acid-phosphatase and Fever

This study was conducted to evaluate the effect of p-Coumaric acid, a common dietary phenol, on monosodium urate crystal-induced inflammation in rats-an experimental model for acute gouty arthritis.. Paw edema, levels/activities of lysosomal enzymes, lipid peroxidation, enzymic antioxidants and a histopathological examination of ankle joints were evaluated in control and monosodium urate crystal-induced inflamed rats. Further, an acetic acid-induced writhing test and tail immersion test were employed to screen for analgesic effects, yeast-induced pyrexia was used to test for antipyretic effects, and gastric ulceration was used to evaluate ulcerogenic effects.. A significant increase in paw edema, lysosomal enzyme activity and lipid peroxidation levels was observed in monosodium urate crystal-induced rats, whereas activities of enzymic antioxidants were found to be decreased when compared to control rats. Nevertheless, treatment with p-Coumaric acid (100 mg/kg b.wt) significantly reverted the altered physical and biochemical parameters back to near normal levels, as evidenced by the histopathology of the ankle joints. In addition, p-Coumaric acid also exhibited potent analgesic and antipyretic effects devoid of any adverse impact on gastric mucosa.. The results of this study reveal the potential anti-inflammatory effect of p-Coumaric acid against monosodium urate crystal-induced inflammation in rats.

Topics: Acetic Acid; Acid Phosphatase; Analgesics; Animals; Anti-Inflammatory Agents; Antipyretics; beta-Glucosidase; Catalase; Coumaric Acids; Diet; Female; Fever; Glucuronidase; Hexosaminidases; Inflammation; Lipid Peroxidation; Male; Pain; Propionates; Rats; Rats, Wistar; Saccharomyces cerevisiae; Superoxide Dismutase; Uric Acid

Activity of acid and alkaline phosphatases, as well as isoenzymes of alkaline phosphatase in the lymph of the thoracic lymphatic duct, hepatic lymph and the peripheral blood have been studied on rabbits in the dynamics of the fever reaction of different duration. The fever reaction was followed by enzyme activity increase in all the body biologic fluids. However the degree of increase of their activity in the lymph was greater that that in the blood. Our data indicate that in the transport of phosphatases released from the tissues in the common circulation the essential role is played by the lymphatic system, the resorption and transport functions of which significantly characterise the dynamics and the level of their changes in the blood in fever reaction.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Fever; Isoenzymes; Lipopolysaccharides; Lymph; Pyrogens; Rabbits; Time Factors

Intravenous injection of E. coli LPS (0.5 micrograms/kg) produced the biphasic elevation of rectal temperature (TR) in conscious oxen. The fever was accompanied by a significant increase of the arylsulphatase A (AsA) activities in plasma and in mononuclear leucocytes. In polymorphonuclear cells a substantial decrease of the AsA activity after 1 hr fever was observed. After 3.5 hr of fever the polymorphonuclear activity of AsA restored to normal found before LPS administration. In contrast with AsA, the pyrogenic dose of LPS caused negligible changes of the acid phosphatase (AcP) activities in the sampled materials. Daily-repeated injections of pyrogen into the same oxen attenuated magnitudes of fever as well as AsA responses in plasma and granulocytes. Heat-induced hyperthermia provoked only minute changes of the AsA and AcP.

Topics: Acid Phosphatase; Animals; Cattle; Cerebroside-Sulfatase; Fever; Kinetics; Lipopolysaccharides; Neutrophils; Sulfatases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Ascorbic Acid; Electron Transport Complex IV; Fever; Oxidoreductases; Phosphoric Monoester Hydrolases; Rats; Succinate Dehydrogenase; Thyroid Gland

Only intact exudate granulocytes from rabbits generated large amounts of endogenous pyrogen when incubated in 0.15 M NaCl. No matter how whole-cell lysates or combinations of subcellular fractions were incubated, their yields of pyrogen never approached those of whole cells; at most, only minimal amounts of pyrogen were formed, once the integrity of the cells had been destroyed. Some pyrogen could be extracted from disrupted cells, but never more than a fraction (<25%) of that released from incubated whole cells. The yield could be slightly improved by lowering the pH (to 3.5) and by increasing the volume of extraction fluid. Virtually all of the preformed pyrogen that could be extracted from sucroselysed cells was found in their cytoplasmic fraction. Contrary to the results of Herion et al. (3), none could be detected in the granular (or lysosomal) fraction. Likewise, all efforts to recover pyrogen from the membrane-nuclear fraction were unsuccessful. In keeping with the finding that preformed pyrogen is contained in the cytoplasmic fraction were the observations that practically all of the aldolase, a cytoplasmic enzyme, and very little of the acid phosphatase, a granular enzyme, were lost from the cells during the release of pyrogen. Lysozyme, an enzyme stored in both the granules and the cytoplasm, was partially released from the cells under the same circumstances. Neither the release of pyrogen nor its slight intracellular buildup that precedes release (4) were affected by concentrations of puromycin that block protein synthesis in the cells and prevent their activation. Hence, it is concluded that the release process, which also involves the formation of active pyrogen (4), does not require protein synthesis, whereas activation of the cells, which may involve the synthesis of an inactive precursor (2), does.

Topics: Acid Phosphatase; Animals; Colchicine; Cytoplasm; Exudates and Transudates; Fever; Fructose-Bisphosphate Aldolase; Lactates; Leukocytes; Muramidase; Neutrophils; Phagocytosis; Puromycin; Pyrogens; Rabbits

Topics: Acid Phosphatase; Alanine Transaminase; Alcohol Oxidoreductases; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Fever; Fructose-Bisphosphate Aldolase; Glutamate Dehydrogenase; L-Lactate Dehydrogenase; Malate Dehydrogenase; Male; Rats; Sorbitol

Topics: Acid Phosphatase; Body Temperature Regulation; Diuresis; Endotoxins; Fever; Glucuronidase; Humans; Hydrocortisone; Sweating; Vasopressins