Biochemical evidence of the interactions of membrane type-1 matrix metalloproteinase (MT1-MMP) with adenine nucleotide translocator (ANT): potential implications linking proteolysis with energy metabolism in cancer cells.

@article{Radichev2009BiochemicalEO,
  title={Biochemical evidence of the interactions of membrane type-1 matrix metalloproteinase (MT1-MMP) with adenine nucleotide translocator (ANT): potential implications linking proteolysis with energy metabolism in cancer cells.},
  author={Ilian A Radichev and Albert G. Remacle and Nor Eddine Sounni and Sergey A. Shiryaev and Dmitri V. Rozanov and WenHong Zhu and Natalya V Golubkova and Tatiana I. Postnova and Vladislav S. Golubkov and Alex Y Strongin},
  journal={The Biochemical journal},
  year={2009},
  volume={420 1},
  pages={37-47}
}
Invasion-promoting MT1-MMP (membrane type-1 matrix metalloproteinase) is a key element in cell migration processes. To identify the proteins that interact and therefore co-precipitate with this proteinase from cancer cells, we used the proteolytically active WT (wild-type), the catalytically inert E240A and the C-end truncated (tailless; DeltaCT) MT1-MMP-FLAG constructs as baits. The identity of the pulled-down proteins was determined by LC-MS/MS (liquid chromatography tandem MS) and then… CONTINUE READING

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  • 2008

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