PRODUCTION OF RECOMBINANT HUMAN LACTOFERRIN FROM THE MILK OF GOAT-PRODUCERS AND ITS PHYSIOLOGICAL EFFECTS
Abstract
Primary male-goats Lac-1 (human lactoferrin gene construction hLF5) and Lac-2 (human lactoferrin gene construction hLF3) with a genome containing a human lactoferrin gene were bred and the sperm bank of primary male-goats was created within the framework of Belarus-Russia Union State programs. The herd of goats that produced recombinant human lactoferrin (rhLF) in their milk was obtained. Human lactoferrin (rhLF) from the milk of transgenic goats, natural human lactoferrin (nhLf) from the woman milk, and natural goat lactoferrin (gLf) from the milk of non-transgenic goats were purified using cation-exchange chromatography. Physicochemical characteristics of rhLF were similar to those of nhLf as revealed by different analytical methods including mass spectrometry and peptide mapping. g. Oral supplementation with rhLF activated lipid metabolism and steroidogenesis, promoted favorable changes in the gut microflor composition as well as the enhancement of the functional activity and the fine structure of the rat liver and gut.
About the Authors
V. S. LUKASHEVICH
Institute of Physiology of the National Academy of Sciences of Belarus, Minsk
Belarus
Belarus
A. I. BUDZEVICH
Scientific and practical center of the National Academy of Sciences of Belarus on animal husbandry, Zhodino
Belarus
Belarus
I. V. SEMAK
Belarusian State University, Minsk
Belarus
Belarus
V. N. KUZNETSOVA
Scientific and practical center of the National Academy of Sciences of Belarus on animal husbandry, Zhodino
Belarus
Belarus
E. V. MALYUSHKOVA
Belarusian State University, Minsk
Belarus
Belarus
A. E. PYZH
Institute of Physiology of the National Academy of Sciences of Belarus, Minsk
Belarus
Belarus
S. A. NOVAKOVSKAYA
Institute of Physiology of the National Academy of Sciences of Belarus, Minsk
Belarus
Belarus
J. A. RUDNICHENKO
Institute of Physiology of the National Academy of Sciences of Belarus, Minsk
Belarus
Belarus
N. A. POPKOV
Scientific and practical center of the National Academy of Sciences of Belarus on animal husbandry, Zhodino
Belarus
Belarus
O. A. IVASHKEVICH
Belarusian State University, Minsk
Belarus
Belarus
I. V. ZALUTSKY
Institute of Physiology of the National Academy of Sciences of Belarus, Minsk
Belarus
Belarus
References
1. Волков, Г. Л. Инновационные технологии в биофармацевтике: модерн и традиции / Г. Л. Волков, Е. С. Гаврилюк // Фармацевтическая отрасль. – 2011. – № 5 (28). – С. 94–98.
2. Lai, T. Advances in Mammalian Cell Line Development / T. Lai, Y. Yang, S. K. Ng // Technologies for Recombinant Protein Production Pharmaceuticals (Basel). – 2013. – Vol. 6, N 5. – P. 579–603.
3. Use of Transgenic Animals in Biotechnology: Prospects and Problems / O. G. Maksimenko [et al.] // Acta Naturae. – 2013. – Vol. 5, N 1. – P. 33–46.
4. Recombinant human lactoferrin from transgenic goats: isolation and physicochemical properties / I. Semak [et al.] // The Xth International Conference on Lactoferrin, Structure, Function and applications, 08–12 May, 2011. – Mazatlan, Mexico. P-VI-6. – P. 74.
5. Recombinant human lactoferrin expressed in transgenic goats / A. Budzevich [et al.] // The Xth International Conference on Lactoferrin, Structure, Function and applications, 08–12 May, 2011. – Mazatlan, Mexico. O-VI-2. – P. 66.
6. Multifunctional iron bound lactoferrin and nanomedicinal approaches to enhance its bioactive functions / J. R. Kanwar [et al.] // Molecules. – 2015. – Vol. 20, N 6. – P. 9703–9731.
7. Production of human lactoferrin in animal milk / I. L. Goldman [et al.] // Biochem. Cell Biol. – 2012. – Vol. 90, N 3. – P. 513–519.
8. Микробиологическая и молекулярно-генетическая оценка воздействия наноматериалов на представителей микробиоценоза / Федеральный центр гигиены и эпидемиологии Роспотребнадзора. – М., 2010. – 58 с.
9. Боголепов, Н. Н. Методы электронно-микроскопического исследования мозга / Н. Н. Боголепов. – М., 1976. – 71 с.
10. Viejo-Díaz, M. Different anti-Candida activities of two human lactoferrin-derived Peptides, Lfpep and kaliocin-1 / M. Viejo-Díaz, M. T. Andrés, J. F. Fierro // Antimicrob. Agents Chemother. – 2005. – Vol. 49, N 7. – P. 2583–2588.
11. Inhibitory effects of bovine lactoferrin on the adherence of enterotoxigenic Escherichia coli to host cells / Y. Kawasaki [et al.] // Biosci. Biotechnol. Biochem. – 2000. – Vol. 64, N 2. – P. 348–354.
12. Shimizu, H. Development of an enteric-coated lactoferrin tablet and its application / H. Shimizu // BioMetals. – 2004. – Vol. 17. – P. 343–347.
13. Human lactoferrin from transgenic goats prevents antibiotic-assotiated structural and metabolic damages in the digestive system / U. Lukashevich [et al.] // The XIth International Conference on Lactoferrin, Structure, Function and applications, October 6–10, 2013. – Rome, Italy, 2013. – P. 41.
14. Recombinant human lactoferrin: biological activity / A. Budzevich [et al.] // The XIth International Conference on Lactoferrin, Structure, Function and applications, October 6–10, 2013. – Rome, Italy, 2013. – P. 32.
15. Средство повышения уровня эндогенного тестостерона в крови / И. В. Залуцкий, Ю. А. Рудниченко, В. С. Лукашевич; Положительное решение предварительной экспертизы по заявке на патент № а20130982 от 14.08.2013 г.
16. Протекторные эффекты рекомбинантного человеческого лактоферрина в отношении токсического действия эндотоксина кишечной палочки на культуру клеток HeLa / М. О. Хотянович [и др.] // Новости медико-биологических наук. – 2011. – Т. 4, № 3. – С. 65–69.
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