IMR Press / FBL / Volume 11 / Issue 3 / DOI: 10.2741/2021

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model
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1 Defence Medical and Environmental Research Institute, DSO National Laboratories
2 Dept. Anatomy NUS, Singapore 117510
Academic Editors:Pandjassarame Kangueane, Meena Sakharkar, Meena Sakharkar
Front. Biosci. (Landmark Ed) 2006, 11(3), 2924–2928;
Published: 1 September 2006
(This article belongs to the Special Issue Bioinformation)

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 ºC (control) and at core temperature (Tc) 42 ºC (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.

Heat stress
Rat model
Hepatocellular proteins
Polyacrylamide gel electrophoresis
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