A secreted proform of neutrophil proteinase 3 regulates the proliferation of granulopoietic progenitor cells

Blood

Volumn 93, Issue 3, 1999, Pages 849-856

  Sköld, Stefan ^a   Rosberg, Bodil ^a   Gullberg, Urban ^a   Olofsson, Tor ^a  

^a LUND UNIVERSITY HOSPITAL   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN G; CD34 ANTIGEN; CYANOGEN BROMIDE; ELASTASE; GRANULOCYTE COLONY STIMULATING FACTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; MYELOBLASTIN; SERINE PROTEINASE INHIBITOR;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL CYCLE S PHASE; CELL PROLIFERATION; CELL STRAIN HL 60; COLONY FORMING UNIT GM; CONTROLLED STUDY; ENZYME RELEASE; GRANULOPOIESIS; HEMATOPOIETIC STEM CELL; HUMAN; HUMAN CELL; IMMUNOBLOTTING; IMMUNOPRECIPITATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; RAT;

EID: 17144468862     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v93.3.849     Document Type: Article

References (38)

1. Olofsson T, Olsson I: Suppression of normal granulopoiesis in vitro by a leukemia associated inhibitor (LAI) of acute and chronic leukemia. Blood 55:975, 1980
2. Olofsson T, Olsson I: Biochemical characterization of a leukemia associated inhibitor (LAI) suppressing normal granulopoiesis in vitro. Blood 55:983, 1980
3. Olofsson T, Olsson I: Suppression of normal granulopoiesis in vitro by a leukemia associated inhibitor (LAI) derived from a human promyelocytic cell line (HL-60). Leuk Res 4:437, 1980
4. Olofsson T, Nilsson E, Olsson I: Characterization of the cells in myeloid leukemia that produce leukemia associated inhibitor (LAI) and demonstration of LAI-producing cells in normal bone marrow. Leuk Res 8:387, 1984
5. Olofsson T: Leukemia associated inhibitor (LAI): Biological characterization and purification of the active subunit, in Najman A, Guigon M, Gorin NC, Mary JY (eds): The Inhibitors of Hematopoiesis. Paris, France/London, UK, Colloque INSERM/John Libbey Eurotext, 1987, p 177
6. Gabay JE: Antimicrobial proteins with homology to serine proteases, in Boman HG, Marsh J, Goode JA (eds): Antimicrobial Peptides, vol 186. Ciba Foundation Symposium, Chichester, UK, Wiley, 1994, p 237
7. Gullberg U, Andersson E, Garwicz D, Lindmark A, Olsson J: Biosynthesis, processing, and sorting of neutrophil proteins - Insight into neutrophil granule development. Eur J Haematol 58:137, 1997
8. Borregaard N, Cowland JB: Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 89:3503, 1997
9. Weiss J: Leukocyte-derived antimicrobial proteins. Curr Opin Hematol 1:78, 1994
10. Janoff A: Elastase and emphysema. Current assessment of the protease-antiprotease hypothesis. Am Rev Respir Dis 132:417, 1985
11. Campanelli D, Melchior M, Fu Y, Nakata M, Shuman H, Nathan C, Gabay JE: Cloning of cDNA for proteinase 3: A serine protease, antibiotic, and autoantigen from human neutrophils. J Exp Med 172:1709, 1990
12. Labbaye C, Musette P, Cayre YE: Wegener autoantigen and myeloblastin are encoded by a single mRNA. Proc Natl Acad Sci USA 88:9253, 1991
13. Rao NV, Wehner NG, Marshall BC, Gray WR, Gray BH, Hoidal JR: Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase - structural and functional properties. J Biol Chem 266:9540, 1991
14. Sturrock AB, Franklin KF, Rao GV, Marshall BC, Rebentisch MB, Lemons RS, Hoidal JR: Structure, chromosomal assignment, and expression of the gene for proteinase-3 - The Wegener's granulomatosis autoantigen. J Biol Chem 267:21193, 1992
15. Bainton DF: Developmental biology of neutrophils and eosinophils, in Gallin JI, Goldstein IM, Snyderman R (eds): Inflammation: Basic Principles and Clinical Correlates. New York, NY, Raven, 1992, p 303
16. Owen CA, Campbell MA, Sannes PL, Boukedes SS, Campbell EJ: Cell surface-bound elastase and cathepsin G on human neutrophils: A novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases. J Cell Biol 131:775, 1995
17. Csernok E, Ernst M, Schmitt W, Bainton DF, Gross WL: Activated neutrophils express proteinase 3 on their plasma membrane in vitro and in vivo. Clin Exp Immunol 95:244, 1994
18. Halbwachs-Mecarelli L, Bessou G, Lesarve P, Lopez S, Witko-Sarsat V: Bimodal distribution of proteinase 3 (PR3) surface expression reflects a constitutive heterogeneity in the polymorphonuclear neutro-phil pool. FEBS Lett 374:29, 1995
19. Mfa) and modulates polymorphonuclear leukocyte adhesion. J Exp Med 184:1213, 1996
20. Hasilik A: The early and late processing of lysosomal enzymes: Proteolysis and compartmentation. Experientia 48:130, 1992
21. Lindmark A, Persson A-M, Olsson I: Biosynthesis and processing of cathepsin G and neutrophil elastase in the leukemic myeloid cell line U-937. Blood 76:2374, 1990
22. McGuire MJ, Lipsky PE, Thiele DL: Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I. J Biol Chem 268:2458, 1993
23. Gullberg U, Lindmark A, Nilsson E, Persson A-M, Olsson I: Processing of human cathepsin G after transfection to the rat basophil/ mast cell tumor line RBL. J Biol Chem 269:25219, 1994
24. Rao NV, Rao GV, Marshall BC, Hoidal JR: Biosynthesis and processing of proteinase 3 in U937 cells. Processing pathways are distinct from those of cathepsin G. J Biol Chem 271:2972, 1996
25. Garwicz D, Lindmark A, Hellmark T, Gladh M, Jögi J, Gullberg U: Characterization of the processing and granular targeting of human proteinase 3 after transfection to the rat RBL and the murine 32D leukemic cell lines. J Leukoc Biol 61:113, 1997
26. Tarr GE: Manual Edman sequencing system, in Shively JE (ed): Methods of Protein Microcharacterization. Clifton, NJ, Humana, 1986, p 155
27. Garwicz D, Lindmark A, Gullberg U: Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/ mast cell line RBL or the murine myeloid cell line 32D. J Biol Chem 270:28413, 1995
28. Gullberg U, Lindmark A, Lindgren G, Persson A-M, Nilsson E, Olsson I: Carboxyl terminal prodomain-deleted human leukocyte elastase and cathepsin G are effectively targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL. J Biol Chem 270:12912,1995
29. Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR: Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51,1989
30. Baslund B, Petersen J, Permin H, Wiik A, Wieslander J: Measurements of proteinase 3 and its complexes with α1-antiproteinase inhibitor and anti-neutrophil cytoplasm antibodies (ANCA) in plasma. J Immunol Methods 175:215, 1994
31. Olofsson T, Sallerfors B: Modulation of the production of leukemia associated inhibitor (LAI) and its interaction with granulocyte-macrophage colony-forming cells. Exp Hematol 15:1163, 1987
32. Sinha D, Bakhshi MR, Kirby EP: Complete cDNA sequence of bovine α1-antitrypsin. Biochim Biophys Acta 1130:209, 1992
33. Sun J, Bird CH, Sutton V, McDonald L, Coughlin PB, De Jong TA, Trapani JA, Bird PI: A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. J Biol Chem 271:27802, 1996
34. Salvesen G, Enghild JJ: An unusual specificity in the activation of neutrophil serine proteinase zymogens. Biochemistry 29:5304, 1990
35. Garwicz D, Lindmark A, Persson A-M, Gullberg U: On the role of the proform-conformation for processing and intracellular sorting of human cathepsin G. Blood 92:1425, 1998
36. Fujinaga M, Chernaia MM, Halenbeck R, Koths K, James MNG: The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies. J Mol Biol 261:267, 1996
37. Metcalf D: Hematopoietic regulators: Redundancy or subtlety? Blood 82:3515, 1993
38. Bensinger WI, Price TH, Dale DC, Appelbaum FR, Clift R, Lilleby K, Williams B, Storb R, Thomas ED, Buckner CD: The effects of daily recombinant human granulocyte colony-stimulating factor administration on normal granulocyte donors undergoing leukapheresis. Blood 81:1883, 1993