Protease activity in protein-free NSO myeloma cell cultures

In Vitro Cellular and Developmental Biology - Animal

Volumn 41, Issue 10, 2005, Pages 330-336

  Spens, Erika ^a   Häggström, Lena ^a  

^a ROYAL INSTITUTE OF TECHNOLOGY   (Sweden)

Author keywords

Aprotinin; Cathepsin L; Conditioned medium; Cystatin C; SLPI; Zymography

Indexed keywords

APROTININ; ASPARTIC PROTEINASE; BENZYLOXYCARBONYLPHENYLALANYLARGININE 7 AMIDO 4 METHYLCOUMARIN; BENZYLOXYCARBONYLPHENYLALANYLTYROSINE TERT BUTYL DIMETHYL KETONE; CASEIN; CATHEPSIN; CATHEPSIN L; COUMARIN DERIVATIVE; CYSTATIN C; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; PAPAIN; PROTEINASE; PROTEINASE INHIBITOR; RECOMBINANT ANTIBODY; SECRETORY LEUKOCYTE PROTEINASE INHIBITOR; SERINE PROTEINASE; UNCLASSIFIED DRUG;

ACIDITY; ALKALINITY; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CANCER CELL CULTURE; CELL FREE SYSTEM; CELL GROWTH; CELL PROLIFERATION; CELL STRAIN NS0; CONTROLLED STUDY; CULTURE MEDIUM; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME RELEASE; ENZYME SUBSTRATE; MITOGENESIS; MOLECULAR WEIGHT; MOUSE; MYELOMA CELL; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN FAMILY; ZYMOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ENDOPEPTIDASES; CATHEPSINS; CELL LINE, TUMOR; CELL PROLIFERATION; CULTURE MEDIA; CYSTATINS; CYSTEINE ENDOPEPTIDASES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HYDROGEN-ION CONCENTRATION; MICE; MOLECULAR SEQUENCE DATA; MULTIPLE MYELOMA; PROTEASE INHIBITORS; PROTEINASE INHIBITORY PROTEINS, SECRETORY; PROTEINS; SEQUENCE ANALYSIS, PROTEIN;

ANIMALIA;

EID: 33645019941     PISSN: 10712690     EISSN: None     Source Type: Journal    
DOI: 10.1290/0507047.1     Document Type: Article

References (31)

1. Abe, T.; Tominaga, Y.; Kikuchi, T.; Watanabe, A.; Satoh, K.; Walanabe, Y.; Nukiwa, T. Bacterial pneumonia causes augmented expression of the secretoiy leukoprotease inhibitor gene in the murine lung. Am. J. Respir. Crit. Care Med. 156:1235-1240; 1997.
2. Asami, O.; Nakamura, T.; Mura, T.; Ichihara, A. Identification of trypsin inhibitor in bovine pituitary extracts as a survival factor for adult rat hepatocytes in primary culture. J. Biochem. 95:299-309; 1984.
3. Catalioto, R. M.; Negrel, R.; Gaillard, D.; Ailhaud, G. Growth-promoting activity in serum-free medium of kallikreinlike arginylesteropeptidases from rat submaxillary gland. J. Cell. Physiol. 130:352-360; 1987.
4. Cook, J. R.; Chen, J. K. Enhancement of transformed cell growth in agar by serine protease inhibitors. J. Cell. Physiol 136:188-193; 1988.
5. Davis, H.; Gascho, C.; Kiernan, J. A. Effects of aprotinin on organ cultures of the rat's kidney. In Vitro 12:192-197; 1976.
6. Elliott, P.; Hohmann, A.; Spanos. J. Protease expression in the supernatant of Chinese Hamster Ovary cells grown in serum-free culture. Biotechnol. Lett. 25:1949-1952; 2003.
7. Ellis, K. J.; Morrison. J. F. Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol. 87:405-426; 1982.
8. Fritz, H.; Wunderer, G. Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs. Arzneimittel-Forschung 33:479-494; 1983.
9. Ghetie, V.; Mihaescu, S. The hydrolysis of rabbit immunoglobulin G with purified cathepsins D and E. Immunochemistry 10:251-255; 1973.
10. Hargreaves, P. G,; Wang, E; Antcliff, J.: Murphy, G.; Lawry, J.; Russell, R. G.; Croucher, P. I. Human myeloma cells shed the interleukin-6 receptor: inhibition by tissue inhibitor of metalloprotease-3 and a hydroxamate-based metalloprotease inhibitor, Br. J. Haematol. 101:694-702; 1998.
11. Henriksen, P. A.; Hitt, M.; Xing, Z., et al. Adenoviral gene delivery of elafin and secretory leukocyte protease inhibitor attenuates NF-kappa B-dependent inflammatory responses of human endothelial cells and macrophages to atherogenic stimuli. J. Immunol. 172:4535-4544; 2004.
12. Hewlett, G. Apropos aprotinin: a review. Biotechnology (NY) 8:565-566, 568; 1990.
13. Holen, I.; Drury, N. L.; Hargreaves, P. G.; Croucher, P. I. Evidence of a role for a non-marrix-type metalloprotease activity in the shedding of syndecan-1 from human myeloma cells. Br. J. Haematol. 114:414-421; 2001.
14. Hunt, L. T.; Barker, W. C.; Dayhoff, M. O. Epidermal growth factor: internal duplication and probable relation to pancreatic secretory trypsin inhibitor. Biochem. Biophys. Res. Commun, 60:1020-8; 1974.
15. Ishidoh, K.; Koniinami, E. Gene regulation and extracellular functions of procathepsin L. Biol. Chem. 379:131-135; 1998.
16. Karl, D. W.; Donovan, M.; Flickinger. M. C. A novel acid protease released by hybridoma cells. Cytotechnology 3:157-169; 1990.
17. Kelly, T.; Borset, M.; Abe, E.; Gaddy-Kurten, D.; Sanderson R. D. Matrix metalloproteases in multiple myeloma. Leuk. Lymphoma 37:273-281; 2000.
18. Kirschke, H.; Eerola, R.; Hopsu-Havu, V. K.; Bromme, D.; Vuorio, E. Antisense RNA inhibition ol cathepsin L expression reduces tumorigenicity of malignant cells. Eur. J. Cancer 36:787-795; 2000.
19. Kratje, R. B.; Lind, W.; Wagner, R. Evaluation of the proteolytic potential of in vitro-cultivated hybridoma and recombinant mammalian cells. J. Biotechnol. 32:107-125; 1994.
20. Leber, T. M.; Balkwill, F. R. Zymography: a single-step staining method for quantitation of proteolytic activity on substrate gels. Anal. Biochem. 249:24-28; 1997.
21. Li, F.; An, H.; Seymour, T. A.; Bradford, S.; Morrissey, M. T.; Bailey, G. S.; Helmrich, A.; Barnes, D. W. Molecular cloning, sequence analysis and expression distribution of rainbow trout (Oncorhynchus mykiss) cystatin C. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 121B:135-143; 1998.
22. Nakamura, T.; Asami, O.; Tanaka, K.; Ichihara, A. Increased survival of rat hepatocytes in serum-free medium by inhibition of a trypsin-like protease associated with their plasma membranes. Exp. Cell Res. 155:81-91; 1984.
23. Neurath, H. Evolution of proteolytic enzymes. Science 224:350-357; 1984.
24. Pandiella, A.; Bosenberg, M. W.; Huang, E. J.: Besmer, P.; Massague, J. Cleavage of membrane-anchored growth factors involves distinct protease activities regulated through common mechanisms. J. Biol. Chem. 267:24028-24033; 1992.
25. Schlaeger, E. J.; Eggimann, B.; Gast, A. Proteolytic activity in the culture supernatants of mouse hybridoma cells. Dev. Biol. Stand. 66:403-108; 1987.
26. Solem, M.; Rawson, C.; Lindburg, K.; Barnes, D. Transforming growth factor beta regulates cystatin C in serum-free mouse embryo (SFME) cells. Biochem. Biophys. Res. Commun. 172:945-951; 1990.
27. Spens, E.; Häggström, L. Defined protein-free NSO myeloma cell cultures: stimulation of proliferation by conditioned medium factors. Biotechnol. Prog. 21:87-95; 2005.
28. Tjin, E. P. M.; Derksen, P. W. B.; Kataoka, H.; Spaargaren, M.; Pals, S. T. Multiple myeloma cells catalyze hepatocyte growth factor (HGF) activation by secreting the serine protease HGF-activator. Blood 104:2172-2175; 2004.
29. Turk, B.; Turk, D.; Turk, V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477:98-111; 2000.
30. Van Erp, R.; Adorf, M.; Van Sommeren, A. P. G.; Gribnau, T. C. J. Monitoring of the production of monoclonal antibodies by hybridomas. Part IJ: characterization and purification of acid proteases present in cell culture supernatant. J. Biotechnol. 20:249-261; 1991.
31. Weber, E.; Gunther, D.; Laube, F.; Wiederanders, B.; Kirschke, H. Hybridoma cells producing antibodies to cathepsin L have greatly reduced potential for tumour growth. J. Cancer Res. Clin. Oncol. 120:564-567; 1994.