title: Involvement of adenylate cyclase and tyrosine kinase signaling pathways in response of crayfish stretch receptor neuron and satellite glia cell to photodynamic treatment.
abstract: Neuroglial interactions are most profound during development or damage of nerve tissue. We studied the responses of crayfish stretch receptor neurons (SRN) and satellite glial cells to photosensitization with sulfonated aluminum phthalocyanine Photosens. Although Photosens was localized mainly in the glial envelope, neurons were very sensitive to photodynamic treatment. Photosensitization gradually inhibited and then abolished neuron activity. Neuronal and glial nuclei shrank. Some neurons and glial cells lost the integrity of the plasma membrane and died through necrosis after the treatment. The nuclei of other glial cells but not neurons become fragmented, indicating apoptosis. The number of glial nuclei around neuron soma increased, probably indicating proliferation for enhanced neuron protection. Adenylate cyclase (AC) inhibition by MDL-12330A, or tyrosine kinase (TK) inhibition by genistein, shortened neuron lifetime, whereas AC activation by forskolin or protein tyrosine phosphatases (PTP) inhibition by sodium orthovanadate prolonged neuronal activity. Therefore, cAMP and phosphotyrosines produced by AC and TK, respectively, protected SRN against photoinactivation. AC inhibition reduced photodamage of the plasma membrane and subsequent necrosis in neuronal and glial cells. AC activation prevented apoptosis in photosensitized glial cells and stimulated glial proliferation. TK inhibition protected neurons but not glia against photoinduced membrane permeabilization and subsequent necrosis whereas PTP inhibition more strongly protected glial cells. Therefore, both signaling pathways involving cAMP and phosphotyrosines might contribute to the maintenance of neuronal activity and the integrity of the neuronal and glial plasma membranes. Adenylate cyclase but not phosphotyrosine signaling pathways modulated glial apoptosis and proliferation under photooxidative stress.
authors.affiliation: Department of Biophysics and Biocybernetics, Rostov State University, 194/1 Stachky ave., Institute of Neurocybernetics, Rostov-on-Don 344090, Russia. uzd@krinc.ru
authors.forename: Anatoly
authors.initials: A
authors.lastname: Uzdensky
authors.forename: Mikhail
authors.initials: M
authors.lastname: Kolosov
authors.forename: Denis
authors.initials: D
authors.lastname: Bragin
authors.forename: Olga
authors.initials: O
authors.lastname: Dergacheva
authors.forename: Olga
authors.initials: O
authors.lastname: Vanzha
authors.forename: Lidiya
authors.initials: L
authors.lastname: Oparina
mesh_terms: D000262:Adenylyl Cyclases / Q000502:physiology* / Q000528:radiation effects*; D000818:Animals; D003400:Astacoidea; D007211:Indoles / Q000494:pharmacology; D009470:Muscle Spindles / Q000187:drug effects / Q000201:enzymology / Q000528:radiation effects*; D009457:Neuroglia / Q000187:drug effects / Q000201:enzymology / Q000528:radiation effects; D009942:Organometallic Compounds / Q000494:pharmacology; D011505:Protein-Tyrosine Kinases / Q000502:physiology* / Q000528:radiation effects*; D027161:Satellite Cells, Perineuronal / Q000187:drug effects / Q000201:enzymology / Q000528:radiation effects*; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology* / Q000528:radiation effects
chemical_list: D007211:Indoles; D009942:Organometallic Compounds; C048577:aluminum tetrasulfophthalocyanine; D011505:Protein-Tyrosine Kinases; D000262:Adenylyl Cyclases