A 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds α4β1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells.

@article{UgarteBerzal2012A1S,
  title={A 17-residue sequence from the matrix metalloproteinase-9 (MMP-9) hemopexin domain binds α4β1 integrin and inhibits MMP-9-induced functions in chronic lymphocytic leukemia B cells.},
  author={Estefania Ugarte-Berzal and Elvira Bail{\'o}n and Irene Amigo-Jim{\'e}nez and Cid{\^o}nia de Lourdes Vituri and Mercedes Hern{\'a}ndez del Cerro and Mar{\'i}a Jos{\'e} Terol and Juan P. Albar and Germ{\'a}n Tenorio Rivas and Jos{\'e} Antonio Garc{\'i}a-Marco and {\'A}ngeles Garc{\'i}a-Pardo},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 33},
  pages={
          27601-13
        }
}
We previously showed that pro-matrix metalloproteinase-9 (proMMP-9) binds to B chronic lymphocytic leukemia (B-CLL) cells and contributes to B-CLL progression by regulating cell migration and survival. Induction of cell survival involves a non-proteolytic mechanism and the proMMP-9 hemopexin domain (PEX9). To help design specific inhibitors of proMMP-9-cell binding, we have now characterized B-CLL cell interaction with the isolated PEX9. B-CLL cells bound soluble and immobilized GST-PEX9, but… CONTINUE READING
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Matrix metalloprotein 4 1 Integrin Binding Site in PEX9 as Target in B-CLL 27612 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME

  • K. Kessenbrock, V. Plaks, Z. Werb
  • AUGUST 10, by gest on July 15,
  • 2010
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