title: Protein kinases in mitochondria of the invertebrate Artemia franciscana.
abstract: The information concerning protein kinases in animal mitochondria is scarce and related only to mammals. No data are available for invertebrates. We demonstrate here the presence of casein kinase II (CK II) and cAMP-dependent protein kinase (PKA) in the purified mitochondria of the crustacean Artemia franciscana. Whereas the mitochondrial CK II showed the same characteristics of the cytosolic enzyme, mitochondrial PKA had an apparent Km for its substrate Kemptide 1 order of magnitude lower than that of the cytosolic enzyme. CK II and PKA phosphorylate different sets of proteins in Artemia mitochondria in vitro. The use of an activity gel assay has allowed the detection of additional protein kinases, as yet unidentified, in Artemia mitochondria.
authors.affiliation: Instituto de Investigaciones Biomédicas (CSIC), Facultad de Medicina (UAM), Arturo Duperier, Madrid, Spain. cvallejo@biomed.iib.uam.es
authors.forename: C G
authors.initials: CG
authors.lastname: Vallejo
authors.forename: A M
authors.initials: AM
authors.lastname: Seguido
authors.forename: M
authors.initials: M
authors.lastname: Fernández-Renart
mesh_terms: D000818:Animals; D001156:Artemia / Q000201:enzymology*; D047390:Casein Kinase II; D002500:Centrifugation, Isopycnic; D017868:Cyclic AMP-Dependent Protein Kinases / Q000032:analysis*; D003600:Cytosol / Q000201:enzymology; D006493:Heparin / Q000494:pharmacology; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology* / Q000378:metabolism; D010748:Phosphopeptides / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000378:metabolism
chemical_list: D010748:Phosphopeptides; D006493:Heparin; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D017868:Cyclic AMP-Dependent Protein Kinases