Production of biologically active salmon calcitonin in the milk of transgenic rabbits

Nature Biotechnology

Volumn 16, Issue 7, 1998, Pages 647-651

  McKee, Colin ^a   Gibson, Allan ^a   Dalrymple, Mike ^a   Emslie, Liz ^a   Garner, Ian ^a   Cottingham, Ian ^a  

^a PPL Therapeutics   (United Kingdom)

Author keywords

Bioreactor; Mammary gland; Posttranslational modification; Protein processing

Indexed keywords

SALCATONIN;

AMIDATION; ARTICLE; BIOREACTOR; CARBOXY TERMINAL SEQUENCE; MILK; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN EXPRESSION; PROTEIN PROCESSING; TRANSGENIC ANIMAL;

AMIDES; ANIMALS; ANIMALS, GENETICALLY MODIFIED; BASE SEQUENCE; CALCITONIN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DNA; FEMALE; LACTALBUMIN; MAMMARY GLANDS, ANIMAL; MASS SPECTROMETRY; MILK; MOLECULAR SEQUENCE DATA; RABBITS; RECOMBINANT FUSION PROTEINS;

ANIMALIA; ORYCTOLAGUS CUNICULUS; OVIS;

EID: 0031853333     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0798-647     Document Type: Article

References (23)

1. Kelley, W.S. 1996. Therapeutic peptides: the devil is in the details. Bio/Technology 14:28-32.
2. Wallis, M., Howell S.L., and Taylor K.W. 1985. Parathyroid hormone and calcitonin, pp. 336-350 in The biochemistry of the polypeptide hormones. John Wiley and Sons, New York.
3. Silva, O.M. and Becker, K.L. 1973. Salmon calcitonin in the treatment of hypercalcemia. Arch. Intern. Med. 132:337-339.
4. Avramides, A. 1977. Salmon and porcine calcitonin treatment of Pagets disease of bone. Clin. Orthop. 127:78-85.
5. Mundy, G.R. 1994. Peptides and growth regulatory factors in bone. Osteoporosis 20:557-573.
6. Cudd, A., Arvinte, T., Das, R.E., Chinni, C., and MacIntyre, I. 1995. Enhanced potency of human calcitonin when fibrillation is avoided. J. Pharm. Sci. 84:717-719.
7. Epand, D.M., Epand, R.F., Stafford, A.R., and Orlowski, R.C. 1988. Deletion sequences of salmon calcitonin that retain the essential biological and conformational features of the intact molecule. J. Med. Chem. 31:1595-1598.
8. Wright, G., Carver, A., Cottom, D., Reeves, D., Scott, A., Simons, P. et al. 1991. High level expression of active human α-1-antitrypsin in the milk of transgenic sheep. Bio/Technology 9:77-84.
9. Lubon, H., Paleyanda, R.K., Velander, W.H., and Drohan, W.N. 1996. Transfusion medicine reviews, Vol. 10, pp. 131-143.
10. Eipper B.A., Stoffers D.A., and Mains R.E. 1992. The biosynthesis of neuropeptides: peptide α-amidation. Annu. Rev. Neurosci. 15:57-85.
11. Brew, K. and Hill, R.L. 1975. Lactose biosynthesis. Rev. Physiol. Biochem. Pharmacol. 72:105-158.
12. Lindahl, L. and Vogel, H.J., 1984. Metal ion dependant hydrophobic interaction chromatography of alpha-lactalbumins. Anal. Biochem. 140:394-402.
13. LaVallie, E.R., Rehemtulla, A., Racie, L.A., DiBlasio, E.A., Ferenz, C. Grant, K.L. et al. 1993. Cloning and functional expression of a cDNA encoding the catalytic subunit of bovine enterokinase. J. Biol. Chem. 268:23311-23317.
14. Ray, M.V.L., Van Duyn, P., Bertlensen, A.H., Jackson-Mathews, D.E., Sturmer, A.M., Merkler, D.J. et al. 1993. Production of recombinant salmon calcitonin by in vitro amidation of an Escerichia coli produced precursor peptide. Bio/Technology 11:64-70.
15. Light, A., Savrthri, H.S., and Liepnieks, J.J., 1980. Specificity of bovine enterokinase toward protein substrates. Anal. Biochem. 106:199-206.
16. Kumar, M.A., Slack, E., Edwards, A., Soliman, H.A., Baghdianz, A., Foster, G.V., and MacIntyre, I. 1965 A biological assay for calcitonin. J. Endocrin. 33:469-475.
17. Han, K.K. and Martinage, A. 1992. Possible relationships between coding recognition amino acid sequence motif or residue(s) and posttranslational chemical modidfication of proteins. Int. J. Biochem. 24:1349-1363.
18. Tamburini, P.P., Young, S.D., Jones, B.N., Palmesino, R.A., and Consalvo, A.P. 1990. Peptide substrate specificity of the α-amidating enzyme isolated from rat medullary thyroid CA-77 cells. Int. J. Peptide and Protein Res. 35:153-156.
19. Shah, G.V., Kacsoh, B., Seshadri, R., Grosvenor, C.E., and Crowley, W.R. 1989. Presence of calcitonin-like peptide in rat milk: possible physiological role in regulation of neonatal prolactin secretion. Endocrinology 125:61-67.
20. Connolly, J.M. and Rose, D.P. 1988. Epidermal growth factor-like proteins in breast fluid and human milk. Life Sci. 42:1751-1756.
21. Strewler, G.J., Budayr, A.A., Halloran, B.P., King, J.C., Diep, D., and Nissenson, R.A. 1989. High levels of parathyroid hormone-like protein in milk. Endocrinology 124:152 (Abstract).
22. Stacey, A., Sehnieke, A., Kerr, M., Scott, A., McKee, C., Cottinham, I. et al. 1995. Lactation is disrupted by α-lactalbumin deficiency and can be restored by human α-lactalbumin gene replacement in mice. Proc. Natl. Acad. Sci. USA 92:2835-2839.
23. Devinoy, E., Thepot, D., Stinnakre, M.G., Fontaine, M.L., Puissant, C., Pavirani, A. et al. 1994. High level production of human growth hormone in the milk of transgenic mice: the upstream region of the rabbit whey acidic protein (WAP) gene targets transgene expression to the mammary gland. Transgenic Research 3:79-89.