title: Regulation of protein kinase FA (a transmembrane signal of insulin and epidermal growth factor) in the brain.
abstract: Two forms of type-1 protein phosphatase activating factor (FA) termed FA1 and FA2 have been identified in plasma membranes of pig brain. FA1 is spontaneously active and trypsin-labile whereas FA2 is inactive and trypsin-resistant. Phospholipid reconstitution studies further indicate that the FA activity in the neutral phospholipids-reconstituted complex is spontaneously active and trypsin-labile whereas the FA activity in the acidic phospholipids-reconstituted complex is trypsin-resistant and inactive. The results indicate that inactive FA2 may have its catalytic domain interacted with negatively-charged phospholipids in brain membranes. This provides initial evidence for the regulation of protein kinase FA (a transmembrane signal of insulin and epidermal growth factor) in the central nervous system.
authors.affiliation: Institute of Molecular Cell Biology, Chang Gung Medical College, Tao-Yuan, Taiwan, Republic of China.
authors.forename: S D
authors.initials: SD
authors.lastname: Yang
authors.forename: J S
authors.initials: JS
authors.lastname: Yu
authors.forename: H C
authors.initials: HC
authors.lastname: Chen
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism*; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002462:Cell Membrane / Q000378:metabolism; D004815:Epidermal Growth Factor / Q000502:physiology*; D006706:Homeostasis; D007328:Insulin / Q000502:physiology*; D007700:Kinetics; D010743:Phospholipids / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*; D015398:Signal Transduction; D013552:Swine; D014357:Trypsin
chemical_list: D007328:Insulin; D010743:Phospholipids; D004815:Epidermal Growth Factor; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D010749:Phosphoprotein Phosphatases; D014357:Trypsin