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Human Leukocyte Elastase (human + leukocyte_elastase)
Selected AbstractsNew Peptolides from the Cyanobacterium Nostoc insulare as Selective and Potent Inhibitors of Human Leukocyte ElastaseCHEMBIOCHEM, Issue 16 2008Christian Mehner Abstract Eight new cyanopeptolins (insulapeptolides A,H) were obtained from the cyanobacterium Nostoc insulare. Their isolation was guided by their bioactivity toward the target enzyme human leukocyte elastase, molecular biological investigations, and MALDI-TOF analysis. These peptides are selective inhibitors of human leukocyte elastase with activities in the nanomolar range. Insulapeptolide D (4) was the most potent compound with an IC50 value of 85 nM (Ki value of 36 nM). [source] Inhibition of Human Leukocyte Elastase by Brunsvicamides,A,C: Cyanobacterial Cyclic PeptidesCHEMMEDCHEM, Issue 9 2009Mihiret Cyanobacterial cyclic peptides, brunsvicamides,A,C, were evaluated as inhibitors of human leukocyte elastase (HLE), and subsequently tested against a panel of proteases and two serine esterases. Brunsvicamides,A,C were found to be highly selective for HLE. [source] The defensive role of lysozyme in human gingiva in inflammatory periodontal diseaseJOURNAL OF PERIODONTAL RESEARCH, Issue 5 2009R. Younes Background and Objective:, The presence of lysozyme in human gingiva has not previously been demonstrated. In this study, we looked for evidence for the potential role of lysozyme as a protector of gingival elastic fibres. The objective of this study was also to determine the ex vivo susceptibility to hydrolysis of gingival elastic fibres from patients with or without periodontal disease by human leukocyte elastase and by human cathepsin G. Materials and Methods:, Using gingival tissue sections from eight control, 10 gingivitis and 10 periodontitis patients, we evaluated the area fraction occupied by gingival elastic fibres (after selective staining) by the use of automated image analysis. In the ex vivo experiments, serial tissue sections from four control, four gingivitis, four young periodontitis and four aged periodontitis patients were submitted to the action of human leukocyte elastase and cathepsin G, after which enzymatic activities were determined by image analysis. Indirect immunodetection of lysozyme was also done on tissue sections for all patients included in this study. Results:, Large variations of the area fraction occupied by elastic fibres were observed in human gingiva from young and aged patients with and without periodontal disease. In control and gingivitis patients, leukocyte elastase and cathepsin G had high comparable elastin solubilizing activities. With young and aged periodontitis patients, the two serine proteinases had weak elastin solubilizing activities. Lysozyme appeared to be present at the periphery of gingival elastic fibres in periodontitis patients. Conclusion:, Lysozyme can be considered an important natural protector of elastic fibres in pathological gingiva. [source] Structure of the complex of porcine pancreatic elastase with a trimacrocyclic peptide inhibitor FR901451ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2005Takayoshi Kinoshita Porcine pancreatic elastase (PPE) resembles the attractive drug target leukocyte elastase, which has the ability to degrade connective tissue in the body. The crystal structure of PPE complexed with a novel trimacrocyclic peptide inhibitor, FR901451, was solved at 1.9,Å resolution. The inhibitor occupied the subsites S3 through S3, of PPE and induced conformational changes in the side chains of Arg64 and Arg226, which are located at the edges of the substrate-binding cleft. Structural comparison of five PPE,inhibitor complexes, including the FR901451 complex and non-ligated PPE, reveals that the residues forming the S2, S1, S1, and S2, subsites in the cleft are rigid, but the two arginine residues playing a part in the S3 and S3, subsites are flexible. Structural comparison of PPE with human leukocyte elastase (HLE) implies that the inhibitor binds to HLE in a similar manner to the FR901451,PPE complex. This structural insight may help in the design of potent elastase inhibitors. [source] New Peptolides from the Cyanobacterium Nostoc insulare as Selective and Potent Inhibitors of Human Leukocyte ElastaseCHEMBIOCHEM, Issue 16 2008Christian Mehner Abstract Eight new cyanopeptolins (insulapeptolides A,H) were obtained from the cyanobacterium Nostoc insulare. Their isolation was guided by their bioactivity toward the target enzyme human leukocyte elastase, molecular biological investigations, and MALDI-TOF analysis. These peptides are selective inhibitors of human leukocyte elastase with activities in the nanomolar range. Insulapeptolide D (4) was the most potent compound with an IC50 value of 85 nM (Ki value of 36 nM). [source] Inhibition of Human Leukocyte Elastase by Brunsvicamides,A,C: Cyanobacterial Cyclic PeptidesCHEMMEDCHEM, Issue 9 2009Mihiret Cyanobacterial cyclic peptides, brunsvicamides,A,C, were evaluated as inhibitors of human leukocyte elastase (HLE), and subsequently tested against a panel of proteases and two serine esterases. Brunsvicamides,A,C were found to be highly selective for HLE. [source] | ||||||||||