Regulation Of Acid Phosphatase Research Articles

Ameliorative potential of Astaxanthin on glyphosate-induced neurocognitive functional changes in adult zebrafish via acid phosphatase and annexin A2 dysfunction

Glyphosate (GYP) is a phosphonate type of herbicide and potentially causes neurodegenerations. Astaxanthin (AST) is a red pigment and it is a group of carotenoids. It possesses the potential antioxidants and neuroprotective actions. However, the ameliorative role of AST in GYP- induced neurocognitive dysfunction has not been studied yet. Hence, the present study is designed to investigate the ameliorative potential of AST in GYP-induced cognitive dysfunction via regulations of acid phosphatase (AP) and annexin A2 (AXA2) actions in the zebrafish model. The cognitive dysfunction was induced by exposure to GYP (0.5 mg/L for 30 minutes/day) for 14 consecutive days. The AST (50, 75, and 100 mg/L for 30 minutes/day) and reference drug i.e., donepezil (DP; 1 µg/mL for 30 minutes/day) were exposed for 14 consecutive days before GYP exposure. On the 14th day, cognitive changes i.e., three horizontal compartment test,optokinetic motor response (OMR), startle response (SR), and T-maze tests were assessed. The changes of biomarkers i.e., acetylcholinesterase (AChE) activity, thiobarbituric acid reactive substances (TBARS), reduced glutathione (GSH), AP, and AXA2 levels were estimated in brain tissue. The administration of AST ameliorates the GYP-induced neurocognitive dysfunctions via the antioxidant, regulation of AP and AXA2 actions. Hence, it can be used for neurocognitive disorders against the phosphonate type of herbicide (GYP) toxicity.

Regulation of acid phosphatase in reverse micellar system by lipids additives: Structural aspects

Reverse micelles system is suggested as a direct tool to study the influence of membrane matrix composition on the activity and structure of membrane-associated enzymes with the use of acid phosphatase (AP) as an example. In reverse micelles the functioning of the monomeric and dimeric forms of AP could be separately observed by variation of the size of the micelles. We found that including the lipids into the micellar system can dramatically affect the enzyme functioning even at low lipid content (2% w/w), and this effect depends on the lipid nature. Structural studies using CD spectroscopy and DLS methods have shown that the influence of lipid composition on the enzyme properties might be caused by the interaction of lipids with the enzyme as well as by the influence of lipids on structure and properties of the micellar matrix.

Methyl jasmonate induces acid phosphatase activity in rice leaves

Summary Regulation of acid phosphatase (APase) activity by methyl jasmonate (MJ) in detached rice (Oryza sasiva cv. Taichung Native 1) leaves was examined. MJ and jasmonic acid increased APase activity by up to 5-fold in detached rice leaves in the light. MJ also increased APase activity in detached leaves of five other rice cultivars and in detached leaves of oats, maize and sorghum in the light. MJ increased APase activity within 8 h of its application under light. APase activity was induced when detached rice leaves were exposed to MJ in darkness, although APase activity was lower than in those exposed to light. Cycloheximide completely abolished MJ-induced APase activity in the light. The results suggest that MJ-induced APase activity is due to de novo APase synthesis.

Regulation of acid phosphatase by gibberellic acid in embryo-less half-seeds of wheat

Approximately 4–5-fold stimulation of acid phosphatase activity was witnessed in embryo-less half-seeds of wheat in response to gibberellic acid (GA 3) (48 h). This enzyme activity was secreted into the incubation medium. The increase in enzyme activity in GA 3-treated wheat half-seeds was inhibited significantly by cordycepin, cycloheximide (CHI) and amino acid analogues. This indicated the requirement of fresh transcription and translation for the GA 3-regulated acid phosphatase activity. Abscisic acid completely abolished the GA 3-induced acid phosphatase activity. Conclusive proof for de novo synthesis of acid phosphatase in GA 3-treated half-seeds was achieved by the in vivo labelling of enzyme with [ 35S]sulphate. The label was recovered in the cysteine residues of the purified enzyme. Acid phosphatase was purified (109-fold) to electrophoretic homogeneity by Con A-agarose affinity chromatography. The molecular weight of the native enzyme is 185 000 as determined by molecular sieve chromatography on Sepharose CL-6B. The K m of the enzyme for p-nitrophenyl phosphate is 5 × 10 −4 M. The pH optimum of the purified enzyme was 5.0. The enzyme activity was completely inhibited by NaF (2 mM). Both β-mercapto-ethanol (10 mM) and dithiothreitol (10 mM) brought about a 2.5–3-fold activation of acid phosphatase, thereby indicating the requirement of free sulfhydryl groups for the catalytic efficiency of the enzyme.

Phosphorus metabolism and activity of some enzymes during the metamorphosis of the mealworm, Tenebrio molitor Linnaeus

1. 1. Phosphorus metabolism during metamorphosis of the beetle, Tenebrio molitor, was studied. 2. 2. The levels of acid and alkaline phosphatases activities were determined in relation to free and total phosphate. 3. 3. A parallel study was also carried out on the levels of isocritrate dehydrogenase, glucose 6-P dehydrogenase and glyceraldehyde 3-P dehydrogenase in order to investigate the correlation between phosphorus metabolism and other metabolic pathways. 4. 4. A discussion about a possible regulation of acid phosphatase by phosphate is presented.