The interaction of heparan sulfate proteoglycans with endothelial transglutaminase-2 limits VEGF165-induced angiogenesis

2015 ◽  
Vol 8 (385) ◽  
pp. ra70-ra70 ◽  
Author(s):  
Nathan Beckouche ◽  
Marine Bignon ◽  
Virginie Lelarge ◽  
Thomas Mathivet ◽  
Cathy Pichol-Thievend ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Transglutaminase 2 ◽  
Heparan Sulfate Proteoglycans

scholarly journals Heparan Sulfate Proteoglycans Are Receptors for the Cell-surface Trafficking and Biological Activity of Transglutaminase-2

2009 ◽  
Vol 284 (27) ◽  
pp. 18411-18423 ◽  
Author(s):  
Alessandra Scarpellini ◽  
Renée Germack ◽  
Hugues Lortat-Jacob ◽  
Takashi Muramatsu ◽  
Ellen Billett ◽  
...  
Keyword(s):  
Biological Activity ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Transglutaminase 2 ◽  
Heparan Sulfate Proteoglycans

scholarly journals Spotlight on the Transglutaminase 2-Heparan Sulfate Interaction

2019 ◽  
Vol 7 (1) ◽  
pp. 5 ◽  
Author(s):  
Giulia Furini ◽  
Elisabetta A.M. Verderio
Keyword(s):  
Heparan Sulfate ◽  
Cardiac Fibrosis ◽  
Metastatic Cancer ◽  
Transglutaminase 2 ◽  
Experimental Models ◽  
Heparan Sulfate Proteoglycans ◽  
Heparin Binding ◽  
Kidney Fibrosis ◽  
The Past ◽  
Heparin Binding Site

Heparan sulfate proteoglycans (HSPGs), syndecan-4 (Sdc4) especially, have been suggested as potential partners of transglutaminase-2 (TG2) in kidney and cardiac fibrosis, metastatic cancer, neurodegeneration and coeliac disease. The proposed role for HSPGs in the trafficking of TG2 at the cell surface and in the extracellular matrix (ECM) has been linked to the fibrogenic action of TG2 in experimental models of kidney fibrosis. As the TG2-HSPG interaction is largely mediated by the heparan sulfate (HS) chains of proteoglycans, in the past few years a number of studies have investigated the affinity of TG2 for HS, and the TG2 heparin binding site has been mapped with alternative outlooks. In this review, we aim to provide a compendium of the main literature available on the interaction of TG2 with HS, with reference to the pathological processes in which extracellular TG2 plays a role.

Localization of cell-surface and basement-membrane heparan-sulfate proteoglycans using the malaria circumsporozoite protein

1994 ◽  
Vol 52 ◽  
pp. 294-295
Author(s):  
U. Frevert ◽  
S. Sinnis ◽  
C. Cerami ◽  
V. Nussenzweig
Keyword(s):  
Heparan Sulfate ◽  
Protein A ◽  
Kidney Tissue ◽  
Plasmodium Species ◽  
Its Region ◽  
Basement Membranes ◽  
Heparan Sulfate Proteoglycans ◽  
Infected Mosquito ◽  
Complement Components ◽  
Region Ii

Malaria sporozoites, which invade hepatocytes within minutes after transmission by an infected mosquito, are covered with the circumsporozoite (CS) protein, which in all Plasmodium species contains the conserved region II-plus. This region is also found as a cell-adhesive motif in a variety of host proteins like thrombospondin, properdin and the terminal complement components.The CS protein with its region II-plus specifically binds to heparan sulfate proteoglycans (HSPG) on the basolateral surface of hepatocytes in the space of Disse (FIG. 1), to certain basolateral cell membranes and basement membranes of the kidney (FIG. 2) as well as to heparin in the granules of connective tissue mast cells. The distribution of the HSPG receptors for the CS protein was examined by incubation of Lowicryl K4M or LR White sections of liver and kidney tissue with the recombinant CS ligand, whose binding sites were detected with a monoclonal anti-CS antibody and protein A gold.

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