Production of bioactive salmon calcitonin from the nonendocrine cell lines COS-7 and CHO

Peptides

Volumn 18, Issue 3, 1997, Pages 439-444

  Takahashi, Ken Ichiro ^a   Liu, Yun Cai ^a   Hayashi, Naoki ^a   Goto, Fumio ^a   Kato, Miyuki ^b   Kawashima, Hiroyuki ^b   Takeuchi, Toshiyuki ^a  

^a GUNMA UNIVERSITY   (Japan)

^b ASTELLAS PHARMA INC   (Japan)

Author keywords

Amidation enzyme; CHO; COS 7; Furin; Salmon calcitonin

Indexed keywords

ALPHA AMIDATING ENZYME; CALCITONIN; FURIN; SALCATONIN;

ANIMAL CELL; ARTICLE; CANCER PAIN; CELL LINE; CHO CELL; CHRONIC PAIN; CLONING VECTOR; CONTROLLED STUDY; NONHUMAN; OSTEOPOROSIS; PRIORITY JOURNAL; TERMINAL DISEASE;

ANIMALS; BIOLOGICAL ASSAY; CALCITONIN; CERCOPITHECUS AETHIOPS; CHO CELLS; COS CELLS; CRICETINAE; CULTURE MEDIA, CONDITIONED; DENTIN; GENETIC VECTORS; RECOMBINANT FUSION PROTEINS; SALMON; TRANSFECTION;

ANIMALIA;

EID: 0030917760     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(96)00336-1     Document Type: Article

References (35)

1. Amara S. G., Jonas V., Rosenfeld M. G. Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products. Nature. 298:1982;240-244.
2. Bradbury A. F., Smyth D. G. Biosynthesis of peptide neurotransmitters: Studies on the formation of peptide amides. Physiol. Bohemoslov. 37:1988;267-274.
3. Bradbury A. F., Smyth D. G. Peptide amidation. Trends. Biochem. Sci. 16:1991;112-115.
4. Bravo D. A., Gleason J. B., Sanchez R. I., Roth R. A., Fuller R. S. Accurate and efficient cleavage of the human insulin proreceptor by the human proprotein-processing protease furin. J. Biol. Chem. 269:1994;25830-25837.
5. Breimer L. H., Maclyntyne I., Zaidi M. Peptides from the calcitonin genes: Molecular genetics, structure and function. Biochem. J. 255:1988;377-390.
6. Bonewald L. F., Wakefield L., Oreffo R. O. C., Escobedo A., Twardzik D. R., Mundy G. R. Latent forms of transforming growth factor- β (TGF- β ) derived from bone cultures: Identification of a naturally occurring 100-kDa complex with similarity to recombinant latent TGF- β Mol. Endocrinol. 5:1991;741-751.
7. Candeletti S., Ferri S. Intracerebroventricular salmon calcitonin reduces autotomy behavior in rats after dorsal rhizotomy. Pain. 48:1992;275-278.
8. Colado M. I., Ormazabal M. J., Goicoechea C., Lopez F., Alfaro M. J., Martin M. I. Involvement of central serotonergic pathways in analgesia elicited by salmon calcitonin in the mouse. Eur. J. Pharmacol. 252:1994;291-297.
9. Dickinson C. J., Takeuchi T., Guo Y., Stadler B. T., Yamada T. Expression and processing of prohormones in nonendocrine cells. Am. J. Physiol. 264:1993;G553-G560.
10. Eipper B. A., Mains R. E. Peptide alpha-amidation. Annu. Rev. Physiol. 50:1988;333-344.
11. Fraioli F., Fabbri A., Gnessi L., Moretti C., Santoro C., Felici M. Subarachnoid injection of salmon calcitonin induces analgesia in man. Eur. J. Pharmacol. 78:1982;381-382.
12. Freed W. J., Perlow M. J., Wyatt R. J. Calcitonin: Inhibitory effect on eating in rats. Science. 206:1979;850-852.
13. Fuller R. S., Brake A. J., Thoner J. Intracellular targeting and structural conversion of a prohormone-processing endoprotease. Science. 246:1989;482-486.
14. Gennari C., Chierichetti S. M., Piolini M., Vibelli C., Agnusdei D., Civitelli R., Gonnelli S. Analgesic activity of salmon calcitonin and human calcitonin against cancer pain: A double-blind, placebo-controlled clinical study. Curr. Ther. Res. 38:1985;298-303.
15. Gobelet C., Waldburger M., Meier J. L. The effect of adding calcitonin to physical treatment on reflex sympathetic dystrophy. Pain. 48:1992;171-175.
16. Hatsuzawa K., Hosaka M., Nakagawa T., Nagase M., Shoda A., Murakami K., Nakayama K. Structure and expression of mouse furin, a yeast Kex2-related protease. J. Biol. Chem. 265:1990;22075-22078.
17. Hayashi N., Kayo T., Sugano K., Takeuchi T. Production of bioactive gastrin from the nonendocrine cell lines CHO and COS-7. FEBS Lett. 337:1994;27-32.
18. Hosaka M., Nagahama M., Kim W-S., Watanabe T., Hatsuzawa K., Ikemizu J., Murakami K., Nakayama K. Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266:1991;12127-12130.
19. Jaeger H., Maier C. Calcitonin in phantom limb pain: A double-blind study. Pain. 48:1992;21-27.
20. Komada M., Hatsuzawa K., Shibamoto S., Ito F., Nakayama K., Kitamura N. Proteolytic processing of hepatocyte growth factor/scatter factor receptor by furin. FEBS Lett. 328:1993;25-29.
21. Liu Y-C., Kawagishi M., Mikayama T., Inagaki Y., Takeuchi T., Ohashi H. Processing of a fusion protein by endoprotease in COS-1 cells for secretion of mature peptide by using a chimeric expression vector. Proc. Natl. Acad. Sci. USA. 90:1993;8957-8961.
22. Lucas B. K., Giere L. M., DeMarco R. A., Shen A., Chisholm V., Crowley C. W. High-level production of recombinant proteins in CHO cells using a dicistoronic DHFR intron expression vector. Nucl. Acids Res. 24:1996;1774-1779.
23. Martin M. I., Goicoechea C., Colado M. I., Alfaro M. J. Analgesic effect of salmon-calcitonin administered by two routes. Effect on morphine analgesia. Eur. J. Pharmacol. 224:1992;77-82.
24. Molloy S. S., Bresnahan P. A., Leppla S. H., Klimpel K. R., Thomas G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267:1992;16396-16402.
25. Moore H-P. H., Walker M. D., Lee F., Kelly R. B. Expressing a human proinsulin cDNA in a mouse ACTH-Secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation. Cell. 35:1983;531-538.
26. Pei D., Weiss S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature. 375:1995;244-247.
27. Ray M. V. L., Van Duyne P., Bertelsen A. H., Jackson-Matthews D. E., Sturmer A. M., Merkler D. J., Consalvo A. P., Young S. D., Gilligan J. P., Shields P. P. Production of recombinant salmon calcitonin by in vitro amidation of an Escherichia coli produced precursor peptide. Biotechnology. 11:1993;64-70.
28. Recker R. R. Clinical review 41. Current therapy for osteoporosis. J. Clin. Endocrinol. 76:1993;14-16.
29. Saneshige S., Mano H., Tezuka K., Kakudo S., Mori Y., Honda Y., Itabashi A., Yamada T., Miyata K., Hakeda Y., Ishii J., Kumegawa M. Retinoic acid directly stimulates osteoclastic bone resorption and gene expression of cathepsin K/OC-2. Biochem. J. 309:1995;721-724.
30. Sellami S., de Beaurepaire R. Medial diencephalic sites involved in calcitonin-induced hyperthermia and analgesia. Brain Res. 616:1993;307-310.
31. Smeekens S. P. Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases. Biotechnology. 11:1993;182-186.
32. Stroller T. J., Shields D. The role of paired basic amino acids in mediating proteolytic cleavage of prosomatostatin. J. Biol. Chem. 264:1989;6922-6928.
33. Takada Y., Kusuda M., Hiura K., Sato T., Mochizuki H., Nagao Y., Tomura M., Yashiro M., Hakeda Y., Kawashima H., Kumegawa M. A simple method to assess osteoclast-mediated bone resorption using unfractionated bone cells. Bone Miner. 17:1992;347-359.
34. Thomas G., Thorne B. A., Hruby D. E. Gene transfer techniques to study neuropeptide processing. Annu. Rev. Physiol. 50:1988;323-332.
35. Yanagita M., Hoshino H., Nakayama K., Takeuchi T. Processing of mutated proinsulin with tetrabasic cleavage sites to mature insulin reflects the expression of furin in nonendocrine cell lines. Endocrinology. 133:1993;639-644.