title: Minor participation of cAMP on the protein kinase phosphorylation of mitochondrial and cytosolic fractions from Ascaris suum: a comparative study with porcine heart muscle.
abstract: In contrast to porcine heart muscle in which cAMP effectively activated the phosphorylation of cytosolic proteins, cAMP exerted a minor effect on the phosphorylation of proteins from the soluble fraction of Ascaris suum muscle. Similarly, cAMP did not enhance the kinase activity in the mitochondrial membranes from porcine heart and A. suum, although major differences in protein phosphorylation were observed between both fractions. However, cAMP-dependent protein kinases (PKA) were evidenced in the parasitic soluble mitochondrial fraction, since the phosphorylation of histone IIA and kemptide was augmented in this fraction, in the presence of cAMP. An increase in the phosphorylation of exogenously added A. suum phosphofructokinase was also obtained when cAMP was added to the parasite soluble mitochondrial fraction. The phosphorylation of phosphofructokinase by this fraction was inhibited when kemptide and cAMP were included in the reaction mixture, suggesting substrate competition for the same PKA. Although PKI (6-22), a reported inhibitor of the catalytic subunit of mammalian cAMP-dependent PKAs, did not affect the endogenous phosphorylation of proteins in the various A. suum fractions, an inhibition on the phosphorylation of exogenously added kemptide and phosphofructokinase was observed when PKI (6-22) was incubated with the parasite mitochondrial soluble fraction.
authors.affiliation: Departamento de Biología Celular, División de Ciencias Biológicas, Universidad Simón Bolivar, Apartado 89.000, Caracas 1081-A, Venezuela. calaboki@usb.ve
authors.forename: Maritza
authors.initials: M
authors.lastname: Calabokis
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Perez
authors.forename: José
authors.initials: J
authors.lastname: Bubis
authors.forename: Zadila
authors.initials: Z
authors.lastname: Suárez-Mata
mesh_terms: D000818:Animals; D017165:Ascaris suum / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D000242:Cyclic AMP / Q000494:pharmacology*; D017868:Cyclic AMP-Dependent Protein Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism; D003600:Cytosol / Q000187:drug effects* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005631:Fructokinases / Q000378:metabolism; D005720:Gamma Rays; D008929:Mitochondria, Heart / Q000187:drug effects* / Q000378:metabolism; D009206:Myocardium / Q000201:enzymology* / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D013552:Swine
chemical_list: D011506:Proteins; D000242:Cyclic AMP; D011494:Protein Kinases; D005631:Fructokinases; C046173:fructokinase; D017868:Cyclic AMP-Dependent Protein Kinases