Inactivation of alpha(2)-Macroglobulin by Activated Human Polymorphonuclear Leukocytes.

[en] The proteolytic activity of trypsin releases the dye Remazol Brilliant Blue from its high molecular weight substrate, the skin powder (Hide Powder Azure, Sigma), with an increase in absorbance at 595 nm. Active alpha(2)- macroglobulin (80 mug/ml) totally inhibits the proteolytic activity of trypsin (14 mug/ml) by trapping this protease. But after a 20 min incubation of alpha(2)-macroglobulin at 37 degrees C with 2 x 10(6) human polymorphonuclear leukocytes activated by N-formyl-L-methionyl-L-leucyl-L-phenylalanine (10(-7) M) and cytochalasin B (10(-8) M), 100% of trypsin activity was recovered, indicating a total inactivation of alpha(2)-macroglobuHn. Incubation with granulocyte myeloperoxidase also inactivates alpha(2)-macroglobulin. Hypochlorous acid, a by-product of myeloperoxidase activity, at a concentration of 10(-7) M also inactivates alpha(2)-macroglobulin, which indicates that an important cause of alpha(2)-macroglobulin inactivation by activated polymorphonuclear leukocytes could be the activity of myeloperoxidase.

Disciplines :

Anesthesia & intensive care
Human health sciences: Multidisciplinary, general & others

Author, co-author :

Deby, Ginette ; Université de Liège - ULiège > Centre de l'oxygène : Recherche et développement (C.O.R.D.)

Croisier, Jean-Louis ; Université de Liège - ULiège > Département des sciences de la motricité > Kinésithérapie générale et réadaptation

Camus, Gérard

Brumioul, D.

Mathy-Hartert, M.; Université de Liège - ULiège > Département des sciences de la santé publique > Immunohématologie - Transfusion

Sondag, Danièle ; Université de Liège - ULiège > Département des sciences cliniques > Département des sciences cliniques

Deby, C.

Lamy, Maurice

Language :

English

Title :

Inactivation of alpha(2)-Macroglobulin by Activated Human Polymorphonuclear Leukocytes.

Publication date :

1994

Journal title :

Mediators of Inflammation

ISSN :

0962-9351

eISSN :

1466-1861

Publisher :

Hindawi Publishing Corporation, Sylvania, United States - Ohio

Volume :

Issue :

Pages :

117-23

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 25 March 2009

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Bibliography

Babior BM, Kipnes RS, Curnutte JT. Biological defense mechanisms: the production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 1973 52: 741–744.
Henson PM, Henson JE, Fittschen C, Kimani G, Bratton DL, Riches DWH. Phagocytic cells: degranulation and secretion. In: Gallin I, Goldstein IM, Snyderman R, eds. Inflammation: Basic Principles and Clinical Correlates, New York: Raven Press, 1988; 362–390.
Klebanoff SJ. Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J Bacteriol 1968; 95: 2131–2138.
Weiss SJ, Lampert MB, Test ST. Long-lived oxidants generated by human neutrophils: characterization and bioactivity. Science 1983; 222: 62 628.
Weiss SJ. Tissue destruction by neutrophils. New Engl J Med 1989; 320: 365–376.
Matheson NR, Wong PS, Travis J. Enzymatic inactivation of human-α1-proteinase inhibitor. Biochem Biophys Res Comm 1979; 88: 402–409.
Clark RA, Stone PJ, El Hag AZ, Calore JD, Franzblau C. Myeloperoxidase-catalyzed inactivation of α1-proteinase inhibitor by human neutrophils. J Biol Chem 1981; 256: 3348–3353.
Barrett AJ, Starkey PM. The interaction of α2-M with proteinases. Biochem J 1973; 133: 709–724.
Roberts RC, Hall PK. Specificity of proteinases for the bait region of α2-M. In: Feinman RD, ed. Chemistry and Biology of α2-M, Vol 421. New York: Annals of the New York Academy of Sciences, 1983; 61–68.
Bretaudière P, Tapon-Bretaudière J, Stoops JK. Structure of native α2 M and its transformation to the protease bound form. Proc Natl Acad Sci USA. 1988; 85: 1437–1441.
Sottrup-Jensen L, Lonblad PB, Stepanik TM, Petersen TE, Magnusson S, Jornvall H. Primary structure of the ‘bait’ region for proteinases in α2-macroglobulin. FEBS Lett 1981; 127: 167–173.
Debanne MT, Beel R, Dolovich J. Uptake of proteinase-α2 M complexes by macrophages. Biochem Biophys Acta 1975; 411: 295–304.
Bieth JG, Kandel M, Zreika M. Interaction of protein substrate and inhibitors with α2-M-bound proteinase. In: Feinman RD, ed. Chemistry and Biology of α2-M, Vol 421. New York: Annals of the New York Academy of Sciences, 1983; 209–217.
Barrett AJ, Brown AA, Sayers CA. The electrophoretically slow and fast forms of the α2-macroglobulin molecule. Biochem J 1979; 181: 401–418.
Steinbuch M, Pejaudier L, Quentin M, Martin V. Molecular alteration of α2- macroglobulin by aliphatic amines. Biochem Biophys Acta 1968; 154: 228–231.
Reddy VY, Pizzo SV, Weiss SJ. Functional inactivation and structural disruption of human α2-macroglobulin by neutrophils and eosinophils. J Biol Chem 1989; 264: 13801–13809.
Chase T, Shaw E. p-Nitrophenyl-p-guanidinbenzoate HCl: a new active site titrant for trypsin. Biochem Biophys Res Commun 1967; 29: 508–514.
Borgeat P, Samuelsson B. Arachidonic acid metabolism in polymorphonuclear leucocytes: effects of ionophore A23187. Proc Natl Acad Sci USA 1979; 76: 2148–2152.
Badwey JA, Curnutte JT, Karnovsky ML. Cis-polyunsaturated fatty acids induce high levels of superoxide production by human neutrophils. J Biol Chem 1981; 256: 12640–12643.
Cullman W, Dick W. A chromogenic assay for evaluation of α2-macroglobulin level in serum and cerebrospinal fluid. J Clin Chem Clin Biochem 1981; 19: 287–290.
Bakkenist ARJ, Wever R, Vulsma T, Plat H, Van Gelder F. Isolation procedure and some properties of myeloperoxidase from human leukocytes. Biochim Biophys Acta 1978; 524: 45–54.
Deby-Dupont G, Pincemail J, Thirion A, Deby C, Lamy M, Franchimont P. Selflabeling of human polymorphonuclear leucocyte myeloperoxidase with 125iodine. Experientia 1991; 47: 952–957.
Swenson RP, Howard JB. Characterization of alkylamine-sensitive site in α2- macroglobulin. Proc Natl Acad Sci 1979; 76: 4313–4316.
Kassell B. Trypsin and chymotrypsin inhibitors from soybeans. In: Lorand L, ed. Methods in Enzymology, Vol 19. New York: Academic Press. 1970: 853–862.
Hubbard Wj, Hess AD, Hsia S, Amos DB. The effects of electrophoretically ‘slow’ and ‘fast’ α2-macroglobulin on mixed lymphocyte cultures. J Immunol 1981; 126: 292–299.
Root RK, Metcalf JA. H202 release from human granulocytes during phagocytosis: relationship to superoxide anion formation and cellular catabolism of H202: studies with normal and cytochalasin B treated cells, J Clin Invest 1977; 60: 1266–1279.
Bakkenist ARJ, De Boer JEG, Plat H, Wever R. The halide complexes of myeloperoxidase and the mechanism of the halogenation reactions. Biochim Biophys Acta 1980; 613: 337–348.
Thomas EL, Grisham MB, Melton DF, Jefferson MM. Evidence for a role of taurine in the in vitro oxidative toxicity of neutrophils towards erythrocytes. J Biol Chem 1985; 260: 3321–3329.
Kellogg EW, Fridovich I. Superoxide, hydrogen peroxide and singlet oxygen in lipid peroxidation by a xanthine oxidase system. J Biol Chem 1975; 250: 8812–8817.
Larsson LJ, Holmgren A, Medstrod B, Lindblom T, Björk I. Subunits of α2- macroglobulin produced by specific reduction of interchain disulfide bonds with thioredoxin. Biochemistry 1988; 27: 983–991.
Moncino MD, Roche PA, Pizzo SV. Characterization of human α2-macroglobulin monomers obtained by reduction with dithiothreitol. Biochemistry 1991; 30: 1545— 1551.
Warren JS, Warp PA, Johnson KJ. Mechanisms of damage to pulmonary endothelium. In: Ryan US, ed. Pulmonary Endothelium in Health and Disease, Vol 32. New York: Marcel Dekker, 1987; 107–120.
Vercellotti M. Role of neutrophils in endothelial injury. In: Bihari DJ, Cerra FB, eds. Multiple Organ Failure, Vol 5. Fullerton: The Society of Critical Care, 1990; 77–91.
Pincemail J, Deby-Dupont G, Lamy M. Role of neutrophils in critically ill patients: myeloperoxidase, a specific marker of their activation. In: Vincent JL, ed. Update in Intensive Care and Emergency Medicine, Vol 8. Berlin: Springer-Verlag, 1989; 24–32.