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

Ganapathy Rajaseger, Chin Leong Lim, Koon Wui Lee, Pachiappan Arjunan, Lu Jia, Shabbir Moochhala

Research output: Contribution to journalArticle

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 °C (control) and at core temperature (Tc) 42 °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.

Original languageEnglish (US)
Pages (from-to)2924-2928
Number of pages5
JournalFrontiers in Bioscience
Volume11
Issue numberSUPPL. 3
DOIs
StatePublished - Jun 5 2006
Externally publishedYes

Fingerprint

Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Rats
Hot Temperature
Proteins
Pyruvate Kinase
Electrophoresis, Gel, Two-Dimensional
Shock
Transketolase
Heat Stroke
Isomerases
Carboxylesterase
Ligases
Liver
Oxidoreductases
Molecular Weight
Molecular weight
Temperature

Keywords

  • 1D PAGE
  • Heat stress
  • Hepatocellular proteins
  • MALDI
  • MS
  • Polyacrylamide gel electrophoresis
  • Rat model

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Rajaseger, G., Lim, C. L., Lee, K. W., Arjunan, P., Jia, L., & Moochhala, S. (2006). Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model. Frontiers in Bioscience, 11(SUPPL. 3), 2924-2928. https://doi.org/10.2741/2021

Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model. / Rajaseger, Ganapathy; Lim, Chin Leong; Lee, Koon Wui; Arjunan, Pachiappan; Jia, Lu; Moochhala, Shabbir.

In: Frontiers in Bioscience, Vol. 11, No. SUPPL. 3, 05.06.2006, p. 2924-2928.

Research output: Contribution to journalArticle

Rajaseger, G, Lim, CL, Lee, KW, Arjunan, P, Jia, L & Moochhala, S 2006, 'Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model', Frontiers in Bioscience, vol. 11, no. SUPPL. 3, pp. 2924-2928. https://doi.org/10.2741/2021
Rajaseger, Ganapathy ; Lim, Chin Leong ; Lee, Koon Wui ; Arjunan, Pachiappan ; Jia, Lu ; Moochhala, Shabbir. / Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model. In: Frontiers in Bioscience. 2006 ; Vol. 11, No. SUPPL. 3. pp. 2924-2928.
@article{2b5fa889cc654b97bce495e0c47527c5,
title = "Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model",
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 °C (control) and at core temperature (Tc) 42 °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.",
keywords = "1D PAGE, Heat stress, Hepatocellular proteins, MALDI, MS, Polyacrylamide gel electrophoresis, Rat model",
author = "Ganapathy Rajaseger and Lim, {Chin Leong} and Lee, {Koon Wui} and Pachiappan Arjunan and Lu Jia and Shabbir Moochhala",
year = "2006",
month = "6",
day = "5",
doi = "10.2741/2021",
language = "English (US)",
volume = "11",
pages = "2924--2928",
journal = "Frontiers in Bioscience - Landmark",
issn = "1093-9946",
publisher = "Frontiers in Bioscience",
number = "SUPPL. 3",

}

TY - JOUR

T1 - Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model

AU - Rajaseger, Ganapathy

AU - Lim, Chin Leong

AU - Lee, Koon Wui

AU - Arjunan, Pachiappan

AU - Jia, Lu

AU - Moochhala, Shabbir

PY - 2006/6/5

Y1 - 2006/6/5

N2 - 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 °C (control) and at core temperature (Tc) 42 °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.

AB - 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 °C (control) and at core temperature (Tc) 42 °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.

KW - 1D PAGE

KW - Heat stress

KW - Hepatocellular proteins

KW - MALDI

KW - MS

KW - Polyacrylamide gel electrophoresis

KW - Rat model

UR - http://www.scopus.com/inward/record.url?scp=33744482874&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33744482874&partnerID=8YFLogxK

U2 - 10.2741/2021

DO - 10.2741/2021

M3 - Article

C2 - 16720364

AN - SCOPUS:33744482874

VL - 11

SP - 2924

EP - 2928

JO - Frontiers in Bioscience - Landmark

JF - Frontiers in Bioscience - Landmark

SN - 1093-9946

IS - SUPPL. 3

ER -