Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G.
作者： Claudia Sissi , Lorena Lucatello , Annamaria Naggi , Giangiacomo Torri , Manlio Palumbo
DOI: 10.1016/J.BCP.2005.10.027
关键词:
摘要: Semi-synthetic low-molecular-weight heparin samples (LMWHs), having homogeneous degree of polymerization and saccharide backbone, but differing in the number location sulfate groups, were investigated their ability to interfere with pharmacologically relevant targets human leukocyte elastase (EL) Cathepsin G (CatG). Spectroscopic studies performed for a quantitative evaluation enzyme-inhibitor dissociation constant, Ki, IC50 values inhibition cleavage target peptide sequences. Both proteases are inhibited by tested polysaccharides through mixed hyperbolic binding process. A non-linear relationship was found between sulfation affinity or enzyme properties, showing composite correlation charge density interference EL/CatG activity.
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R Egbring, W Schmidt, G Fuchs, K Havemann, Demonstration of granulocytic proteases in plasma of patients with acute leukemia and septicemia with coagulation defects Blood. ,vol. 49, pp. 219- 231 ,(1977) , 10.1182/BLOOD.V49.2.219.219
P. Hof, I. Mayr, R. Huber, E. Korzus, J. Potempa, J. Travis, J. C. Powers, W. Bode, The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities. The EMBO Journal. ,vol. 15, pp. 5481- 5491 ,(1996) , 10.1002/J.1460-2075.1996.TB00933.X
A. Naggi, G. Torri, B. Casu, J. Pangrazzi, M. Abbadini, M. Zametta, M.B. Donati, J. Lansen, J.P. Maffrand, “Supersulfated” heparin fragments, a new type of low-molecular weight heparin: Physico-chemical and pharmacological properties Biochemical Pharmacology. ,vol. 36, pp. 1895- 1900 ,(1987) , 10.1016/0006-2952(87)90485-0
K.J. Frommherz, B. Faller, J.G. Bieth, Heparin strongly decreases the rate of inhibition of neutrophil elastase by alpha 1-proteinase inhibitor. Journal of Biological Chemistry. ,vol. 266, pp. 15356- 15362 ,(1991) , 10.1016/S0021-9258(18)98623-0
Heparin protects cathepsin G against inhibition by protein proteinase inhibitors. Journal of Biological Chemistry. ,vol. 269, pp. 29502- 29508 ,(1994) , 10.1016/S0021-9258(18)43908-7
Benito Casu, Ulf Lindahl, Structure and biological interactions of heparin and heparan sulfate. Advances in Carbohydrate Chemistry and Biochemistry. ,vol. 57, pp. 159- 206 ,(2001) , 10.1016/S0065-2318(01)57017-1
P C Esmon, M A Fournel, R E Jordan, R M Nelson, J Kilpatrick, J O Newgren, Inactivation of human antithrombin by neutrophil elastase. Kinetics of the heparin-dependent reaction. Journal of Biological Chemistry. ,vol. 264, pp. 10493- 10500 ,(1989) , 10.1016/S0021-9258(18)81648-9
E K Silverman, E J Campbell, M A Campbell, Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. Journal of Immunology. ,vol. 143, pp. 2961- 2968 ,(1989)
A Baici, Graphical and statistical analysis of hyperbolic tight-binding inhibition Biochemical Journal. ,vol. 244, pp. 793- 796 ,(1987) , 10.1042/BJ2440793
S T Olson, I Björk, Antithrombin. A bloody important serpin. Advances in Experimental Medicine and Biology. ,vol. 425, pp. 17- 33 ,(1997)