Biopolym. Cell. 2002; 18(5):423-428.
http://dx.doi.org/10.7124/bc.000621
Viruses and Cell
Comparative study on the efficiency of human recombinant prolactin expression in two baculovirus systems
1Strokovskaya L. I., 1Meleshko R. A., 1Kikhno I. M., 1Solomko A. P.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

The comparative study on the human recombinant Prolactin expression in the system NPV Malacosoma neustria (Mane)–cell Anteraea pernyi (Ap) and the system based on NPV Autographa californica (Ac) and insect cell lines Hf, Sf21 and Sfl is performed. The level of Prolactin expression is shown to be 50–70 mg/l of a medium for both NPV ManePRL and monolayer culture Ap, while for a recombinant virus AcPRL this parameter is 1.7 times higher in cells Sf9 and Sf21 and 3.5 times higher in cells Hf. Thus the major part of the human recombinant hormone synthesized in all cases is in an aggregate state.
Full text: (PDF, in Russian)

References

[1] Freeman ME, Kanyicska B, Lerant A, Nagy G. Prolactin: structure, function, and regulation of secretion. Physiol Rev. 2000;80(4):1523-631. Review.
[2] Strokovskaya LI, Kikhno IM, Veselovsky OV, Skuratovskaya IN, Miryuta NYu, Petrenko AI, Solomko AP. Malacosoma neustria nuclear polyhedrosis virus expression vector. Biopolym Cell. 1990; 6(3):84-9.
[3] Strokovskaya LI, Kalinina NO, Kikhno IM, Solomko AP. The expression of recombinant human prolactin with use of the baculovirus vector on the basis of Malacosoma Neustria nuclear polyhedrosis virus. Dopovidi Nats Akad Nauk Ukrainy. 1997; (1):166-9.
[4] Sukhorada EM, Kanyuka VYu, Miloserdova VD. Reproduction of silkworm ringed nuclear polyhedrosis virus by prolonged passaging in insect transplanted cells lines. Entomopathogenic viruses and their practical significance. Kyiv, Naukova dumka, 1981; 44-50.
[5] Nishimura A, Morita M, Nishimura Y, Sugino Y. A rapid and highly efficient method for preparation of competent Escherichia coli cells. Nucleic Acids Res. 1990;18(20):6169.
[6] Maniatis T, Fritch EF, Sambrook J. Molecular cloning: A laboratory manual. New York: Cold Spring Harbor Lab. press, 1989.
[7] Zolotukhin SB, Markelova EYu, Panasenko GV, Naidenov VG, Shved AD, Sautin YuYu, Patsko YaV. A fast method for cloning of specific cDNA. Cloning of human prolactin cDNA. Biopolym Cell. 1989; 5(6):87-92.
[8] Strokovskaia LI, Kikhno IM, Kalinina NO, Chashchina LI, Solomko AP. Heterologous protein expression in the baculovirus vector system: the nuclear polyhedrosis virus of Malacosoma neustria in Antheraea pernyi cells. Tsitol Genet. 1996;30(1):42-8. .
[9] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[10] Luckow VA, Summers MD. Trends in the development of baculovirus expression vectors. Bio/Technology. 1988;6(1):47–55.
[11] Kikhno IM, Strokovskaya LI. Baculovirus system for foreign genes expression – present and future of biotechnology receaving of biologically active proteins of various origin. Biopolym Cell. 1994; 10(5):31-48.
[12] Bole-Feysot C, Goffin V, Edery M, Binart N, Kelly PA. Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice. Endocr Rev. 1998;19(3):225-68.
[13] Luckow VA, Lee SC, Barry GF, Olins PO. Efficient generation of infectious recombinant baculoviruses by site-specific transposon-mediated insertion of foreign genes into a baculovirus genome propagated in Escherichia coli. J Virol. 1993;67(8):4566-79.