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The glycosylation of alpha-1-antitrypsin expressed in transgenic mice

Kemp, Pauline Anne. and Freedman, Robert B. and Clark, A.J. and Jenkins, Nigel (1997) The glycosylation of alpha-1-antitrypsin expressed in transgenic mice. In: Funatsu, K. and Shirai, Y. and Matsushita, T., eds. Animal Cell Technology: Basic & Applied Aspects: Proceedings of the Eighth Annual Meeting of the Japanese Association for Animal Cell Technology. Kluwer Academic, pp. 517-522. ISBN 0-7923-4486-3. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. (Contact us about this Publication)

Abstract

Alpha-l-Antitrypsin (AAT) is a serine protease inhibitor whose main physiological role is the control of neutrophil elastase. In AAT deficiency disorders, mutants are poorly secreted or have low stability leading to emphysema and liver disease. AAT has three N-linked glycosylation sites; the unglycosylated protein is fully active but has a much reduced half-life in the circulation. Therefore, for therapeutic use large quantities of fully glycosylated AAT are required. Transgenic animals that express human AAT in mammary tissue have the potential to be used as bioreactors. Their ability to glycosylate the recombinant protein is crucial. AAT has been purified from human plasma and transgenic mouse milk, the glycopeptides isolated and the glycosylation microheterogeneity characterised. The major N-glycans identified from recombinant human AAT purified from transgenic mouse milli and from human plasma were complex sialylated biantennary structures. However, individual mice showed variation in site occupancy, the degree of fucosylation and the range of minor N-glycan structures detected.

Item Type: Book section
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 21 Sep 2009 12:31 UTC
Last Modified: 06 Aug 2019 11:34 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/18140 (The current URI for this page, for reference purposes)
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