Abstract
For mass-production of laminin α β γ trimers, the interchain assemble domains of mouse laminin β 1 and γ 1 chains were expressed in budding yeast. In spite of a high level of expression, the products were not transported correctly into the lumen of endoplasmic reticulum for N-glycosylated and interchain disulfide-bonding. Chain-specific immunoprecipitation suggested that such miss-transported laminin chains were associated to each other.
Laminins are a family of basement membrane glycoproteins having strong influence to proliferation and differentiation of various tissues cells(l). Laminins are also important to organize tissue cells into epithelium and endothelium. In tissue engineering experiments, direct application of Matrigel, a reconstituted form of basement membrane composed of mainly laminin-1, to animal models has proven to be beneficial for the formation and maintenance of new tissues. For example, Matrigel not only enhances survival and integration of grafted dopamine neurons into the striatum but also increases the rate of peripheral nerve regeneration. When injected subcutaneously into connective tissues of mice in combination with basic fibroblast growth factor(bFGF), neovescularization in the Matrigel plug occurs by invasion of endothelial cells, which is followed by invesion and maturation of endogenous adipocyte precursor cells(2). Laminins are composed of α, β and γ chains and trimeric assembly either of α l-α 5, of β 1-β 3 and of γ l-γ 3 chains produces at least 15 different lamini isoforms(3). In this study, we have explored the possibility of muss production of laminins in budding yeast for potential use in tissue engineering and reconstructive therapy.
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Reference
Martin, G.R., Timple, R., and Kuhr, K. (1988) Basement membrane proteins: molecular structure and function. Adv. Protein Chem. 39, 1–50
Kawaguchi, N., Toriyama. K., Nicodemou-Lena, E., Inou, K., Torii, S., and Kitagawa, Y. (1998) De novo adipogenesis in mice at the site of injection of basement membrane and basic fibrobrast growth factor. Proc. Natl. Acad. Sci. USA. 95, 1062–1066
Miner, J.H., Patton, B.L., Lentz, S.I., Gillbert, D.J., Sinder, W.D., Jenkins, N.A., Copeland, N.G., and Sanes, J.R. (1997) The laminin alpha chains: Expression, developmental transitions, and chromosomal locations of alphal-5, identification of heterotrimeric laminin8–ll, and cloning of a novel alpha3 isoform. J. Cell Biol 137, 685–701
Niimi, T., Miki, K., and Kitagawa, Y. (1997) Expression of the long arm sequence of mouse laminin alphal, betal, gammal chain in COS1 cells and assembly of mouse-monkey hybrid laminin. J.Biochem. 121, 854–861
Niimi, T., Kitagawa, Y. (1997) Distinct roles of mouse laminin betal long arm domains for alphalbetalgammal trimer formation. FEBS Lett. 400, 71–74
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© 2003 Springer Science+Business Media Dordrecht
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Mizuno, K., Kadowaki, T., Kitagawa, Y. (2003). Mass-Production in Yeast of Laminins as the Material of Reconstructive Therapy. In: Yagasaki, K., Miura, Y., Hatori, M., Nomura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0726-8_35
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DOI: https://doi.org/10.1007/978-94-017-0726-8_35
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-6557-5
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