Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q.

@article{Rozanov2004NonproteolyticRI,
  title={Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q.},
  author={Dmitri V. Rozanov and Sergey Sikora and Adam Godzik and Tatiana I. Postnova and Vladislav S. Golubkov and Alexei Y Savinov and Stephen Tomlinson and Alex Y Strongin},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 48},
  pages={50321-8}
}
Membrane type-1 matrix metalloproteinase (MT1-MMP), a prototypic member of the membrane-tethered MMP family, is an essential component of a cellular proteolysis apparatus. Recognition of protein cleavage targets followed by proteolysis is a main function of MT1-MMP. For the first time, however, we present evidence that MT1-MMP and other structurally related membrane MMPs bind C1q, the recognition unit of the first component of complement C1 that initiates activation of the classical pathway of… CONTINUE READING