Zinc ions promote the interaction between heparin and heparin cofactor II

Eckert R, Ragg H (2003)
FEBS Letters 541(1-3): 121-125.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Eckert, Ralf; Ragg, HermannUniBi
Einrichtung
Centrum für Biotechnologie
Technische Fakultät
Abstract / Bemerkung
The effects of bivalent cations on heparin binding, structure, and thrombin inhibition rates of heparin cofactor II were examined. Zn2+ - and to a lesser extent Cu2+ and Ni2+ - enhanced the interaction between heparin cofactor II and heparin as demonstrated by heparin affinity chromatography and surface plasmon resonance experiments. Metal chelate chromatography and increased intrinsic protein fluorescence in the presence of Zn2+ indicated that heparin cofactor II as metal ion-binding properties. The results are compatible with the hypothesis that Zn2+ induces a conformational change in heparin cofactor IIhat favors its interaction with heparin. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Stichworte
heparin cofactor II; serpin; zinc; heparin; thrombin
Erscheinungsjahr
2003
Zeitschriftentitel
FEBS Letters
Band
541
Ausgabe
1-3
Seite(n)
121-125
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1953801

Zitieren

Eckert R, Ragg H. Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Letters. 2003;541(1-3):121-125.
Eckert, R., & Ragg, H. (2003). Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Letters, 541(1-3), 121-125. https://doi.org/10.1016/S0014-5793(03)00322-3
Eckert, Ralf, and Ragg, Hermann. 2003. “Zinc ions promote the interaction between heparin and heparin cofactor II”. FEBS Letters 541 (1-3): 121-125.
Eckert, R., and Ragg, H. (2003). Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Letters 541, 121-125.
Eckert, R., & Ragg, H., 2003. Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Letters, 541(1-3), p 121-125.
R. Eckert and H. Ragg, “Zinc ions promote the interaction between heparin and heparin cofactor II”, FEBS Letters, vol. 541, 2003, pp. 121-125.
Eckert, R., Ragg, H.: Zinc ions promote the interaction between heparin and heparin cofactor II. FEBS Letters. 541, 121-125 (2003).
Eckert, Ralf, and Ragg, Hermann. “Zinc ions promote the interaction between heparin and heparin cofactor II”. FEBS Letters 541.1-3 (2003): 121-125.

9 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The effect of Zn(2+) on Pelodiscus sinensis creatine kinase: unfolding and aggregation studies.
Wang SF, Lee J, Wang W, Si YX, Li C, Kim TR, Yang JM, Yin SJ, Qian GY., J Biomol Struct Dyn 31(6), 2013
PMID: 22888913
The effect of heparan sulfate application on bone formation during distraction osteogenesis.
Gdalevitch M, Kasaai B, Alam N, Dohin B, Lauzier D, Hamdy RC., PLoS One 8(2), 2013
PMID: 23457615
Cooperation of binding sites at the hydrophilic domain of cell-surface sulfatase Sulf1 allows for dynamic interaction of the enzyme with its substrate heparan sulfate.
Milz F, Harder A, Neuhaus P, Breitkreuz-Korff O, Walhorn V, Lübke T, Anselmetti D, Dierks T., Biochim Biophys Acta 1830(11), 2013
PMID: 23891937
Zn2+ mediates high affinity binding of heparin to the αC domain of fibrinogen.
Fredenburgh JC, Leslie BA, Stafford AR, Lim T, Chan HH, Weitz JI., J Biol Chem 288(41), 2013
PMID: 23990470
Motoneurons secrete angiogenin to induce RNA cleavage in astroglia.
Skorupa A, King MA, Aparicio IM, Dussmann H, Coughlan K, Breen B, Kieran D, Concannon CG, Marin P, Prehn JH., J Neurosci 32(15), 2012
PMID: 22496549
A zinc complex of heparan sulfate destabilises lysozyme and alters its conformation.
Hughes AJ, Hussain R, Cosentino C, Guerrini M, Siligardi G, Yates EA, Rudd TR., Biochem Biophys Res Commun 425(4), 2012
PMID: 22884801
Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain.
Frese MA, Milz F, Dick M, Lamanna WC, Dierks T., J Biol Chem 284(41), 2009
PMID: 19666466
Survey of the year 2003 commercial optical biosensor literature.
Rich RL, Myszka DG., J Mol Recognit 18(1), 2005
PMID: 15549676
Reformable intramolecular cross-linking of the N-terminal domain of heparin cofactor II: effects on enzyme inhibition.
Brinkmeyer S, Eckert R, Ragg H., Eur J Biochem 271(21), 2004
PMID: 15511233

42 References

Daten bereitgestellt von Europe PubMed Central.

Phylogenetic analyses of amino acid variation in the serpin proteins.
Atchley WR, Lokot T, Wollenberg K, Dress A, Ragg H., Mol. Biol. Evol. 18(8), 2001
PMID: 11470841
Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses.
Ragg H, Lokot T, Kamp PB, Atchley WR, Dress A., Mol. Biol. Evol. 18(4), 2001
PMID: 11264410

AUTHOR UNKNOWN, 0
Activation of heparin cofactor II by heparin oligosaccharides.
Maimone MM, Tollefsen DM., Biochem. Biophys. Res. Commun. 152(3), 1988
PMID: 3377765
Physicochemical aspects of heparin cofactor II.
Pratt CW, Whinna HC, Meade JB, Treanor RE, Church FC., Ann. N. Y. Acad. Sci. 556(), 1989
PMID: 2660681
On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans.
Ragg H, Ulshofer T, Gerewitz J., J. Biol. Chem. 265(9), 1990
PMID: 2318889
Crystal structures of native and thrombin-complexed heparin cofactor II reveal a multistep allosteric mechanism.
Baglin TP, Carrell RW, Church FC, Esmon CT, Huntington JA., Proc. Natl. Acad. Sci. U.S.A. 99(17), 2002
PMID: 12169660
Glycosaminoglycan-mediated leuserpin-2/thrombin interaction. Structure-function relationships.
Ragg H, Ulshofer T, Gerewitz J., J. Biol. Chem. 265(36), 1990
PMID: 2266131
The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.
Van Deerlin VM, Tollefsen DM., J. Biol. Chem. 266(30), 1991
PMID: 1939083
Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.
Mitchell JW, Church FC., J. Biol. Chem. 277(22), 2002
PMID: 11856753
Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.
Hayakawa Y, Hirashima Y, Kurimoto M, Hayashi N, Hamada H, Kuwayama N, Endo S., FEBS Lett. 522(1-3), 2002
PMID: 12095635
Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.
Liaw PC, Austin RC, Fredenburgh JC, Stafford AR, Weitz JI., J. Biol. Chem. 274(39), 1999
PMID: 10488098
Regulated diversity of heparan sulfate.
Lindahl U, Kusche-Gullberg M, Kjellen L., J. Biol. Chem. 273(39), 1998
PMID: 9737951
Synthesis and sorting of proteoglycans.
Prydz K, Dalen KT., J. Cell. Sci. 113 Pt 2(), 2000
PMID: 10633071
Selective binding of zinc ions to heparin rather than to other glycosaminoglycans.
Parrish RF, Fair WR., Biochem. J. 193(2), 1981
PMID: 6796046
Decorin is a Zn2+ metalloprotein.
Yang VW, LaBrenz SR, Rosenberg LC, McQuillan D, Hook M., J. Biol. Chem. 274(18), 1999
PMID: 10212220
Binding of heparin to human high molecular weight kininogen.
Bjork I, Olson ST, Sheffer RG, Shore JD., Biochemistry 28(3), 1989
PMID: 2713360
High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells.
Renne T, Dedio J, David G, Muller-Esterl W., J. Biol. Chem. 275(43), 2000
PMID: 10843988
Reactive site peptide structural similarity between heparin cofactor II and antithrombin III.
Griffith MJ, Noyes CM, Church FC., J. Biol. Chem. 260(4), 1985
PMID: 3838304
Murine heparin cofactor II: purification, cDNA sequence, expression, and gene structure.
Zhang GS, Mehringer JH, Van Deerlin VM, Kozak CA, Tollefsen DM., Biochemistry 33(12), 1994
PMID: 7908224
Structure-function relationships in heparin cofactor II: spectral analysis of aromatic residues and absence of a role for sulfhydryl groups in thrombin inhibition.
Church FC, Meade JB, Pratt CW., Arch. Biochem. Biophys. 259(2), 1987
PMID: 3426230
Tyrosine sulfation and N-glycosylation of human heparin cofactor II from plasma and recombinant Chinese hamster ovary cells and their effects on heparin binding.
Bohme C, Nimtz M, Grabenhorst E, Conradt HS, Strathmann A, Ragg H., Eur. J. Biochem. 269(3), 2002
PMID: 11846800

Brockhinke, Appl. Phys. B 71(), 2000
Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin.
Olson ST, Bjork I, Shore JD., Meth. Enzymol. 222(), 1993
PMID: 8412815
Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II.
Ciaccia AV, Willemze AJ, Church FC., J. Biol. Chem. 272(2), 1997
PMID: 8995378
Activation of heparin cofactor II by calcium spirulan.
Hayakawa Y, Hayashi T, Lee JB, Ozawa T, Sakuragawa N., J. Biol. Chem. 275(15), 2000
PMID: 10753952
Kinetic analysis of the role of zinc in the interaction of domain 5 of high-molecular weight kininogen (HK) with heparin.
Lin Y, Pixley RA, Colman RW., Biochemistry 39(17), 2000
PMID: 10819977

Westrup, Biochim. Biophys. Acta 1217(), 1994
Isolation of frog and chicken cDNAs encoding heparin cofactor II.
Colwell NS, Tollefsen DM., Thromb. Haemost. 80(5), 1998
PMID: 9843172
The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface.
DeLa Cadena RA, Colman RW., Protein Sci. 1(1), 1992
PMID: 1304876
Partial identification of the Zn2+-binding sites in factor XII and its activation derivatives.
Rojkaer R, Schousboe I., Eur. J. Biochem. 247(2), 1997
PMID: 9266689
Zinc-dependent conformational changes in domain D5 of high molecular mass kininogen modulate contact activation.
Herwald H, Morgelin M, Svensson HG, Sjobring U., Eur. J. Biochem. 268(2), 2001
PMID: 11168375
Properties of a 19-kDa Zn2+-binding protein and sequence of the Zn2+-binding domains.
Brand IA, Heinickel A, Kratzin H, Soling HD., Eur. J. Biochem. 177(3), 1988
PMID: 3197718
Zn(2+)-mediated structure formation and compaction of the "natively unfolded" human prothymosin alpha.
Uversky VN, Gillespie JR, Millett IS, Khodyakova AV, Vasilenko RN, Vasiliev AM, Rodionov IL, Kozlovskaya GD, Dolgikh DA, Fink AL, Doniach S, Permyakov EA, Abramov VM., Biochem. Biophys. Res. Commun. 267(2), 2000
PMID: 10631119
What does it mean to be natively unfolded?
Uversky VN., Eur. J. Biochem. 269(1), 2002
PMID: 11784292
Determination of ultrafiltrable zinc in plasma by flameless atomic absorption spectrophotometry.
Whitehouse RC, Prasad AS, Cossack ZT., Clin. Chem. 29(11), 1983
PMID: 6627638
Zinc as a cofactor for heparin neutralization by histidine-rich glycoprotein.
Kluszynski BA, Kim C, Faulk WP., J. Biol. Chem. 272(21), 1997
PMID: 9153200
The self-association of biglycan from bovine articular cartilage.
Liu J, Laue TM, Choi HU, Tang LH, Rosenberg L., J. Biol. Chem. 269(45), 1994
PMID: 7961776
Contact activation: a revision.
Schmaier AH., Thromb. Haemost. 78(1), 1997
PMID: 9198136
Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies.
Bernardo MM, Day DE, Halvorson HR, Olson ST, Shore JD., J. Biol. Chem. 268(17), 1993
PMID: 8509387
The amyloid beta-protein precursor and its mammalian homologues. Evidence for a zinc-modulated heparin-binding superfamily.
Bush AI, Pettingell WH Jr, de Paradis M, Tanzi RE, Wasco W., J. Biol. Chem. 269(43), 1994
PMID: 7929392
Cell-surface prion protein interacts with glycosaminoglycans.
Pan T, Wong BS, Liu T, Li R, Petersen RB, Sy MS., Biochem. J. 368(Pt 1), 2002
PMID: 12186633
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 12706831
PubMed | Europe PMC

Suchen in

Google Scholar