acid-phosphatase and Liver-Diseases--Alcoholic

To find out the active principles against ethanol-induced toxicity in mice, Andrographis paniculata Nees. (Ap) was chosen and isolated andrographolide (ANDRO) and arabinogalactan proteins (AGPs). ANDRO was detected by HPTLC, FTIR and quantified by HPLC (10mg/g of Ap powder). AGPs was detected by beta-glucosyl Yariv staining of SDS-PAGE gel, FTIR and quantified by single radial gel diffusion assay with beta-glucosyl Yariv reagent (0.5mg/g Ap powder). The mice are pretreated intra-peritoneally (i.p.) with different doses (62.5, 125, 250, and 500mg/kg) of body weight of mice] of ANDRO and AGPs for 7 days and then ethanol (7.5g/kg of body weight) was injected, i.p. Besides, silymarin was used as standard hepatoprotective agent for comparative study with ANDRO and AGPs. The ameliorative activity of ANDRO and AGP against hepatic renal alcohol toxicity was measured by assessing GOT, GPT, ACP, ALP and LP levels in liver and kidney. It has been observed that pretreatment of mice with ANDRO and AGPs at 500mg/kg of body weight and 125mg/kg of body weight respectively could able to minimize the toxicity in compare to ethanol treated group as revealed by the different enzymatic assay in liver and kidney tissues and the results were comparable with silymarin. Hence, out of several ill-defined compounds present in Ap, ANDRO and AGPs are the potential bioactive compounds responsible for protection against ethanol-induced toxicity.

Topics: Acid Phosphatase; Alkaline Phosphatase; Andrographis; Animals; Aspartate Aminotransferases; Central Nervous System Depressants; Chromatography, High Pressure Liquid; Disease Models, Animal; Diterpenes; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Ethanol; Galactans; Glucosides; India; Kidney Diseases; Lipid Peroxidation; Liver Diseases, Alcoholic; Male; Mice; Phloroglucinol; Protective Agents; Silymarin; Spectroscopy, Fourier Transform Infrared

Protein accumulation in liver cells contributes to alcohol-induced hepatomegaly and is the result of an ethanol-elicited deceleration of protein catabolism (Alcohol Clin Exp Res 13:49, 1989). Because lysosomes are active in the degradation of most hepatic proteins, the present studies were conducted to determine whether ethanol administration altered the proteolytic activities of partially purified hepatic lysosomes. Rats were fed liquid diets containing either ethanol (36% of calories) or isocaloric maltodextrin for periods of 2-34 days. Prior to death, all animals were injected with [3H]leucine to label hepatic proteins. Rats subjected to even brief periods of ethanol feeding (2-8 days) exhibited significant hepatomegaly and hepatic protein accumulation compared with pair-fed control animals. Crude liver homogenates and isolated lysosomal-mitochondrial and cytosolic subfractions were incubated at 37 degrees C, and the acid-soluble radioactivity generated during incubation was measured as an index of proteolysis. At neutral pH, in vitro protein breakdown in incubated liver homogenates and subcellular fractions from control and ethanol-fed rats did not differ significantly. The extent of protein hydrolysis increased when samples were incubated at pH 5.5, which approximates the pH optimum for catalysis by lysosomal acid proteases. Under the latter conditions, partially purified lysosomes from control animals had 2-fold higher levels of proteolysis than corresponding fractions from ethanol-fed rats. The difference in proteolytic capacity appeared to be related to a lower latency and a higher degree of fragility of lysosomes from ethanol-fed rats at the acidic pH.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acid Phosphatase; Alcohol Drinking; Animals; beta-Galactosidase; Cathepsin B; Ethanol; Fasting; Hydrogen-Ion Concentration; Liver; Liver Diseases, Alcoholic; Lysosomes; Organ Size; Peptide Hydrolases; Proteins; Rats; Subcellular Fractions

A comparative evaluation of the morphohistochemical changes in the liver in adult and young animals following a two-month alcohol intoxication revealed the following changes in the younger animals: the absence of lymphocytic-macrophagal infiltrates, a larger number of binuclear cells and the appearance of large amounts of lymphocytes with a marked positive reaction to alkaline phosphatase.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Liver; Liver Diseases, Alcoholic; Lymphocytes; Macrophages; Male; Rats

Sera from 9 persons with either biopsy-proven alcoholic liver disease or a history of chronic, excessive ethanol consumption were analyzed for their content of various hydrolases. Compared to controls, significant elevations in the following enzyme activities were seen in sera from the patient population: acid phosphatase (2.0-fold), beta-glucuronidase (2.1-fold), hexosaminidase (1.4-fold), and alpha-L-fucosidase (2.3-fold). In addition, alpha-mannosidase activity, previously reported to be unchanged in cases of hepatic cirrhosis [Reglero et al., Clinica chim. Acta 130: 155-158], (1980) was found to be significantly increased (p less than 0.001) when assays were performed at acid (pH 4.5) or intermediate (pH 5.5) hydrogen ion concentrations. Fractionation of sera on DEAE-Sephadex columns showed that the increase in alpha-mannosidase activity in the serum of patients with alcoholic liver disease was due to increases in the level of at least one 'acid alpha-mannosidase' and two intermediate pH optimum alpha-mannosidases. The general increase in the activity of a group of glycosidases is consistent with a hypothesis involving decreased clearance of glycoproteins from the blood of persons with hepatic cirrhosis.

Topics: Acid Phosphatase; Adult; Aged; Alcoholism; alpha-L-Fucosidase; alpha-Mannosidase; Female; Glucuronidase; Hexosaminidases; Humans; Isoenzymes; Liver; Liver Cirrhosis, Alcoholic; Liver Diseases, Alcoholic; Male; Mannosidases; Middle Aged

Topics: Acid Phosphatase; Animals; Female; Haplorhini; Histocytochemistry; Liver; Liver Diseases, Alcoholic; Lysosomes; Macaca; Macaca radiata; Male; Microscopy, Electron