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Volumn 272, Issue 3 16-3, 1997, Pages

Glycosaminoglycans regulate elastase inhibition by oxidized secretory leukoprotease inhibitor

Author keywords

dermatan sulfate; heparan sulfate; heparin; inflammation; oxidation of elastase inhibitors

Indexed keywords

CHONDROITIN 4 SULFATE; CHONDROITIN 6 SULFATE; DERMATAN SULFATE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; LEUKOCYTE ELASTASE; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR;

EID: 0030910018     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1997.272.3.l533     Document Type: Article
Times cited : (25)

References (35)
  • 1
    • 0028064657 scopus 로고
    • Oxidized mucus proteinase inhibitor: A fairly potent neutrophil elastase inhibitor
    • Boudier, C., and J. G. Bieth. Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor. Biochem. J. 303: 61-68, 1994.
    • (1994) Biochem. J. , vol.303 , pp. 61-68
    • Boudier, C.1    Bieth, J.G.2
  • 2
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin, M.-C., and U. Lindahl. Glycosaminoglycans and the regulation of blood coagulation. Biochem. J. 289: 313-330, 1993.
    • (1993) Biochem. J. , vol.289 , pp. 313-330
    • Bourin, M.-C.1    Lindahl, U.2
  • 3
    • 0019258204 scopus 로고
    • Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants
    • Carp, H., and A. Janoff. Inactivation of bronchial mucous proteinase inhibitor by cigarette smoke and phagocyte-derived oxidants. Exp. Lung Res. 1: 225-237, 1980.
    • (1980) Exp. Lung Res. , vol.1 , pp. 225-237
    • Carp, H.1    Janoff, A.2
  • 4
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu, B., M. Petitou, M. Provasoli, and P. Sinaÿ. Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13: 221-225, 1988.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinaÿ, P.4
  • 5
    • 0029055476 scopus 로고
    • Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils
    • Domigan, N. M., T. S. Charlton, M. W. Duncan, C. C. Winterbourn, and A. J. Kettle. Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J. Biol. Chem. 270: 16542-16548, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16542-16548
    • Domigan, N.M.1    Charlton, T.S.2    Duncan, M.W.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 6
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6: 1948-1954, 1967.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 7
    • 0025274374 scopus 로고
    • Location of the protease-inhibitory region of secretory leukocyte protease inhibitor
    • Eisenberg, S. P., K. K. Hale, P. Heimdal, and R. C. Thompson. Location of the protease-inhibitory region of secretory leukocyte protease inhibitor. J. Biol. Chem. 265: 7976-7981, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7976-7981
    • Eisenberg, S.P.1    Hale, K.K.2    Heimdal, P.3    Thompson, R.C.4
  • 8
    • 0026657360 scopus 로고
    • Heparin-induced conformational change and activation of mucus proteinase inhibitor
    • Faller, B., Y. Mely, D. Gerard, and J. G. Bieth. Heparin-induced conformational change and activation of mucus proteinase inhibitor. Biochemistry 31: 8285-8290, 1992.
    • (1992) Biochemistry , vol.31 , pp. 8285-8290
    • Faller, B.1    Mely, Y.2    Gerard, D.3    Bieth, J.G.4
  • 9
    • 0023890859 scopus 로고
    • Human mucus proteinase inhibitor (human MPI)
    • Fritz, H. Human mucus proteinase inhibitor (human MPI). Biol. Chem. Hoppe-Seyler Suppl. 369: 79-82, 1988.
    • (1988) Biol. Chem. Hoppe-Seyler Suppl. , vol.369 , pp. 79-82
    • Fritz, H.1
  • 11
    • 0020314265 scopus 로고
    • Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin
    • Griffith, M. J. Kinetics of the heparin-enhanced antithrombin III/thrombin reaction. Evidence for a template model for the mechanism of action of heparin. J. Biol Chem. 257: 7360-7365, 1982.
    • (1982) J. Biol Chem. , vol.257 , pp. 7360-7365
    • Griffith, M.J.1
  • 12
    • 0040469390 scopus 로고
    • The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine α-chymotrypsin
    • Grütter, M. G., G. Fendrich, R. Huber, and W. Bode. The 2.5 Å X-ray crystal structure of the acid-stable proteinase inhibitor from human mucous secretions analysed in its complex with bovine α-chymotrypsin. EMBO J. 7: 345-351, 1988.
    • (1988) EMBO J. , vol.7 , pp. 345-351
    • Grütter, M.G.1    Fendrich, G.2    Huber, R.3    Bode, W.4
  • 13
    • 0028360823 scopus 로고
    • A procedure for quantitative determination of tris(2-carboxyethyl) phosphine, an odorless reducing agent more stable and effective than dithiothreitol
    • Han, J. C., and G. Y. Han. A procedure for quantitative determination of tris(2-carboxyethyl) phosphine, an odorless reducing agent more stable and effective than dithiothreitol. Anal. Biochem. 220: 5-10, 1994.
    • (1994) Anal. Biochem. , vol.220 , pp. 5-10
    • Han, J.C.1    Han, G.Y.2
  • 14
    • 0025943193 scopus 로고
    • Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP)
    • Heinzel-Wieland, R., G. J. Steffens, and L. Flohé. Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP). Biomed. Biochim. Acta 50: 677-681, 1991.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 677-681
    • Heinzel-Wieland, R.1    Steffens, G.J.2    Flohé, L.3
  • 15
    • 0025847743 scopus 로고
    • Glycosaminoglycans: Molecular properties, protein interactions, and role in physiological processes
    • Jackson, R. L., S. J. Busch, and A. D. Cardin. Glycosaminoglycans: molecular properties, protein interactions, and role in physiological processes. Physiol. Rev. 71: 481-539, 1991.
    • (1991) Physiol. Rev. , vol.71 , pp. 481-539
    • Jackson, R.L.1    Busch, S.J.2    Cardin, A.D.3
  • 16
    • 0027132418 scopus 로고
    • Secretory leucocyte proteinase inhibitor is produced by human articular cartilage chondrocytes and intervertebral disc fibrochondrocytes
    • Jacoby, A. S., J. Melrose, B. G. Robinson, V. J. Hyland, and P. Ghosh. Secretory leucocyte proteinase inhibitor is produced by human articular cartilage chondrocytes and intervertebral disc fibrochondrocytes. Eur. J. Biochem. 218: 951-957, 1993.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 951-957
    • Jacoby, A.S.1    Melrose, J.2    Robinson, B.G.3    Hyland, V.J.4    Ghosh, P.5
  • 17
    • 0021941090 scopus 로고
    • Elastase in tissue injury
    • Janoff, A. Elastase in tissue injury. Annu. Rev. Med. 36: 207-216, 1985.
    • (1985) Annu. Rev. Med. , vol.36 , pp. 207-216
    • Janoff, A.1
  • 18
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellén, L., and U. Lindahl. Proteoglycans: structures and interactions. Annu. Rev. Biochem. 60: 443-475, 1991.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellén, L.1    Lindahl, U.2
  • 19
    • 0023887196 scopus 로고
    • Interaction among stimulated human polymorphonuclear leucocytes, released elastase and bronchial antileucoprotease
    • Kramps, J. A., C. van Twisk, E. C. Klasen, and J. H. Dijkman. Interaction among stimulated human polymorphonuclear leucocytes, released elastase and bronchial antileucoprotease. Clin. Sci. Lond. 75: 53-62, 1988.
    • (1988) Clin. Sci. Lond. , vol.75 , pp. 53-62
    • Kramps, J.A.1    Van Twisk, C.2    Klasen, E.C.3    Dijkman, J.H.4
  • 21
    • 0027495712 scopus 로고
    • Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis
    • McElvaney, N. G., B. Doujaiji, M. J. Moan, M. R. Burnham, M. C. Wu, and R. G. Crystal. Pharmacokinetics of recombinant secretory leukoprotease inhibitor aerosolized to normals and individuals with cystic fibrosis. Am. Rev. Respir. Dis. 148: 1056-1060, 1993.
    • (1993) Am. Rev. Respir. Dis. , vol.148 , pp. 1056-1060
    • McElvaney, N.G.1    Doujaiji, B.2    Moan, M.J.3    Burnham, M.R.4    Wu, M.C.5    Crystal, R.G.6
  • 22
    • 0028961396 scopus 로고
    • Mapping the heparin-binding site of mucus proteinase inhibitor
    • Mellt, P., J. Ermolieff, and J. G. Bieth. Mapping the heparin-binding site of mucus proteinase inhibitor. Biochemistry 34: 2645-2652, 1995.
    • (1995) Biochemistry , vol.34 , pp. 2645-2652
    • Mellt, P.1    Ermolieff, J.2    Bieth, J.G.3
  • 23
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5 to 35°
    • Morris, J. C. The acid ionization constant of HOCl from 5 to 35°. J. Phys. Chem. 70: 3798-3805, 1966.
    • (1966) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 24
    • 0026451068 scopus 로고
    • Proteinase/proteinase inhibitor imbalance in sputum sol phases from patients with chronic obstructive pulmonary disease. Suggestion for a key role played by antileukoprotease
    • Piccioni, P. D., J. A. Kramps, A. Rudolphus, A. Bulgheroni, and M. Luisetti. Proteinase/proteinase inhibitor imbalance in sputum sol phases from patients with chronic obstructive pulmonary disease. Suggestion for a key role played by antileukoprotease. Chest 102: 1470-1476, 1992.
    • (1992) Chest , vol.102 , pp. 1470-1476
    • Piccioni, P.D.1    Kramps, J.A.2    Rudolphus, A.3    Bulgheroni, A.4    Luisetti, M.5
  • 25
    • 0023094302 scopus 로고
    • Ozone effects on inhibitors of human neutrophil proteinases
    • Smith, C. E., M. S. Stack, and D. A. Johnson. Ozone effects on inhibitors of human neutrophil proteinases. Arch. Biochem. Biophys. 253: 146-155, 1987.
    • (1987) Arch. Biochem. Biophys. , vol.253 , pp. 146-155
    • Smith, C.E.1    Stack, M.S.2    Johnson, D.A.3
  • 28
    • 0026029117 scopus 로고
    • Anti-neutrophil elastase defense of the normal respiratory epithelial surface provided by the secretory leukoprotease inhibitor
    • Vogelmeier, C., R. C. Hubbard, G. A. Fells, H.-P. Schnebli, R. C. Thompson, H. Fritz, and R. G. Crystal. Anti-neutrophil elastase defense of the normal respiratory epithelial surface provided by the secretory leukoprotease inhibitor. J. Clin. Invest. 87: 482-488, 1991.
    • (1991) J. Clin. Invest. , vol.87 , pp. 482-488
    • Vogelmeier, C.1    Hubbard, R.C.2    Fells, G.A.3    Schnebli, H.-P.4    Thompson, R.C.5    Fritz, H.6    Crystal, R.G.7
  • 29
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • Weiss, S. J., R. Klein, A. Slivka, and M. Wei. Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation. J. Clin. Invest. 70: 598-607, 1982.
    • (1982) J. Clin. Invest. , vol.70 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 32
    • 0028199929 scopus 로고
    • Functions of the N-terminal domain of secretory leukoprotease inhibitor
    • Ying, Q.-L., M. Kemme, and S. R. Simon. Functions of the N-terminal domain of secretory leukoprotease inhibitor. Biochemistry 33: 5445-5450, 1994.
    • (1994) Biochemistry , vol.33 , pp. 5445-5450
    • Ying, Q.-L.1    Kemme, M.2    Simon, S.R.3
  • 33
    • 0030215480 scopus 로고    scopus 로고
    • 1-proteinase inhibitor and accelerates inhibition by secretory leukoprotease inhibitor
    • 1-proteinase inhibitor and accelerates inhibition by secretory leukoprotease inhibitor. Am. J. Respir. Cell Mol. Biol. 15: 283-291, 1996.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 283-291
    • Ying, Q.-L.1    Kemme, M.2    Simon, S.R.3
  • 34
    • 0029556790 scopus 로고
    • Accelerated binding of secretory leukoprotease inhibitor to human leukocyte elastase mediated by single stranded sites in DNA from tracheobronchial mucus
    • Ying, Q.-L., and S. R. Simon. Accelerated binding of secretory leukoprotease inhibitor to human leukocyte elastase mediated by single stranded sites in DNA from tracheobronchial mucus. Am. J. Respir. Cell Mol. Biol. 13: 703-711, 1995.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.13 , pp. 703-711
    • Ying, Q.-L.1    Simon, S.R.2
  • 35
    • 0021840561 scopus 로고
    • Apossible origin of chemiluminescence in phagocytosing neutrophils. Myeloperoxidase-mediated chlorination of proteins and tryptophan
    • Zgliczynski, J. M., E. Olszowska, S. Olszowski, T. Stelmaszynska, and E. Kwasnowska. Apossible origin of chemiluminescence in phagocytosing neutrophils. Myeloperoxidase-mediated chlorination of proteins and tryptophan. Int. J. Biochem. 17: 393-397, 1985.
    • (1985) Int. J. Biochem. , vol.17 , pp. 393-397
    • Zgliczynski, J.M.1    Olszowska, E.2    Olszowski, S.3    Stelmaszynska, T.4    Kwasnowska, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.