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pubmed-article:9598901pubmed:abstractTextWe 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 between the effects of CMT on already active MMP versus the oxidative activation of latent MMP (pro-MMP).lld:pubmed
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pubmed-article:9598901pubmed:articleTitleFunctional sites of chemically modified tetracyclines: inhibition of the oxidative activation of human neutrophil and chicken osteoclast pro-matrix metalloproteinases.lld:pubmed
pubmed-article:9598901pubmed:affiliationDepartment of Medical Chemistry, Institute of Dentistry, University of Helsinki and Helsinki University Central Hospital, Finland.lld:pubmed
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pubmed-article:9598901pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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