Cross-linking and binding of fibronectin with asymmetric acetylcholinesterase.
The similarities between the tail of asymmetric acetylcholinesterase (AcChE) and collagen prompted us to investigate if asymmetric AcChE, like collagen, can interact with fibronectin. Gradient centrifugation studies revealed that asymmetric, but not globular, AcChE bound to fibronectin and could be cross-linked covalently to fibronectin by plasma transglutaminase. The interaction of asymmetric AcChE with fibronectin paralleled the interaction of fibronectin with collagen. These results raise the possibility that fibronectin may be involved in attaching asymmetric AcChE to cell surfaces.
D000110:Acetylcholinesterase / Q000378:metabolism; D000818:Animals; D003094:Collagen; D003902:Detergents; D005353:Fibronectins / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D009132:Muscles / Q000201:enzymology; D017830:Octoxynol; D011092:Polyethylene Glycols; D011485:Protein Binding; D011784:Quail; D012710:Serum Albumin, Bovine; D014357:Trypsin
D003902:Detergents; D005353:Fibronectins; D046911:Macromolecular Substances; D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols; D017830:Octoxynol; D003094:Collagen; D000110:Acetylcholinesterase; D014357:Trypsin