Artificial extracellular matrix proteins contain heparin-binding and RGD-containing domains to improve osteoblast-like cell attachment and growth

2006 ◽  
Vol 79A (3) ◽  
pp. 557-565 ◽  
Author(s):  
Suh-Chin Wu ◽  
Jung-Chuan Yu ◽  
Shan-hui Hsu ◽  
David Chanhen Chen
Keyword(s):  
Extracellular Matrix ◽  
Cell Attachment ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Heparin Binding ◽  
Artificial Extracellular Matrix

scholarly journals The Haemophilus influenzae Hap Autotransporter Binds to Fibronectin, Laminin, and Collagen IV

2002 ◽  
Vol 70 (9) ◽  
pp. 4902-4907 ◽  
Author(s):  
Doran L. Fink ◽  
Bruce A. Green ◽  
Joseph W. St. Geme
Keyword(s):  
Extracellular Matrix ◽  
Respiratory Tract ◽  
Haemophilus Influenzae ◽  
Extracellular Matrix Proteins ◽  
Collagen Iv ◽  
Binding Domain ◽  
Matrix Proteins ◽  
Heparin Binding ◽  
Upper Respiratory Tract ◽  
Passenger Domain

ABSTRACT Nontypeable Haemophilus influenzae (NTHI) initiates infection by colonizing the upper respiratory tract mucosa. NTHI disease frequently occurs in the context of respiratory tract inflammation, where organisms encounter damaged epithelium and exposed basement membrane. In this study, we examined interactions between the H. influenzae Hap adhesin and selected extracellular matrix proteins. Hap is an autotransporter protein that undergoes autoproteolytic cleavage, with release of the adhesive passenger domain, Haps, from the bacterial cell surface. We found that Hap promotes bacterial adherence to purified fibronectin, laminin, and collagen IV and that Hap-mediated adherence is enhanced by inhibition of autoproteolysis. Adherence is inhibited by pretreatment of bacteria with a polyclonal antiserum recognizing Haps. Purified Haps binds with high affinity to fibronectin, laminin, and collagen IV but not to collagen II. Binding of Haps to fibronectin involves interaction with the 45-kDa gelatin-binding domain but not the 30-kDa heparin-binding domain of fibronectin. Taken together, these observations suggest that interactions between Hap and extracellular matrix proteins may play an important role in NTHI colonization of the respiratory tract.

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.

Receptor-mediated adhesive and anti-adhesive functions of chondroitin sulfate proteoglycan preparations from embryonic chicken brain

1995 ◽  
Vol 108 (12) ◽  
pp. 3807-3816 ◽  
Author(s):  
H. Ernst ◽  
M.K. Zanin ◽  
D. Everman ◽  
S. Hoffman
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Cell Attachment ◽  
Extracellular Matrix Proteins ◽  
Cell Spreading ◽  
The Other ◽  
Matrix Proteins ◽  
Surface Receptors ◽  
Core Proteins ◽  
Proteoglycan Aggregates

Chondroitin sulfate proteoglycans inhibit the adhesion of cells to extracellular matrix proteins that otherwise permit adhesion. Although proteoglycans are widely assumed to act by masking the other protein in a mixed substrate, recent studies suggest that proteoglycans inhibit adhesion through mechanisms initiated by their binding to specific cell surface receptors. To explore this issue, we developed a purification scheme to isolate proteoglycan aggregates, monomers, and core proteins. Two distinct adhesion assays were used to study the interaction of these proteoglycan preparations with human foreskin fibroblasts: the gravity assay in which cell attachment is stabilized by cell spreading, and the centrifugation assay in which spreading does not play a role. All proteoglycan preparations mediate adhesion in the centrifugation assay but not in the gravity assay. In the centrifugation assay, proteoglycan aggregates and monomers are considerably more active than other extracellular matrix proteins while proteoglycan core proteins are at least as active as other extracellular matrix proteins. Proteoglycan core proteins bind to cell-associated hyaluronic acid, but not to integrins. Using mixed substrates in the gravity assay, all proteoglycan preparations inhibited cell attachment to fibronectin and vitronectin but not to collagen I and laminin. Although proteoglycan aggregates and monomers are more active than core proteins in inhibiting adhesion in the gravity assay, core proteins are still clearly active. A variety of control experiments suggest that the inhibition of cell attachment by proteoglycans is mediated through the specific interactions of proteoglycans with cell surface receptors, resulting in the inhibition of cell spreading. These results suggest at least two molecular mechanisms for proteoglycan-fibroblast interactions, one involving the chondroitin sulfate on the proteoglycan and an as yet unidentified receptor, the other involving the proteoglycan core protein and cell-associated hyaluronic acid.

scholarly journals Enhanced cell attachment using a novel cell culture surface presenting functional domains from extracellular matrix proteins

2008 ◽  
Vol 56 (2) ◽  
pp. 71-79 ◽  
Author(s):  
M. J. Cooke ◽  
S. R. Phillips ◽  
D. S. H. Shah ◽  
D. Athey ◽  
J. H. Lakey ◽  
...  
Keyword(s):  
Cell Culture ◽  
Extracellular Matrix ◽  
Cell Attachment ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Functional Domains ◽  
Culture Surface

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
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