The proteoglycan bikunin has a defined sequence

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Authors
Ly, Mellisa
Leach, Franklin E.
Laremore, Tatiana N.
Toida, Toshihiko
Amster, I. Jonathan
Linhardt, Robert J.
Issue Date
2011-01-01
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Abstract
Proteoglycans are complex glycoconjugates that regulate critical biological pathways in all higher organisms. Bikunin, the simplest proteoglycan, with a single glycosaminoglycan chain, is a serine protease inhibitor used to treat acute pancreatitis. Unlike nucleic acids and proteins, whose synthesis is template driven, Golgi-synthesized glycosaminoglycans are not believed to have predictable or deterministic sequences. Bikunin peptidoglycosaminoglycans were prepared and fractionated to obtain a collection of size-similar and charge-similar chains. Fourier transform mass spectral analysis identified a small number of parent molecular ions corresponding to monocompositional peptidoglycosaminoglycans. Fragmentation using collision-induced dissociation unexpectedly afforded a single sequence for each monocompositional parent ion, unequivocally demonstrating the presence of a defined sequence. The biosynthetic pathway common to all proteoglycans suggests that even more structurally complex proteoglycans, such as heparan sulfate, may have defined sequences, requiring a readjustment in the understanding of information storage in complex glycans.
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Nature Chemical Biology, 7, 827-833
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Full Citation
The proteoglycan bikunin has a defined sequence, M. Ly, F. E. Leach III, T. N. Laremore, T. Toida, I. J. Amster, R.J. Linhardt, Nature Chemical Biology, 7, 827-833, 2011.
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Nature
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ISSN
15524469
15524450
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