PHOSPHOLIPASE A(2) AND PROTEIN-KINASE-C ENZYMATIC-ACTIVITIES AND THEIR INTERACTIONS IN HYDRA-VULGARIS (Articolo in rivista)

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  • PHOSPHOLIPASE A(2) AND PROTEIN-KINASE-C ENZYMATIC-ACTIVITIES AND THEIR INTERACTIONS IN HYDRA-VULGARIS (Articolo in rivista) (literal)
Anno
  • 1995-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/0305-0491(94)00243-N (literal)
Alternative label
  • Borrelli L, Carginale V, Capasso A, Schneider T, Leitz T, De Petrocellis L, Di Marzo V. (1995)
    PHOSPHOLIPASE A(2) AND PROTEIN-KINASE-C ENZYMATIC-ACTIVITIES AND THEIR INTERACTIONS IN HYDRA-VULGARIS
    in Comparative biochemistry and physiology. B. Comparative biochemistry; Pergamon-Elsevier Science Ltd., Oxford (Regno Unito)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Borrelli L, Carginale V, Capasso A, Schneider T, Leitz T, De Petrocellis L, Di Marzo V. (literal)
Pagina inizio
  • 211 (literal)
Pagina fine
  • 219 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 111 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. CNR, IST CHIM MOLEC INTERESSE BIOL, NAPLES, ITALY 2. CNR, IST BIOCHIM PROT & ENZIMOL, NAPLES, ITALY 3. CNR, IST CIBERNETICA, 80072 Arco Felice, NAPLES, ITALY 4. UNIV HEIDELBERG, INST ZOOL, D-69120 HEIDELBERG, GERMANY (literal)
Titolo
  • PHOSPHOLIPASE A(2) AND PROTEIN-KINASE-C ENZYMATIC-ACTIVITIES AND THEIR INTERACTIONS IN HYDRA-VULGARIS (literal)
Abstract
  • Recent reports have assigned to activation of phospholipase A(2) (PLA(2)), with subsequent production of arachidonic acid (AA) and its derivatives, and to stimulation of protein kinase C (PKC), a key role in the control of body pattern, tentacle regeneration, and bud formation in two Hydra species, Experiments conducted in vivo suggested also the occurrence of a bidirectional interaction between the two enzymes during these processes. Here we describe for the first time the simultaneous partial characterization of PLA(2) and PKC activities in a hydrozoan species, the freshwater Hydra vulgaris. PLA(2) activity was found to be associated with membrane fractions, dependent on pH and on millimolar Ca2+ concentrations and counteracted by a specific inhibitor of mammalian membrane PLA(2), oleyloxyethyl-phosphoryl-choline (OOPC). A PKC-like enzyme with a molecular weight of about 70 kDa was partially purified from cytosolic extracts. Its activity was also found to depend on Ca2+ as well as phosphatidylserine, but was not influenced by AA. Conversely, the PKC activator tetradecanoylphorbol-11-acetate (TPA) induced PLA(2) activation and AA liberation in H. vulgaris polyps in vivo, While PKC-PLA(2) interactions have been extensively investigated in mammals, the present study represents the first example of PKC-induced activation of an invertebrate PLA(2). (literal)
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