Advanced search
1 file | 167.53 KB

A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid

Author
Organization
Abstract
A crucial event in the process of apoptosis is caspase-dependent generation of truncated Bid (tBid), inducing release of cytochrome c. In an in vitro reconstitution system we combined purified recombinant tBid with isolated liver mitochondria and identified the released proteins using a proteomic matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) approach. In order to meet physiological conditions, the concentration of tBid was chosen such that it was unable to induce cytochrome c release in mitochondria derived from liver-specific Bcl-2-transgenic mice. Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi. Western blotting confirmed the absence of adenylate kinase 3, a matrix mitochondrial protein. These results demonstrate that a physiologically relevant concentration of tBld is sufficient to induce release of particular intermembrane mitochondrial proteins belonging to a broad molecular-mass range.
Keywords
ENDOPLASMIC-RETICULUM, CASPASE ACTIVATION, PERMEABILITY TRANSITION, CELL-DEATH, WD-40 REPEAT REGION, BCL-2 FAMILY MEMBERS, CYTOCHROME-C RELEASE, tBid, mitochondria, MALDI-PSD, apoptosis, caspase, ADENYLATE KINASE, STRUCTURAL BASIS, SERINE-PROTEASE

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 167.53 KB

Citation

Please use this url to cite or link to this publication:

Chicago
van Loo, Geert, Hans Demol, Maria Van Gurp, B Hoorelbeke, Peter Schotte, Rudi Beyaert, B Zhivotovsky, et al. 2002. “A Matrix-assisted Laser Desorption Ionization Post-source Decay (MALDI-PSD) Analysis of Proteins Released from Isolated Liver Mitochondria Treated with Recombinant Truncated Bid.” Cell Death and Differentiation 9 (3): 301–308.
APA
van Loo, Geert, Demol, H., Van Gurp, M., Hoorelbeke, B., Schotte, P., Beyaert, R., Zhivotovsky, B., et al. (2002). A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid. CELL DEATH AND DIFFERENTIATION, 9(3), 301–308.
Vancouver
1.
van Loo G, Demol H, Van Gurp M, Hoorelbeke B, Schotte P, Beyaert R, et al. A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid. CELL DEATH AND DIFFERENTIATION. 2002;9(3):301–8.
MLA
van Loo, Geert, Hans Demol, Maria Van Gurp, et al. “A Matrix-assisted Laser Desorption Ionization Post-source Decay (MALDI-PSD) Analysis of Proteins Released from Isolated Liver Mitochondria Treated with Recombinant Truncated Bid.” CELL DEATH AND DIFFERENTIATION 9.3 (2002): 301–308. Print.
@article{156373,
  abstract     = {A crucial event in the process of apoptosis is caspase-dependent generation of truncated Bid (tBid), inducing release of cytochrome c. In an in vitro reconstitution system we combined purified recombinant tBid with isolated liver mitochondria and identified the released proteins using a proteomic matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) approach. In order to meet physiological conditions, the concentration of tBid was chosen such that it was unable to induce cytochrome c release in mitochondria derived from liver-specific Bcl-2-transgenic mice. Several mitochondrial proteins were identified to be released in a tBid-dependent way, among which cytochrome c, DIABLO/Smac, adenylate kinase 2, acyl-CoA-binding protein, endonuclease G, polypyrimidine tract-binding protein, a type-I RNA helicase, a WD-40 repeat-containing protein and the serine protease Omi. Western blotting confirmed the absence of adenylate kinase 3, a matrix mitochondrial protein. These results demonstrate that a physiologically relevant concentration of tBld is sufficient to induce release of particular intermembrane mitochondrial proteins belonging to a broad molecular-mass range.},
  author       = {van Loo, Geert and Demol, Hans and Van Gurp, Maria and Hoorelbeke, B and Schotte, Peter and Beyaert, Rudi and Zhivotovsky, B and Gevaert, Kris and Declercq, Wim and Vandekerckhove, Jo{\"e}l and Vandenabeele, Peter},
  issn         = {1350-9047},
  journal      = {CELL DEATH AND DIFFERENTIATION},
  keyword      = {ENDOPLASMIC-RETICULUM,CASPASE ACTIVATION,PERMEABILITY TRANSITION,CELL-DEATH,WD-40 REPEAT REGION,BCL-2 FAMILY MEMBERS,CYTOCHROME-C RELEASE,tBid,mitochondria,MALDI-PSD,apoptosis,caspase,ADENYLATE KINASE,STRUCTURAL BASIS,SERINE-PROTEASE},
  language     = {eng},
  number       = {3},
  pages        = {301--308},
  title        = {A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid},
  url          = {http://dx.doi.org/10.1038/sj.cdd.4400966},
  volume       = {9},
  year         = {2002},
}

Altmetric
View in Altmetric
Web of Science
Times cited: