Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model.

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Rajaseger G, Lim CL, Lee KW, Arjunan P, Jia L, Moochhala S

Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model.

Front Biosci. 2006 Sep 1;11:2924-8.

PubMed ID
16720364 [ View in PubMed
]
Abstract

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.

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Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
Pyruvic acidPyruvate kinase PKLRProteinHumans
Unknown
Not AvailableDetails