
Moochhala
Shabbir
S
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D018882:Heat Stress Disorders; D006360:Heat-Shock Proteins / Q000032:analysis* / Q000096:biosynthesis*; D008099:Liver / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D051381:Rats; D017208:Rats, Wistar; D012680:Sensitivity and Specificity; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006360:Heat-Shock Proteins