Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1988 Apr 1;251(1):141–145. doi: 10.1042/bj2510141

Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin.

A A Horner 1, M Kusche 1, U Lindahl 1, C B Peterson 1
PMCID: PMC1148975  PMID: 3390150

Abstract

Rat skin heparin proteoglycans vary markedly in the proportions of their constituent polysaccharide chains that have high binding affinity for antithrombin. As the proportion of such chains in a proteoglycan rises, their degree of affinity for antithrombin also increases [Horner (1987) Biochem. J. 244, 693-698]. The antithrombin-binding-site densities of such chains have now been determined, by measuring heparin-induced enhancement of the intrinsic fluorescence of antithrombin and by chemical analysis for the disaccharide sequence glucuronosyl-N-sulphoglucosaminyl (3,6-di-O-sulphate), which is unique to this site in heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555]. Antithrombin-binding-site density ranged from one to five sites per chain.

Full text

PDF
141

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bienkowski M. J., Conrad H. E. Structural characterization of the oligosaccharides formed by depolymerization of heparin with nitrous acid. J Biol Chem. 1985 Jan 10;260(1):356–365. [PubMed] [Google Scholar]
  2. Einarsson R., Andersson L. O. Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence. Biochim Biophys Acta. 1977 Jan 25;490(1):104–111. doi: 10.1016/0005-2795(77)90110-6. [DOI] [PubMed] [Google Scholar]
  3. Horner A. A. Heterogeneity of rat skin heparin chains with high affinity for antithrombin. Biochem J. 1987 Jun 15;244(3):693–698. doi: 10.1042/bj2440693. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Horner A. A. Macromolecular heparin from rat skin. Isolation, characterization, and depolymerization with ascorbate. J Biol Chem. 1971 Jan 10;246(1):231–239. [PubMed] [Google Scholar]
  5. Horner A. A. Rat heparins. A study of the relative sizes and antithrombin-binding characteristics of heparin proteoglycans, chains and depolymerization products from rat adipose tissue, heart, lungs, peritoneal cavity and skin. Biochem J. 1986 Nov 15;240(1):171–179. doi: 10.1042/bj2400171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Horner A. A., Young E. Asymmetric distribution of sites with high affinity for antithrombin III in rat skin heparin proteoglycans. J Biol Chem. 1982 Aug 10;257(15):8749–8754. [PubMed] [Google Scholar]
  7. Hovingh P., Piepkorn M., Linker A. Biological implications of the structural, antithrombin affinity and anticoagulant activity relationships among vertebrate heparins and heparan sulphates. Biochem J. 1986 Jul 15;237(2):573–581. doi: 10.1042/bj2370573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jacobsson K. G., Lindahl U., Horner A. A. Location of antithrombin-binding regions in rat skin heparin proteoglycans. Biochem J. 1986 Dec 15;240(3):625–632. doi: 10.1042/bj2400625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jacobsson K. G., Riesenfeld J., Lindahl U. Biosynthesis of heparin. Effects of n-butyrate on cultured mast cells. J Biol Chem. 1985 Oct 5;260(22):12154–12159. [PubMed] [Google Scholar]
  10. Jordan R. E., Favreau L. V., Braswell E. H., Rosenberg R. D. Heparin with two binding sites for antithrombin or platelet factor 4. J Biol Chem. 1982 Jan 10;257(1):400–406. [PubMed] [Google Scholar]
  11. Lindahl U., Bäckström G., Thunberg L., Leder I. G. Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6551–6555. doi: 10.1073/pnas.77.11.6551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lindahl U., Thunberg L., Bäckström G., Riesenfeld J., Nordling K., Björk I. Extension and structural variability of the antithrombin-binding sequence in heparin. J Biol Chem. 1984 Oct 25;259(20):12368–12376. [PubMed] [Google Scholar]
  13. Marcum J. A., Atha D. H., Fritze L. M., Nawroth P., Stern D., Rosenberg R. D. Cloned bovine aortic endothelial cells synthesize anticoagulantly active heparan sulfate proteoglycan. J Biol Chem. 1986 Jun 5;261(16):7507–7517. [PubMed] [Google Scholar]
  14. Nesheim M., Blackburn M. N., Lawler C. M., Mann K. G. Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity-purified heparin. J Biol Chem. 1986 Mar 5;261(7):3214–3221. [PubMed] [Google Scholar]
  15. Nordenman B., Danielsson A., Björk I. The binding of low-affinity and high-affinity heparin to antithrombin. Fluorescence studies. Eur J Biochem. 1978 Sep 15;90(1):1–6. doi: 10.1111/j.1432-1033.1978.tb12567.x. [DOI] [PubMed] [Google Scholar]
  16. Pejler G., Bäckström G., Lindahl U., Paulsson M., Dziadek M., Fujiwara S., Timpl R. Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans. J Biol Chem. 1987 Apr 15;262(11):5036–5043. [PubMed] [Google Scholar]
  17. Peterson C. B., Blackburn M. N. Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J Biol Chem. 1985 Jan 10;260(1):610–615. [PubMed] [Google Scholar]
  18. Robinson H. C., Horner A. A., Hök M., Ogren S., Lindahl U. A proteoglycan form of heparin and its degradation to single-chain molecules. J Biol Chem. 1978 Oct 10;253(19):6687–6693. [PubMed] [Google Scholar]
  19. Thunberg L., Bäckström G., Lindahl U. Further characterization of the antithrombin-binding sequence in heparin. Carbohydr Res. 1982 Mar 1;100:393–410. doi: 10.1016/s0008-6215(00)81050-2. [DOI] [PubMed] [Google Scholar]
  20. Yong L. C., Watkins S., Wilhelm D. L. The mast cell: distribution and maturation in the peritoneal cavity of the adult rat. Pathology. 1975 Oct;7(4):307–318. doi: 10.3109/00313027509081687. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES