Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding

Böhme C, Nimtz M, Grabenhorst E, Conradt HS, Strathmann A, Ragg H (2002)
EUROPEAN JOURNAL OF BIOCHEMISTRY 269(3): 977-988.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Abstract
The structure of post-translational modifications of human heparin cofactor II isolated from human serum and from recombinant Chinese hamster ovary cells and their effects on heparin binding have been characterized. Oligosaccharide chains were found attached to all three potential N-glycosylation sites in both protein preparations. The carbohydrate structures of heparin cofactor II circulating in blood are complex-type diantennary and triantennary chains in a ratio of 6 : 1 with the galactose being > 90% sialylated with alpha2 --> 6 linked N-acetylneuraminic acid. About 50% of the triantennary structures contain one sLe(x) motif. Proximal alpha1 --> 6 fucosylation of oligosacharides from Chinese hamster ovary cell-derived HCII was detected in > 90%. of the diantennary and triantennary glycans, the latter being slightly less sialylated with exclusively alpha2 --> 3-linked N-acetylneuraminic acid units. Applying the ESI-MS/MS-MS technique, we demonstrate that the tryptic peptides comprising tyrosine residues in positions 60 and 73 were almost completely sulfated irrespective of the protein's origin. Treatment of transfected Chinese hamster ovary cells with chlorate or tunicamycin resulted in the production of heparin cofactor II molecules that eluted with higher ionic strength from heparin-Sepharose, indicating that tyrosine sulfation and N-linked glycans may affect the inhibitor's interaction with glycosaminoglycans.
Publishing Year
ISSN
PUB-ID

Cite this

Böhme C, Nimtz M, Grabenhorst E, Conradt HS, Strathmann A, Ragg H. Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. EUROPEAN JOURNAL OF BIOCHEMISTRY. 2002;269(3):977-988.
Böhme, C., Nimtz, M., Grabenhorst, E., Conradt, H. S., Strathmann, A., & Ragg, H. (2002). Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. EUROPEAN JOURNAL OF BIOCHEMISTRY, 269(3), 977-988.
Böhme, C., Nimtz, M., Grabenhorst, E., Conradt, H. S., Strathmann, A., and Ragg, H. (2002). Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. EUROPEAN JOURNAL OF BIOCHEMISTRY 269, 977-988.
Böhme, C., et al., 2002. Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. EUROPEAN JOURNAL OF BIOCHEMISTRY, 269(3), p 977-988.
C. Böhme, et al., “Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 269, 2002, pp. 977-988.
Böhme, C., Nimtz, M., Grabenhorst, E., Conradt, H.S., Strathmann, A., Ragg, H.: Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding. EUROPEAN JOURNAL OF BIOCHEMISTRY. 269, 977-988 (2002).
Böhme, Christoph, Nimtz, Manfred, Grabenhorst, Eckart, Conradt, Harald S., Strathmann, Annemarie, and Ragg, Hermann. “Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding”. EUROPEAN JOURNAL OF BIOCHEMISTRY 269.3 (2002): 977-988.
This data publication is cited in the following publications:
This publication cites the following data publications:

6 Citations in Europe PMC

Data provided by Europe PubMed Central.

Glycosaminoglycan-binding properties and kinetic characterization of human heparin cofactor II expressed in Escherichia coli.
Sarilla S, Habib SY, Tollefsen DM, Friedman DB, Arnett DR, Verhamme IM., Anal. Biochem. 406(2), 2010
PMID: 20670608
Sucrose octasulfate selectively accelerates thrombin inactivation by heparin cofactor II.
Sarilla S, Habib SY, Kravtsov DV, Matafonov A, Gailani D, Verhamme IM., J. Biol. Chem. 285(11), 2010
PMID: 20053992
The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex.
Li Z, Kienetz M, Cherney MM, James MN, Bromme D., J. Mol. Biol. 383(1), 2008
PMID: 18692071
Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
Hyuga M, Itoh S, Kawasaki N, Ohta M, Ishii A, Hyuga S, Hayakawa T., Biologicals 32(2), 2004
PMID: 15454184

48 References

Data provided by Europe PubMed Central.

Structure and expression of the gene coding for the human serpin hLS2.
Ragg H, Preibisch G., J. Biol. Chem. 263(24), 1988
PMID: 2841345
Characterization of sites of tyrosine sulfation in proteins and criteria for predicting their occurrence.
Hortin G, Folz R, Gordon JI, Strauss AW., Biochem. Biophys. Res. Commun. 141(1), 1986
PMID: 3801003
Protein sulfation on tyrosine
Huttner, Modern Cell Biol. 6(), 1988
In vitro alpha1-3 or alpha1-4 fucosylation of type I and II oligosaccharides with secreted forms of recombinant human fucosyltransferases III and VI.
Nimtz M, Grabenhorst E, Gambert U, Costa J, Wray V, Morr M, Thiem J, Conradt HS., Glycoconj. J. 15(9), 1998
PMID: 10052591
Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells.
Grabenhorst E, Schlenke P, Pohl S, Nimtz M, Conradt HS., Glycoconj. J. 16(2), 1999
PMID: 10612409
Structures of sialylated oligosaccharides of human erythropoietin expressed in recombinant BHK-21 cells.
Nimtz M, Martin W, Wray V, Kloppel KD, Augustin J, Conradt HS., Eur. J. Biochem. 213(1), 1993
PMID: 8477709
Recombinant factor IX.
White GC 2nd, Beebe A, Nielsen B., Thromb. Haemost. 78(1), 1997
PMID: 9198163
New consensus features for tyrosine O-sulfation determined by mutational analysis.
Bundgaard JR, Vuust J, Rehfeld JF., J. Biol. Chem. 272(35), 1997
PMID: 9268297
Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155.
Garone L, Edmunds T, Hanson E, Bernasconi R, Huntington JA, Meagher JL, Fan B, Gettins PG., Biochemistry 35(27), 1996
PMID: 8688424
Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity.
Olson ST, Frances-Chmura AM, Swanson R, Bjork I, Zettlmeissl G., Arch. Biochem. Biophys. 341(2), 1997
PMID: 9169007
Role of lysine 173 in heparin binding to heparin cofactor II.
Whinna HC, Blinder MA, Szewczyk M, Tollefsen DM, Church FC., J. Biol. Chem. 266(13), 1991
PMID: 1902471
A comparison of three heparin-binding serine proteinase inhibitors.
Pratt CW, Whinna HC, Church FC., J. Biol. Chem. 267(13), 1992
PMID: 1315739

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 11846800
PubMed | Europe PMC

Search this title in

Google Scholar