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MODIFIED GLYCOSYLATION IN RECOMBINANT HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES (TIMP), PRODUCED IN CHO CELLS GROWN IN THE PRESENCE OF GLYCOPROCESSING INHIBITORS
Chaplin, L. C. Cockett, M. I. Willenbrock, F. Hipkiss, J. B.
Chaplin, L. C.
Cockett, M. I.
Willenbrock, F.
Hipkiss, J. B.
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Issue Date
1991
Submitted date
2024-02-28
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Abstract
Tissue inhibitor of metalloproteinases (TIMP)is a glycoprotein of approximate M=30KDa, which has 2 Nlinked glycosylation sites giving rise to heterogeneous glycosylation, and characterised by a multiple bandpattern for the native protein on SDS-PAGE. The present work reports the production of TIMP with modified glycosylation by the use of a range of specific glycoprocessinginhibitors during cell culture. The inhibitors interfere with the normal trimming pathway during N-glycosylation of glycoproteins. Modified TIMPs showed greater homogeneity of glycosylation, higher iso-electric points, and similar inhibitory activity of metalloproteinases, compared with native TIMP. Theinhibitors could be used over a wide range of concentrations without having a significant effect on the production of TIMP,or on cell growth. This approach to modification of glycosylation may show significant advantagesin the production of glycoproteinsfor crystallization studies over more conventional methods such as enzymic deglycosylation, use of tunicamycin, or expression in coli,
Citation
Protein glycosylation, 279 - 282
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Book chapter
conference paper
conference paper
Language
en
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Series/Report no.
GBF monographs ; Volume 15
ISSN
0930-4320
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ISBN
1560811846
3527283676
3527283676
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Attribution-NonCommercial-ShareAlike 4.0 International