RSS-Feed abonnieren
DOI: 10.1055/s-0041-1724119
Hemostatic and Nonhemostatic Effects of Heparan Sulfate Proteoglycans
![](https://www.thieme-connect.de/media/sth/202103/lookinside/thumbnails/10-1055-s-0041-1724119_02878-1.jpg)
Heparan sulfate proteoglycans (HSPGs) are composed of negatively charged heparan sulfate (HS) chains linked to a core protein. HS chains have an ancient evolutionary history, and are highly conserved. Virtually every cell type in metazoan (multicellular animals) organisms produces HS. The chains are synthesized by a highly ordered sequence of enzymatic events in the Golgi apparatus and are present on cell surface membranes, membranes of intracellular organelles, basement membranes, and in the extracellular matrix. These complex polysaccharides serve as low-affinity receptors to numerous proteins that contain a heparin-binding domain. Modulation of the HS chains may potentially affect cell surface interactions with numerous molecules, cells, and microparticles.[1] As HSPGs are important gatekeepers at the cell surface, they are involved in ample biological processes including hemostasis. In the present issue of Seminars in Thrombosis and Hemostasis, we introduce several fields where a significant role of HSPGs has been established, making them an important mechanism linking hemostasis, inflammation, angiogenesis, and cancer. Research in the field of HS chains is lagging behind because of the lack of advanced laboratory assays. While the protein part in the HSPGs complex (e.g., syndecan) can be easily evaluated using an antibody interacting with the protein, commercially available assays to assess the sugar chains of HS are sparse.
Publikationsverlauf
Artikel online veröffentlicht:
01. April 2021
© 2021. Thieme. All rights reserved.
Thieme Medical Publishers, Inc.
333 Seventh Avenue, 18th Floor, New York, NY 10001, USA
-
References
- 1 Esko JD, Selleck SB. Order out of chaos: assembly of ligand binding sites in heparan sulfate. Annu Rev Biochem 2002; 71: 435-471
- 2 Vlodavsky I, Barash U, Nguyen HM, Yang S-M, Ilan N. Biology of the heparanase-heparan sulfate axis an its role in disease pathogenesis. Semin Thromb Hemost 2021; 47 (03) 240-253
- 3 Nadir Y. Effect of heparanase and heparan sulfate chains in hemostasis. Semin Thromb Hemost 2021; 47 (03) 254-260
- 4 Hiebert LM. Heparan sulfate proteoglycans in diabetes. Semin Thromb Hemost 2021; 47 (03) 261-273
- 5 Oshima K, King SI, McMurtry SA, Schmidt EP. Endothelial heparan sulfate proteoglycans in sepsis: the role of the glycocalyx. Semin Thromb Hemost 2021; 47 (03) 274-282
- 6 Koganti R, Memon A, Shukla D. Emerging roles of heparan sulfate proteoglycans in viral pathogenesis. Semin Thromb Hemost 2021; 47 (03) 283-294
- 7 Lepedda AJ, Nieddu G, Piperigkou Z, Kyriakopoulou K, Karamanos N, Formato M. Circulating heparan sulfate proteoglycans as biomarkers in health and disease. Semin Thromb Hemost 2021; 47 (03) 295-307
- 8 Peall IW, Okolicsanyi RK, Griffiths LR, Haupt LM. 3D human neural stem cell models to mimic heparan sulfate proteoglycans (HSPGs) and the neural niche. Semin Thromb Hemost 2021; 47 (03) 308-315
- 9 Gerlza T, Trojacher C, Kitic N, Adage T, Kungl AJ. Development of molecules antagonizing heparan sulfate proteoglycans (HSPGs). Semin Thromb Hemost 2021; 47 (03) 316-332