Publications by authors named "T B Batikian"

Regularities of biologically active lipid metabolites formation in dynamics (5, 10, 30, 60 s) by phorbol 12-miristate 13-acetate stimulation in [14C]palmitic acid have been investigated in normal and leukemia peripheral blood lymphocytes prelabeled with [14C]palmitate. In normal cells there was two-phase formation of 1,2-diacylglycerol (5, 30 s), lysophosphatidylcholine (10, 60 s), as well as free palmitic acid at 10 s of stimulation. Under the identical experimental conditions there was inhibition of investigated lipid release processes at early (5 and 10 s) stages of stimulation of leukemic lymphocytes.

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The influence of a 30-day hypokinesia on the phosphoinositide cycle (PIC) initiation and on the inclusion of [14C]-arachidonic acid into cerebral synaptosome phospholipids was studied in rats. The results show that the catabolism of phospholipids prevails on the background of signal transduction in synaptosomes on the 30th day of hypokinesia. The effect of gamma-aminobutyric acid (GABA) is manifested by a sharp increase in the PIC activity 5 sec upon initiation and leads to normalization of the PIC activity in the late stage (5 min).

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Deacylation of the phosphatidylcholine fraction in plasma membranes of rat thymocytes and human blood lymphocytes was studied as well as its relationship to the activation of phosphoinositide-specific phosphodiesterase at early stages of mitogen-initiated phosphoinositide cycle. The data indicate that in lymphocyte membranes, enzymatic system of cascade deacylation of the phosphatidylcholine fraction includes calcium-activated phospholipase A1 and lysophospholipase. The enzyme system contributes to the rapid and reversible modification of the lipid bilayer of lymphocyte plasma membrane and can cooperate with phosphoinositide-specific phosphodiesterase during its activation at early stages of the initiation of phosphoinositide pathway during translocation of the external mitogenic signal.

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It has been shown for the first time that lysosomal (tritosomal) membranes of rat liver contain enzymes that are responsible for the deacylation-reacylation of phospholipids; their activity optimum lies at pH 7.0. Deacylation of lysosomal membrane phospholipids is controlled by a cascade of enzymatic reactions involving Ca2(+)-dependent phospholipase A1 which exhibits the maximal activity at 2.

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