Interaction of Trypanosoma cruzi adenylate cyclase with liver regulatory factors.
Trypanosoma cruzi adenylate cyclase catalytic subunits may interact with regulatory factors from rat liver membranes, reconstituting heterologous systems which are catalytically active in assay mixtures containing MgATP. The systems show stimulatory responses to glucagon and guanosine 5'-[beta gamma-imido]triphosphate (p[NH]ppG) or fluoride. Reconstitution was obtained by three different methods: fusion of rat liver membranes (pretreated with N-ethylmaleimide) to T. cruzi membranes; interaction of detergent extracts of rat liver membranes with T. cruzi membranes; or interaction of purified preparations of T. cruzi adenylate cyclase and of liver membrane factors in phospholipid vesicles. The liver factors responsible for the guanine nucleotide effect were characterized as the NS protein. Data also indicate that reconstitution requires the presence of a membrane substrate.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002772:Cholera Toxin / Q000494:pharmacology; D005934:Glucagon / Q000494:pharmacology; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D009243:NAD / Q000494:pharmacology; D009492:Neurospora crassa / Q000201:enzymology; D051381:Rats; D012969:Sodium Fluoride / Q000494:pharmacology; D014349:Trypanosoma cruzi / Q000201:enzymology*
D009243:NAD; D012969:Sodium Fluoride; D005934:Glucagon; D002772:Cholera Toxin; D000262:Adenylyl Cyclases