The extracellular matrix proteins laminin and fibronectin modify the AMPase activity of 5'-nucleotidase from chicken gizzard smooth muscle.
Laminin and fibronectin, but not collagen, affect the AMPase activity of the purified transmembrane protein 5'-nucleotidase. Laminin stimulates whereas fibronectin inhibits the AMPase activity of this ectoenzyme. The AMPase-modulating effects by these components of the extracellular matrix require a preincubation period of several hours when detergent-solubilized 5'-nucleotidase is employed, they can, however, instantaneously be elicited with liposome-incorporated 5'-nucleotidase.
D015720:5'-Nucleotidase; D000249:Adenosine Monophosphate / Q000378:metabolism; D000818:Animals; D003094:Collagen / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism*; D000070559:Gizzard, Non-avian / Q000201:enzymology; D007797:Laminin / Q000378:metabolism*; D008081:Liposomes; D009130:Muscle, Smooth / Q000201:enzymology; D009708:Nucleotidases / Q000378:metabolism*
D005353:Fibronectins; D007797:Laminin; D008081:Liposomes; D000249:Adenosine Monophosphate; D003094:Collagen; D009708:Nucleotidases; D015720:5'-Nucleotidase