Identification of interleukin-8 converting enzyme as cathepsin L

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1649, Issue 1, 2003, Pages 30-39

  Ohashi, Kensaku ^a,c   Naruto, Masanobu ^a   Nakaki, Toshio ^b   Sano, Emiko ^a  

^a TORAY INDUSTRIES INC   (Japan)

^b TEIKYO UNIVERSITY   (Japan)

^c Toray Medical Company   (Japan)

Author keywords

Cathepsin L; Fibroblast; Interleukin 8; Processing

Indexed keywords

AMINO ACID; ARGININE; CATHEPSIN L; DIPEPTIDYL CARBOXYPEPTIDASE; INTERLEUKIN 8; POLYACRYLAMIDE; POLYCLONAL ANTIBODY; SERINE; CATHEPSIN; CYSTEINE PROTEINASE; PROTEIN PRECURSOR;

AMINO TERMINAL SEQUENCE; ARTICLE; CHEMOTAXIS; CHROMATOGRAPHY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME RELEASE; FIBROBLAST CULTURE; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN PROCESSING; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; WESTERN BLOTTING; CELL CULTURE; CULTURE MEDIUM; CYTOLOGY; DRUG EFFECT; ENZYMOLOGY; FIBROBLAST; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; ISOLATION AND PURIFICATION; LIVER; METABOLISM; METHODOLOGY; NEUTROPHIL;

BLOTTING, WESTERN; CATHEPSINS; CELLS, CULTURED; CHEMOTAXIS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CULTURE MEDIA; CYSTEINE ENDOPEPTIDASES; FIBROBLASTS; HUMANS; INTERLEUKIN-8; LIVER; NEUTROPHILS; PROTEIN PRECURSORS; PROTEIN PROCESSING, POST-TRANSLATIONAL;

EID: 0041620473     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00152-3     Document Type: Article

References (54)

1. Yoshimura T., Matsushima K., Tanaka S., Robinson E.A., Appella E., Oppenheim J.J., Leonard E.J. Purification of a human monocyte-derived neutrophil chemotactic factor that has peptide sequence similarity to other host defense cytokines. Proc. Natl. Acad. Sci. U. S. A. 84:1987;9233-9237.
2. Schroder J.M., Mrowietz U., Morita E., Christophers E. Purification and partial biochemical characterization of a human monocyte-derived, neutrophil-activating peptide that lacks interleukin 1 activity. J. Immunol. 139:1987;3474-3483.
3. Walz A., Peveri P., Aschauer H., Baggiolini M. Purification and amino acid sequencing of NAF, a novel neutrophil-activating factor produced by monocytes. Biochem. Biophys. Res. Commun. 149:1987;755-761.
4. Matsushima K., Morishita K., Yoshimura T., Lavu S., Kobayashi Y., Lew W., Appella E., Kung H.F., Leonard E.J., Oppenheim J.J. Molecular cloning of a human monocyte-derived neutrophil chemotactic factor (MDNCF) and the induction of MDNCF mRNA by interleukin 1 and tumor necrosis factor. J. Exp. Med. 167:1988;1883-1893.
5. Schroder J.M., Sticherling M., Henneicke H.H., Preissner W.C., Christophers E. IL-1 alpha or tumor necrosis factor-alpha stimulate release of three NAP-1/IL-8-related neutrophil chemotactic proteins in human dermal fibroblasts. J. Immunol. 144:1990;2223-2232.
6. Van Damme J., Decock B., Conings R., Lenaerts J.P., Opdenakker G., Billiau A. The chemotactic activity for granulocytes produced by virally infected fibroblasts is identical to monocyte-derived interleukin 8. Eur. J. Immunol. 19:1989;1189-1194.
7. Nakagawa H., Hatakeyama S., Ikesue A., Miyai H. Generation of interleukin-8 by plasmin from AVLPR-interleukin-8, the human fibroblast-derived neutrophil chemotactic factor. FEBS Lett. 282:1991;412-414.
8. Elner V.M., Strieter R.M., Elner S.G., Baggiolini M., Lindley I., Kunkel S.L. Neutrophil chemotactic factor (IL-8) gene expression by cytokine-treated retinal pigment epithelial cells. Am. J. Pathol. 136:1990;745-750.
9. Standiford T.J., Kunkel S.L., Basha M.A., Chensue S.W., Lynch J.P. III, Toews G.B., Westwick J., Strieter R.M. Interleukin-8 gene expression by a pulmonary epithelial cell line. A model for cytokine networks in the lung. J. Clin. Invest. 86:1990;1945-1953.
10. Kupper T.S. The activated keratinocyte: a model for inducible cytokine production by non-bone marrow-derived cells in cutaneous inflammatory and immune responses. J. Invest. Dermatol. 94:1990;146S-150S.
11. Larsen C.G., Anderson A.O., Oppenheim J.J., Matsushima K. Production of interleukin-8 by human dermal fibroblasts and keratinocytes in response to interleukin-1 or tumour necrosis factor. Immunology. 68:1989;31-36.
12. Gregory H., Young J., Schroder J.M., Mrowietz U., Christophers E. Structure determination of a human lymphocyte derived neutrophil activating peptide (LYNAP). Biochem. Biophys. Res. Commun. 151:1988;883-890.
13. Bazzoni F., Cassatella M.A., Rossi F., Ceska M., Dewald B., Baggiolini M. Phagocytosing neutrophils produce and release high amounts of the neutrophil-activating peptide 1/interleukin 8. J. Exp. Med. 173:1991;771-774.
14. Strieter R.M., Kasahara K., Allen R., Showell H.J., Standiford T.J., Kunkel S.L. Human neutrophils exhibit disparate chemotactic factor gene expression. Biochem. Biophys. Res. Commun. 173:1990;725-730.
15. Strieter R.M., Kunkel S.L., Showell H.J., Marks R.M. Monokine-induced gene expression of a human endothelial cell-derived neutrophil chemotactic factor. Biochem. Biophys. Res. Commun. 156:1988;1340-1345.
16. Gimbrone M.A. Jr., Obin M.S., Brock A.F., Luis E.A., Hass P.E., Hebert C.A., Yip Y.K., Leung D.W., Lowe D.G., Kohr W.J.et al. Endothelial interleukin-8: a novel inhibitor of leukocyte-endothelial interactions. Science. 246:1989;1601-1603.
17. Schroder J.M., Christophers E. Secretion of novel and homologous neutrophil-activating peptides by LPS-stimulated human endothelial cells. J. Immunol. 142:1989;244-251.
18. Beaubien B.C., Collins P.D., Jose P.J., Totty N.F., Hsuan J., Waterfield M.D., Williams T.J. A novel neutrophil chemoattractant generated during an inflammatory reaction in the rabbit peritoneal cavity in vivo. Purification, partial amino acid sequence and structural relationship to interleukin 8. Biochem. J. 271:1990;797-801.
19. Collins P.D., Jose P.J., Williams T.J. The sequential generation of neutrophil chemoattractant proteins in acute inflammation in the rabbit in vivo. Relationship between C5a and proteins with the characteristics of IL-8/neutrophil-activating protein 1. J. Immunol. 146:1991;677-684.
20. Jose P.J., Collins P.D., Perkins J.A., Beaubien B.C., Totty N.F., Waterfield M.D., Hsuan J., Williams T.J. Identification of a second neutrophil-chemoattractant cytokine generated during an inflammatory reaction in the rabbit peritoneal cavity in vivo. Purification, partial amino acid sequence and structural relationship to melanoma-growth-stimulatory activity. Biochem. J. 278:1991;493-497.
21. 2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity. J. Exp. Med. 167:1988;1364-1376.
22. Thelen M., Peveri P., Kernen P., von Tscharner V., Walz A., Baggiolini M. Mechanism of neutrophil activation by NAF, a novel monocyte-derived peptide agonist. FASEB J. 2:1988;2702-2706.
23. Willems J., Joniau M., Cinque S., van Damme J. Human granulocyte chemotactic peptide (IL-8) as a specific neutrophil degranulator: comparison with other monokines. Immunology. 67:1989;540-542.
24. Smith W.B., Gamble J.R., Clark-Lewis I., Vadas M.A. Interleukin-8 induces neutrophil transendothelial migration. Immunology. 72:1991;65-72.
25. Peveri P., Walz A., Dewald B., Baggiolini M. A novel neutrophil- activating factor produced by human mononuclear phagocytes. J. Exp. Med. 167:1988;1547-1559.
26. Leonard E.J., Yoshimura T., Tanaka S., Raffeld M. Neutrophil recruitment by intradermally injected neutrophil attractant/activation protein-1. J. Invest. Dermatol. 96:1991;690-694.
27. Swensson O., Schubert C., Christophers E., Schroder J.M. Inflammatory properties of neutrophil-activating protein-1/interleukin 8 (NAP-1/IL-8) in human skin: a light- and electronmicroscopic study. J. Invest. Dermatol. 96:1991;682-689.
28. Foster S.J., Aked D.M., Schroder J.M., Christophers E. Acute inflammatory effects of a monocyte-derived neutrophil-activating peptide in rabbit skin. Immunology. 67:1989;181-183.
29. Colditz I., Zwahlen R., Dewald B., Baggiolini M. In vivo inflammatory activity of neutrophil-activating factor, a novel chemotactic peptide derived from human monocytes. Am. J. Pathol. 134:1989;755-760.
30. Rampart M., Van Damme J., Zonnekeyn L., Herman A.G. Granulocyte chemotactic protein/interleukin-8 induces plasma leakage and neutrophil accumulation in rabbit skin. Am. J. Pathol. 135:1989;21-25.
31. 2- terminal amino acid sequence identity with melanoma growth stimulatory activity. J. Exp. Med. 171:1990;1091-1100.
32. Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:1987;368-379.
33. Yoshimura T., Robinson E.A., Appella E., Matsushima K., Showalter S.D., Skeel A., Leonard E.J. Three forms of monocyte-derived neutrophil chemotactic factor (MDNCF) distinguished by different lengths of the amino-terminal sequence. Mol. Immunol. 26:1989;87-93.
34. Van Damme J., Van Beeumen J., Conings R., Decock B., Billiau A. Purification of granulocyte chemotactic peptide/interleukin-8 reveals N-terminal sequence heterogeneity similar to that of beta-thromboglobulin. Eur. J. Biochem. 181:1989;337-344.
35. 2- terminally processed forms. Eur. J. Immunol. 20:1990;2113-2118.
36. Hebert C.A., Luscinskas F.W., Kiely J.M., Luis E.A., Darbonne W.C., Bennett G.L., Liu C.C., Obin M.S., Gimbrone M.A. Jr., Baker J.B. Endothelial and leukocyte forms of IL-8. Conversion by thrombin and interactions with neutrophils. J. Immunol. 145:1990;3033-3040.
37. Padrines M., Wolf M., Walz A., Baggiolini M. Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett. 352:1994;231-235.
38. McDonald J.K., Kadkhodayan S. Cathepsin L - a latent proteinase in guinea pig sperm. Biochem. Biophys. Res. Commun. 151:1988;827-835.
39. Sano E., Iizuka M., Kobayashi S. Effect of glucocorticoid hormones on growth of human fibroblast cells and interferon production in a microcarrier culture system. Cell Struct. Funct. 12:1987;509-517.
40. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
41. Eggleton P., Gargan R., Fisher D. Rapid method for the isolation of neutrophils in high yield without the use of dextran or density gradient polymers. J. Immunol. Methods. 121:1989;105-113.
42. Joseph L., Lapid S., Sukhatme V. The major ras induced protein in NIH3T3 cells is cathepsin L. Nucleic Acids Res. 15:1987;3186.
43. Nishimura Y., Furuno K., Kato K. Biosynthesis and processing of lysosomal cathepsin L in primary cultures of rat hepatocytes. Arch. Biochem. Biophys. 263:1988;107-116.
44. Nishimura Y., Kawabata T., Kato K. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys. 261:1988;64-71.
45. Smith S.M., Gottesman M.M. Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli. J. Biol. Chem. 264:1989;20487-20495.
46. Barrett A.J., Davies M.E., Grubb A. The place of human gamma-trace (cystatin C) amongst the cysteine proteinase inhibitors. Biochem. Biophys. Res. Commun. 120:1984;631-636.
47. Hansen T., Petrow P.K., Gaumann A., Keyszer G.M., Eysel P., Eckardt A., Brauer R., Kriegsmann J. Cathepsin B and its endogenous inhibitor cystatin C in rheumatoid arthritis synovium. J. Rheumatol. 27:2000;859-865.
48. Mason R.W., Walker J.E., Northrop F.D. The N-terminal amino acid sequences of the heavy and light chains of human cathepsin L. Relationship to a cDNA clone for a major cysteine proteinase from a mouse macrophage cell line. Biochem. J. 240:1986;373-377.
49. Nishimura Y., Kawabata T., Furuno K., Kato K. Evidence that aspartic proteinase is involved in the proteolytic processing event of procathepsin L in lysosomes. Arch. Biochem. Biophys. 271:1989;400-406.
50. Nishimura Y., Kawabata T., Yano S., Kato K. Inhibition of intracellular sorting and processing of lysosomal cathepsins H and L at reduced temperature in primary cultures of rat hepatocytes. Arch. Biochem. Biophys. 283:1990;458-463.
51. Hara K., Kominami E., Katunuma N. Effect of proteinase inhibitors on intracellular processing of cathepsin B, H and L in rat macrophages. FEBS Lett. 231:1988;229-231.
52. Kirschke H., Barrett A.J., Rawlings N.D. Proteinases 1: lysosomal cysteine proteinases. Protein Profile. 2:1995;1581-1643.
53. Mason R.W., Gal S., Gottesman M.M. The identification of the major excreted protein (MEP) from a transformed mouse fibroblast cell line as a catalytically active precursor form of cathepsin L. Biochem. J. 248:1987;449-454.
54. Lemaire R., Huet G., Zerimech F., Grard G., Fontaine C., Duquesnoy B., Flipo R.M. Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br. J. Rheumatol. 36:1997;735-743.