scholarly journals Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans

2007 ◽  
Vol 28 (3) ◽  
pp. 209-221 ◽  
Author(s):  
Joan C. Marini ◽  
Antonella Forlino ◽  
Wayne A. Cabral ◽  
Aileen M. Barnes ◽  
James D. San Antonio ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Binding Sites ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Binding ◽  
Lethal Mutations ◽  
Helical Domain

scholarly journals Binding of soluble type I collagen to fibroblasts: effects of thermal activation of ligand, ligand concentration, pinocytosis, and cytoskeletal modifiers.

1982 ◽  
Vol 95 (3) ◽  
pp. 747-751 ◽  
Author(s):  
B D Goldberg
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Thermal Activation ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Binding ◽  
Bacterial Collagenase ◽  
Ligand Interactions ◽  
Organizing Center ◽  
High Ligand

Efficient binding of native, soluble 125I-labeled type I rat collagen to mouse 3T3 fibroblast monolayers requires prior warming of the ligand to 35-37 degrees C for 10-30 min. Decreased binding at high ligand concentrations is ascribed to ligand-ligand interactions rather than to negative cooperativity. Addition of bacterial collagenase to monolayers labeled with the 125I-ligand releases a constant fraction (80%) of the bound ligand over a 2-h interval at 37 degrees C, indicating that little of the ligand becomes inaccessible by pinocytosis. Colchicine (10(-7) M) and vinblastine (5 X 10(-8) M) do not inhibit binding by morphologically intact monolayers. Cytochalasins and concanavalin A show dose-related inhibition of binding by intact monolayers that is due to a reduction in the number of available binding sites rather than to a change in binding site affinity. The collagen binding site on the fibroblast surface is proposed as an organizing center for the assembly of periodic type I collagen fibrils.

Sign in / Sign up

Export Citation Format

Share Document