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1.
Article in English | MEDLINE | ID: mdl-10374257

ABSTRACT

With the aim of examining the response of plant cells to UV-C irradiation, we investigated the behaviour of the phosphatidylinositol 4,5 bisphosphate (PtdIns 4,5-P2) molecule (the precursor of the phosphoinositide signal transduction cascade) by exposing callus cells from Peucedanum verticillare to UV-C (130 J m-2) and by examining the level and the fatty acid composition of PtdIns 4,5-P2 at different times after irradiation. We show that a pathway for the UV-C response includes transient PtdIns 4,5-P2 breakdown. The effect of ultraviolet rays is mimicked by H2O2 suggesting that in this plant it may be brought about by reactive oxygen intermediates (ROI), as already underlined in experimental animal models.


Subject(s)
Phosphatidylinositols/metabolism , Plants/metabolism , Plants/radiation effects , Reactive Oxygen Species/metabolism , Animals , Fatty Acids/analysis , Hydrogen Peroxide/pharmacology , Phosphatidylinositol 4,5-Diphosphate/metabolism , Phosphatidylinositols/radiation effects , Plant Cells , Plants/drug effects , Ultraviolet Rays
2.
Radiobiologiia ; 32(6): 807-14, 1992.
Article in Russian | MEDLINE | ID: mdl-1494647

ABSTRACT

It has been shown that single local X-irradiation (0.21 C/kg) of the rabbit hind limb in the early period of acute radiation injury (1 and 14 h) causes a decrease in saturation of sarcoplasmic reticulum membrane lipids. It is mainly connected with a decreased saturation of the total fraction of phosphatidyl serine, phosphatidyl inositol and phosphatidyl choline. The above changes can increase permeability of the sarcoplasmic reticulum membranes for Ca(2+)-ion after X-irradiation.


Subject(s)
Membrane Lipids/radiation effects , Radiation Injuries, Experimental/metabolism , Sarcoplasmic Reticulum/radiation effects , Acute Disease , Animals , Female , Male , Phosphatidylcholines/radiation effects , Phosphatidylinositols/radiation effects , Phosphatidylserines/radiation effects , Rabbits , Radiation Dosage , Time Factors
3.
Biochem Biophys Res Commun ; 156(3): 1111-9, 1988 Nov 15.
Article in English | MEDLINE | ID: mdl-2847726

ABSTRACT

In the rat retina, light-induced break down of polyphosphoinositides and structural alterations of photoreceptor outer segment disk-membranes were enhanced by chronic lithium treatment at doses equivalent to therapeutic levels in humans. Furthermore, the recovery of phosphoinositide baseline levels after light exposure was delayed in lithium treated retinas. Light and lithium may thus affect phospholipid membranes in the retina. Initial processes in the pathogenesis of light damage in the retina are largely unknown to date. The hydrolysis of polyphosphoinositides may possibly constitute such an initial event.


Subject(s)
Light , Lithium/pharmacology , Phosphatidylinositols/radiation effects , Retina/radiation effects , Animals , Male , Membrane Lipids/analysis , Microscopy, Electron , Phosphatidylinositols/analysis , Phospholipids/analysis , Photoreceptor Cells/drug effects , Photoreceptor Cells/radiation effects , Rats , Retina/drug effects , Retina/ultrastructure , Time Factors
4.
J Biol Chem ; 263(1): 17-20, 1988 Jan 05.
Article in English | MEDLINE | ID: mdl-2826436

ABSTRACT

Light stimulates the hydrolysis of exogenous, [3H]inositol-labeled phosphatidylinositol bisphosphate (PtdInsP2) added to squid photoreceptor membranes, releasing inositol trisphosphate (InsP3). At free calcium levels of 0.05 microM or greater, hydrolysis of the labeled lipid is stimulated up to 4-fold by GTP and light together, but not separately. This activity is the biochemical counterpart of observations on intact retina showing that a rhodopsin-activated GTP-binding protein is involved in visual transduction in invertebrates, and that InsP3 release is correlated with visual excitation and adaptation. Using an in vitro assay, we investigated the calcium and GTP dependence of the phospholipase activity. At calcium concentrations between 0.1 and 0.5 microM, some hydrolysis occurs independently of GTP and light, with a light- and GTP-activated component superimposed. At 1 microM calcium there is no background activity, and hydrolysis absolutely requires both GTP and light. Ion exchange chromatography on Dowex 1 (formate form) of the water-soluble products released at 1 microM calcium reveals that the product is almost entirely InsP3. Invertebrate rhodopsin is homologous in sequence and function to vertebrate visual pigment, which modulates the concentration of cyclic GMP through the mediation of the GTP-binding protein transducin. While there is some evidence that light also modulates PtdInsP2 content in vertebrate photoreceptors, the case for its involvement in phototransduction is stronger for the invertebrate systems. The results reported here support the scheme of rhodopsin----GTP-binding protein----phospholipase C activation in invertebrate photoreceptors.


Subject(s)
Guanosine Triphosphate/pharmacology , Phosphatidylinositols/metabolism , Photoreceptor Cells/metabolism , Animals , Cell Membrane/metabolism , Cell Membrane/radiation effects , Decapodiformes , Kinetics , Light , Phosphatidylinositol 4,5-Diphosphate , Phosphatidylinositols/radiation effects , Photoreceptor Cells/drug effects , Photoreceptor Cells/radiation effects
5.
Article in Russian | MEDLINE | ID: mdl-2849483

ABSTRACT

The content of polyphosphoinositides and phosphatidic acid increases in the squid axon under the action of laser radiation and the content of monophosphoinsitide decreases. At the same time the absorption of calcium ions by axon decreases. It is suggested that the laser radiation intensifies the synthesis of polyphosphoinositides and inhibits the system responsible for their degradation as well causes the desorption of the surface-bound calcium.


Subject(s)
Axons/radiation effects , Calcium/radiation effects , Lasers , Phosphatidylinositols/radiation effects , Absorption , Animals , Axons/metabolism , Calcium/metabolism , Decapodiformes , Electric Stimulation , Phosphatidylinositols/metabolism
6.
Biochem Biophys Res Commun ; 124(2): 503-6, 1984 Oct 30.
Article in English | MEDLINE | ID: mdl-6093803

ABSTRACT

Isolated frog (Rana Pipiens) retinas were labeled in the dark with either [32P] PO4-orthophosphate or myo-[2-3H]inositol for 2.5-4 hrs. After washing the retinas with cold buffer, they were exposed to brief flashes of light (5 secs or 15 secs) and their rod outer segments isolated. Upon separation of labeled phospholipids, a specific decrease in label in phosphatidylinositol 4,5-bisphosphate was observed, whereas there was no significant effect on the labeling of phosphatidylinositol 4-phosphate, phosphatidylinositol, or phosphatidic acid. These results are indicative of a light-activated phosphatidylinositol 4,5-bisphosphate-specific phospholipase C in frog rod outer segments.


Subject(s)
Light , Phosphatidylinositols/radiation effects , Retina/radiation effects , Animals , Darkness , Phosphatidylinositol 4,5-Diphosphate , Phosphatidylinositols/metabolism , Phosphorus Radioisotopes , Rana pipiens , Retina/metabolism , Tritium
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