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Original Article

Isolation and characterization of an abundant elastase inhibitor from nacl extracts of bovine nasal septa and articular cartilage

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Pages 289-305 | Received 23 May 1991, Accepted 02 Jun 1992, Published online: 07 Jul 2009

References

  • Kleesiek I., Reinards R., Brackertz D., Neumann S., Lang H., Greiling H. Granulocyte elastase as a new biochemical marker in the diagnosis of chronic joint disease. Rheumatol. Int. 1986; 6: 161–169
  • Janoff A., Feinstein G., Malemud C. J., Elias J. M. Degradation of cartilage proteoglycans by human leukocyte granule neutral protease. I. Penetration of enzyme into rabbit articular cartilage and release of 35504 labeled material from the tissue. J. Clin. Invest. 1976; 57: 615–624
  • Burkhardt H., Kasten M., Rails S., Rehkopf E. Interference of cartilage surface with interaction of granulocyte elastase with alpha-l-protease inhibitor. Rheumatol. Int. 1987; 7: 133–138
  • Schalkwijk J., van den Berg W. B., Van De Putte L. B. A., Joosten L. A. B. Elastase secretion by activated polymorphonuclear leucocyte causes chondrocyte damage of matrix degeneration in intact articular cartilage: Escape of inactivation by alpha-l-proteinase inhibitor. Br. J. Exp. Pathol. 1987; 68: 81–88
  • Twumasi D. L., Liener I. E. Proteases from purulent sputum. Purification and properties of the elastase and chymotrypsin-like enzymes. J. Biol. Chem. 1977; 252: 1917–1926
  • March J. C., Parikh I., Cuatrecasas P. A simplified method for cyanogen bromide activation of agarose for affinity chromatography. Anal. Biochem. 1974; 60: 149–152
  • Tengblad A. A comparative study of the binding of cartilage link protein and the hyaluronate-binding region of the cartilage proteoglycan to hyaluronic-substituted Sepharose. Biochem. J. 1981; 199: 297–305
  • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 22: 680–685
  • Oakley B. R., Kirsch D. R., Morris N. R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 1980; 60: 149–152
  • Fairbanks G., Steck T. L., Wallach D. F. H. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 1971; 10: 2606–2616
  • Nakajima K., Powers J. C., Ashe B. M., Zimmerman M. Mapping the extended substrate binding site of the cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha-l-protease inhibitor reactive site. J. Biol. Chem. 1979; 254: 4027–4032
  • Erlanger B. F., Kakowsky H., Cohen W. Arch. Biochem. Biophys. 1961; 95: 271–278
  • Bieth J., Spies B., Wermuth C. G. The synthesis and analytical use of a highly sensitive and convenient substrate of elastase. Biochem. Med. 1974; 11: 350–357
  • Feinstein G., Kupfer A., Sokolovsky M. N-acetyl-(L-Ala)3-p-nitroanilide as a new chromogenic substrate for elastase. Biochem. Biophys. Res. Acta 1973; 50: 1020–1026
  • Hummel B. C. W. A method for automated analysis of the activity of trypsin, chymotrypsin and their inhibitors. Can. J. Biochem. Physiol. 1959; 37: 1393–1400
  • Stewart K. K. A method for automated analysis of the activity of trypsin, chymotrypsin and their inhibitors. Anal. Biochem. 1973; 51: 11–18
  • Barrett A. J., Kirschke H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 1981; 80: 535–561
  • Homandberg G. A., Wai T. Reduction of disulfides in urokinase and insertion of a synthetic peptide. Biochim. Biophys. Acta 1990; 1038: 209–215
  • Shugar D. Measurement of lysozyme activity and the ultra violet inactivation of lysozyme. Biochim. Biophys Acta 1952; 8: 302–308
  • Schauer R. Characterization of sialic acids. Methods Enzymol. 1978; 50: 64–89
  • Chandrasekhar A., Esterman M. A., Hoffman H. A. Microdetermination of proteoglycans and glycosaminoglycans in the presence of guanidine hydrochloride. Analytical Biochemistry 1987; 161: 103–108
  • Levery S., Hakomori S. Microscale methylation analysis of glycolipids using capillary gas chromatography-chemical ionization mass fragmentography with selected ion monitoring. Methods Enzymol. 1987; 138: 13–25
  • Sorgente N., Hascall V. C., Kuettner K. E. Extractability of lysozyme from bovine nasal cartilage. Biochim. Biophys. Acta. 1972; 284: 441–450
  • Riddles P W, Blakely R. L., Zerner B. Reassessment of Ellman's reagent. Methods Enzymol. 1983; 91: 49–60
  • Roughley P. J., Murphy G., Barrett A. J. Proteinase inhibitors of bovine nasal cartilage. Biochem. J. 1978; 169: 721–724
  • Killackey J. J., Roughley P. J., Mort J. S. Proteinase inhibitors of human articular cartilage. Collagen Rel. Res. 1983; 3: 419–430
  • Lesjak M. S., Ghosh P. Polypeptide proteinase inhibitors from human articular cartilage. Biochim. Biophys. Acta 1984; 789: 266–277
  • Martel-Pelletier J., Cloutier J. M., Pelletier J. P. Cathepsin B and cysteine protease inhibitors in human osteoarthritis. J. Orthop. Res. 1990; 8: 336–344
  • Burkhardt H., Kastan M., Rauls S. Purification and characterization of a serine proteinase inhibitor from human articular cartilage. Biochim. Biophys. Acta 1987; 924: 312–318
  • Knight J. A., Stephens R. W, Bushell G. R., Ghosh P, Taylor T. K. F. Neutral proteinase inhibitors from human intervertebral disc and femoral head cartilage. Biochim. Biophys. Acta 1979; 584: 304–310
  • Andrews J. L., Ghosh P. Low molecular weight serine proteinase inhibitor of human articular cartilage. Isolation, characterization and biosynthesis. Arthritis Rheum 1990; 33: 1384–1393
  • Boehm B., Deutzmann R., Burkhardt H. Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions. Biochem J. 1991; 274: 269–273
  • Kuettner K. E., Croxen R. L., Eisenstein L., Sorgente N. Proteinase inhibitory activity in connective tissue. Experientia 1974; 30: 595–597
  • Sorgente N., Kuettner K. E., Eisenstein R. The isolation, purification and partial characterization of proteinase inhibitors from bovine cartilage and aorta. Protides Biol. Fluids 1975; 23: 227–230
  • DiMuzio M., Tripier D., Kuettner K. E. Purification and characterization of an elastase inhibitor derived from hyaline cartilage. J. Rheumatol Suppl. 1987; 14: 45–48
  • Keith D. A., Paz M. A., Gallop P. M., Glimcher M. J. Histologic and biochemical identification and characterization of an elastin in cartilage. J. Histochem. Cytochem. 1977; 25: 1154–1162
  • Murphy G., Cockett M. I., Ward R. V., Docherty A. J. P. Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. Biochem. J. 1991; 277: 277–279
  • Sandy J. D., Spiratana A., Brown H. L. G., Lowther D. A. Evidence of polymorphonuclearleucocyte-derived proteinases in arthritic cartilage. Biochem J. 1981; 193: 193–202
  • Menninger H., Burkhardt H., Roske W., Ehlebracht W., Hering B., Gurr E., Mohr W., Mierau H. D. Lysosomal elastase: effect on mechanical and biochemical properties of normal cartilage: inhibition by polysulfonated glycosaminoglycan and binding to chondrocytes. Rheumatol. Int. 1981; 1: 73–78

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