Functional sites of chemically modified tetracyclines: inhibition of the oxidative activation of human neutrophil and chicken osteoclast pro-matrix metalloproteinases.

@article{Sorsa1998FunctionalSO,
  title={Functional sites of chemically modified tetracyclines: inhibition of the oxidative activation of human neutrophil and chicken osteoclast pro-matrix metalloproteinases.},
  author={Timo Sorsa and Nungavaram S. Ramamurthy and Anthony T Vernillo and Xiaoe Zhang and Yrj{\"o} T. Konttinen and Barry R. Rifkin and Lorne M. Golub},
  journal={The Journal of rheumatology},
  year={1998},
  volume={25 5},
  pages={975-82}
}
OBJECTIVE We studied the relative ability of 6 different chemically modified non-antimicrobial analogs of tetracycline (CMT) to inhibit human and chicken matrix metalloproteinases (MMP) in vitro. The ability of tetracycline and its analogs to inhibit MMP appears to depend on the Ca++/Zn++ binding site at C11 (carbonyl oxygen) and C12 (OH group) of the molecule, which is lacking in CMT-5, the pyrazole derivative of tetracycline. This significant property of CMT-5 was used to differentiate… CONTINUE READING