scholarly journals Comparative Cell Response to Artificial Extracellular Matrix Proteins Containing the RGD and CS5 Cell-Binding Domains

2004 ◽  
Vol 5 (2) ◽  
pp. 497-504 ◽  
Author(s):  
Julie C. Liu ◽  
Sarah C. Heilshorn ◽  
David A. Tirrell
Keyword(s):  
Extracellular Matrix ◽  
Cell Response ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Cell Binding ◽  
Binding Domains ◽  
Artificial Extracellular Matrix

scholarly journals Interaction of Fimbriae of Haemophilus influenzae Type B with Heparin-Binding Extracellular Matrix Proteins

2000 ◽  
Vol 68 (10) ◽  
pp. 5696-5701 ◽  
Author(s):  
Ritva Virkola ◽  
Mirko Brummer ◽  
Heikki Rauvala ◽  
Loek van Alphen ◽  
Timo K. Korhonen
Keyword(s):  
Extracellular Matrix ◽  
Haemophilus Influenzae ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Haemophilus Influenzae Type ◽  
Heparin Binding ◽  
Type B ◽  
Binding Domains ◽  
Human Fibronectin ◽  
High Concentrations

ABSTRACT The interaction of the fimbriae of Haemophilus influenzae type b (Hib) with two heparin-binding extracellular matrix proteins, human fibronectin (Fn) and heparin-binding growth-associated molecule (HB-GAM) from mouse, were studied. The fimbriated Hib strain 770235 fim+, as well as the recombinant strainE. coli HB101(pMH140), which expressed Hib fimbriae, adhered strongly to Fn and HB-GAM immobilized on glass. Purified Hib fimbriae bound to Fn and HB-GAM, and within the Fn molecule, the binding was localized to the N-terminal 30,000-molecular-weight (30K) and 40K fragments, which contain heparin-binding domains I and II, respectively. Fimbrial binding to Fn, HB-GAM, and the 30K and the 40K fragments was inhibited by high concentrations of heparin. The results show that fimbriae of Hib interact with heparin-binding extracellular matrix proteins. The nonfimbriated Hib strain 770235 fim− exhibited a low level of adherence to Fn but did not react with HB-GAM, indicating that Hib strains also possess a fimbria-independent mechanism to interact with Fn.

Design and Biosynthesis of Elastin-like Artificial Extracellular Matrix Proteins Containing Periodically Spaced Fibronectin CS5 Domains

1999 ◽  
Vol 32 (5) ◽  
pp. 1701-1703 ◽  
Author(s):  
Alyssa Panitch ◽  
Tetsuji Yamaoka ◽  
Maurille J. Fournier ◽  
Thomas L. Mason ◽  
David A. Tirrell
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Artificial Extracellular Matrix

scholarly journals Glycoprotein IV-independent adhesion of sickle red blood cells to immobilized thrombospondin under flow conditions

Blood ◽  
1996 ◽  
Vol 87 (11) ◽  
pp. 4862-4870 ◽  
Author(s):  
CC Joneckis ◽  
DD Shock ◽  
ML Cunningham ◽  
EP Orringer ◽  
LV Parise
Keyword(s):  
Extracellular Matrix ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Vascular Occlusion ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Flow Conditions ◽  
Adhesion Receptors ◽  
Binding Domains ◽  
Adhesive Site

The abnormal adherence of red blood cells (RBC to the blood vessel wall is believed to contribute to the vascular occlusion observed in patients with sickle call anemia. The cell adhesion receptors GPIV (CD36) and integrin alpha 4 beta 1 (CD49d/CD29) were previously identified on circulating sickle reticulocytes, and shown to mediate sickle RBC adhesion to the endothelium. The presence of damaged endothelium in these patients suggests that exposed extracellular matrix proteins could provide a potential substrate for sickle RBC adhesion. To determine whether RBC adhesion receptors could mediate adhesion to extracellular matrix proteins, we tested their ability to adhere to a variety of immobilized, purified proteins under flow conditions. Neither sickle nor normal RBC adhered to fibronectin, vitronectin, fibrinogen, or collagen. In contrast, we observed substantial adhesion of sickle but not normal RBC to thrombospondin (TSP). The adhesion was not inhibited with known antagonists of the GPIV-TSP interaction, nor by inhibitors of several other known binding domains in TSP. Moreover, the adhesion was resistant to inhibition by soluble TSP, suggesting that immobilization of TSP exposes an adhesive site that is cryptic on TSP in solution. However, the glycosaminoglycans, chondroitin sulfate A, and dextran sulfate were potent inhibitors of this adhesion. These results suggest that a mechanism distinct from GPIV is responsible for sickle RBC adhesion to immobilized TSP under flow conditions.

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