Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0034067 (emphysema)
 11,506 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The CO2 laser is a precision surgical laser because of its high degree of absorption in soft tissue with limited lateral damage. The tissue, which absorbs the CO2 laser energy, and has a high water content, will be converted to vapor with a small residue of ash and a by-product of heat. The laser can only be effective if these by-products, i.e. vapors, heat, and carbon ash residue, are not injurious and are well tolerated by the joint. These by-products must be either reabsorbed by the synovium or remain as a nonviable substance in the joint. From April 1989 through April 1990, 40 patients underwent 43 operative arthroscopies of the knee using the Pfizer CO2 laser. All procedures were chondroplasties, synovectomies, and/or meniscectomies. All accessible CO2 carbon ash residue was removed from the joint after the procedures using an intraarticular shaver and hand rasp. Postoperatively there were no cases of hemorrhagic effusions, subcutaneous emphysema, or synovitis. Histologic examinations performed on 10 patients undergoing subsequent surgery showed no evidence of carbon ash residue or synovitis seen grossly or microscopically. The carbon ash residue is not noxious to the joint and is completely removed from the joint, presumably by the synovial response.
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PMID:The synovial response after CO2 laser arthroscopy of the knee. 828 Mar 30

Human macrophage elastase (MMP-12) plays an important role in inflammatory processes and has been implicated in diseases such as emphysema and chronic obstructive pulmonary disease (COPD). It is therefore an attractive target for therapeutic agents. As part of a structure-based drug design programme to find new inhibitors of MMP-12, the crystal structures of the MMP-12 catalytic domain (residues 106-268) complexed to three different non-peptidic small molecule inhibitors have been determined. The structures reveal that all three ligands bind in the S1' pocket but show varying degrees of interaction with the Zn atom. The structures of the complexes with inhibitors CP-271485 and PF-00356231 reveal that their central morpholinone and thiophene rings, respectively, sit over the Zn atom at a distance of approximately 5A, locating the inhibitors halfway down the S1' pocket. In both of these structures, an acetohydroxamate anion, an artefact of the crystallisation solution, chelates the zinc atom. By contrast, the acetohydroxamate anion is displaced by the ligand in the structure of MMP-12 complexed to PD-0359601 (Bayer), a potent zinc chelating N-substituted biaryl butyric acid, used as a reference compound for crystallisation. Although a racemate was used for the crystallisation, the S enantiomer only is bound in the crystal. Important hydrophobic interactions between the inhibitors and residues from the S1' pocket are observed in all of the structures. The relative selectivity displayed by these ligands for MMP-12 over other MMP family members is discussed.
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PMID:Crystal structures of novel non-peptidic, non-zinc chelating inhibitors bound to MMP-12. 1528 3