Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The number of white blood cells and of polymorphonuclear leukocytes remained unchanged in vervet monkeys (Cercopithecus aethiops) receiving a "O" protein diet. The motility of the polymorphonuclear leukocytes and their phagocytic and killing indices with and without leukokinin stimulation decreased in protein-depleted animals. Acid cathepsin decreased, DNA relatively increased, and peroxidase, alkaline phosphatase, acid phenylphosphatase, and lysozyme reached higher levels in the polymorphonuclear leukocytes of animals on a "O" protein diet.
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PMID:Polymorphonuclear neutrophilic leukocytes in protein deficiency. 40 70

Endometrial cells isolated from uteri of ovariectomized rats were treated in vitro with 1 X 10(-9) M estradiol-17 beta (E2beta) to analyze early changes in membrane properties during hormone-induced growth. After 30-min exposure to E2beta at 22 degrees C, cells exhibited an enhanced capacity to bind erythrocytes (hemadsorption) in the presence of concanavalin A (Con A) to 237% of the level in paired controls. Fluorescence microscopy revealted that approximately 25% of cells exposed to E2beta, but not estradiol-17 alpha (E2alpha), showed a redistribution into polar clusters of Con A-binding sites that were dispersed in random patches at the external surfaces of control cells. These hormore-induced membrane alterations were abolished by prior treatment of cells with inhibitors of thiol proteinase activity of the cathepsin B1 (CB1) type, such as leupeptin and iodoacetate. Leupeptin at 4.5 X 10(-7) M also reduced the affinity of [3H]E2beta binding to intact cells but did not influence specific binding of the hormone to macromolecular components of cytosol. A pronounced increase in the availability of endogenous CB1, But not of alkaline phosphatase, succinate, or lactate dehydrogenase, in the extracellular media was elicited within 30 min after E2beta treatment. In cells cultured in chemically defined medium for up to 48 h, E2beta, but not E2alpha, enhanced cell proliferation and stimulated [3H]thymidine incorporation into macromolecular form. These E2beta-induced effects were abolished by prior treatment of cells with liposome-entrapped leupeptin at a final concentration of 7 X 10(-8) M. The net rate of intercellular adhesion among endometrial cells was also enhanced by E2beta. This hormonal response was diminished by prior exposure to leupeptin. Fractionation of cells by selection for adhesiveness due to E2beta exposure for 30 min yielded a subpopulation of rapidly dividing cells which surpassed their less adhesive counterparts in cathepsin secretion and in Con A-mediated hemadsorption. These results indicate that leupeptin-sensitive proteinase activity may contribute to membrane and growth modifications elicited by E2beta treatment in endometrial cells.
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PMID:Estrogen-induced membrane alterations and growth associated with proteinase activity in endometrial cells. 45 77

The measurement of acid and alkaline phosphatase and cathepsin activities in bronchial aspirates obtained through bronchoscopy from a series of 75 patients suggests a procedure that may have value as a routine diagnostic examination. Using this approach, seven patients with neoplasms in the lung showed elevated levels of alkaline phosphatase and cathepsin in bronchial aspirates without elevation in acid phosphatase activity.
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PMID:A preliminary study of elevated alkaline phosphatase and cathepsin in bronchial aspirates of patients with lung cancer and bronchitis. 115 37

In a study of 4-hr hemorrhagic hypotension in dogs, the plasma levels of the lysosomal enzymes, cathepsin (CATH) and acid phosphatase (AP) showed early and progressive increases in activity. The plasma levels of the intestinal fraction of alkaline phosphatase (IAkP) and aspartate aminotransferase (AAT) were increased after 2 hr of hypotension and the liver specific enzyme, ornithine carbamyltransferase (OCT), and creatine phosphokinase (CPK), after 3 hr. All of the enzymes showed large increases after 4 hr of hypotension. The plasma levels of CATH showed the earliest and largest relative increase indicating that with the shock model used, this enzyme was the most sensitive indicator of shock severity. The increase in plasma enzyme levels was probably the result of tissue damage in the splanchnic region but the elevation of plasma CPK, a muscle specific enzyme, indicates some muscle cell damage as well. While the increase in the plasma enzyme activity is probably due, in large part, to cellular damage, it is likely that a decreased enzyme removal rate--resulting from a hypofunctional RES--also contributes to the elevated plasma enzyme levels during hemorrhagic hypotension.
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PMID:Changes in plasma levels of lysosomal and non lysosomal enzymes during hemorrhagic hypotension. 116 70

Acid phosphatase, alkaline phosphatase and acid cathepsin activity increased in the subcellular fraction of the grey matter of dog brain in proportion to the duration of compression ischemia, particularly in the postmitochondrial supernatant. An increase in the alkaline phosphatase and of the acid cathepsin activity in the postmitochondrial supernatant was also observed at the period of clinical death caused by blood loss and preceded by hypotension of different duration and various levels of arterial pressure. Comparison of the above data indicated a common mechanism of proteolysis activation in the nervous tissue in the terminal states under study.
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PMID:[Change in phosphatase and acid cathepsin activity in the dog cerebral cortex in terminal states]. 122 90

Dietary hexachlorocyclohexane (HCH) and gamma-isomer of HCH produced significant increase in liver weights of mice. Elevated levels of alanine and aspartate aminotransferases and of alkaline phosphatase in the blood of these animals suggested hepatotoxicity. Hepatic soluble enzymes--aspartate aminotransferase and lactate dehydrogenase--were markedly lowered. Among the hepatic lysosomal enzymes, acid phosphatase and acid cathepsin were increased in the experimental animals. Hepatic glucose-6-phosphatase was lowered by HCH while aldolase activity was increased. Hydrolytic enzymes in small intestine, viz., disaccharidases, lipase, amylase, dipeptidase and phosphatases, were also affected by dietary HCH and gamma-HCH. The results suggested cellular toxicity in hepatocytes of HCH and gamma-HCH fed animals, and also interference in gastrointestinal absorption.
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PMID:Biochemical toxicity of hexachlorocyclohexane and its gamma-isomer in albino mice. 248 47

1. Homogenates of guinea-pig polymorphonuclear leucocytes were separated by differential centrifugation into six particulate fractions and a soluble fraction. 2. The distributions in these fractions of protein, DNA, succinate dehydrogenase, beta-glucuronidase, peroxidase, alkaline phosphatase, acid phosphatase (against p-nitrophenyl phosphate and beta-glycerophosphate), cathepsin, and catalase were compared. 3. Almost all of the DNA sedimented in the first two pellets, indicating that the nuclei were relatively intact. 4. The four hydrolases and peroxidase showed different distribution patterns, although these activities were previously reported to be localized mainly in the single ;granule' fraction isolated from leucocytes. 5. The particles containing peroxidase, acid phosphatase and alkaline phosphatase all exhibited latency. Maximum activity for each enzyme was obtained at roughly similar concentrations of Triton X-100. 6. The acid phosphatase of these cells was distributed between two populations of particles that differed in both sedimentation characteristics and density. The acid phosphatase(s) of the two populations showed slightly different substrate specificities. This bimodal distribution was not an artifact of the procedure used to elicit the cells. 7. Catalase was recovered almost entirely in the soluble fraction and showed no latency in freshly prepared homogenates. No urate oxidase was detected. 8. We conclude that the ;granule' fraction of the polymorphonuclear leucocyte, as isolated by previous workers, contains at least three, probably more, populations of particles with different enzyme contents, and that these cells probably do not contain peroxisomes.
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PMID:The distributions of some granule-associated enzymes in guinea-pig polymorphonuclear leucocytes. 541 96

It is believed that the degree of periodontal tissue breakdown and tooth loss increase with age. In periodontal tissues which are gingiva, periodontal ligament (PL), alveolar bone and tooth cementum, the PL which is soft connective tissue, lies between the tooth cementum and alveolar bone, having the primary function of tooth support, and maintaining the homeostasis of supporting tissues, as well as providing the healing process. We therefore investigated the effects of in vitro cellular aging on alkaline phosphatase (ALP), cathepsin activities and collagen secretion from human PL cells obtained from 18-23 year-old patients' teeth. ALP, cathepsin activities and collagen secretion may play important roles in the remodeling and maintaining of periodontal tissues. To investigate the life span of PL cells, the cells were sequentially subcultivated. The maximum population doubling level of the PL cells in the present experiment was 22-25 passages. Investigating some important biological activities of the PL cells at different passage levels (6-7, 30% of life span to 17-20, 75% of life span), ALP activity and collagen secretion were found to have significantly decreased while cathepsin B and L activities significantly increased with cellular aging. Since these biological activities in human PL cells tend to be more catabolic with increase in cellular aging, the increase in periodontal breakdown with age may be partly related to the catabolic changes of the PL cells themselves.
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PMID:Effects of in vitro cellular aging on alkaline phosphatase, cathepsin activities and collagen secretion of human periodontal ligament derived cells. 905 41

A method has been described for isolation of the specific cytoplasmic granules of rabbit polymorphonuclear leucocytes. Homogeneous suspensions of leucocytes were disrupted by lysis in 0.34 M sucrose. This procedure liberated the cytoplasmic contents of the cell and dissolved a considerable proportion of the nuclei. Following disruption, the sucrose lysate was separated into three fractions by differential centrifugation, i.e. 400 g or nuclear pellet, 8,200 g or granule pellet and the postgranule supernate. Microscopic examination revealed that the 8,200 g pellet was composed of intact granules as well as occasional mitochondria. The other two fractions were morphologically heterogeneous. Studies with isolated granules demonstrated their lysis by a variety of weak acids and surface-active agents. When buffered solutions were employed between the ranges of pH 2.0 and 9.0, granule lysis began at pH 5.5 and was complete at pH 4.0. Chemical analysis disclosed that the granule pellet contained protein and phospholipid with only traces of nucleic acids. Approximately 70 to 80 per cent of the total cellular antimicrobial agent phagocytin was present in the granule fraction. This material was liberated from the granules by acid (pH 5.0 or lower). Studies on selected enzymes showed that acid phosphatase, alkaline phosphatase, nucleotidase, ribonuclease, deoxyribonuclease, and beta glucuronidase were predominantly localized in the granule fraction. Approximately 50 per cent of total cellular lysozyme and cathepsin were also present in the 8,200 g pellet. Disruption of the granules was associated with the release of the majority of granule protein and enzymes in a non-sedimentable form. The properties and composition of rabbit polymorphonuclear leucocyte granules seem to be analogous to those of liver lysosomes.
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PMID:The isolation and properties of the specific cytoplasmic granules of rabbit polymorphonuclear leucocytes. 1369 90

Increased expression of several osteoblastic proteases and MEPE (a bone matrix protein) occurs in X-linked hypophosphatemic rickets (hyp). This is associated with an increased release of a protease-resistant MEPE peptide (ASARM peptide), a potent inhibitor of mineralization. Cathepsin B cleaves MEPE releasing ASARM peptide and hyp osteoblast/osteocyte cells hypersecrete cathepsin D, an activator of cathepsin B. Our aims were to determine whether cathepsin inhibitors correct the mineralization defect in vivo and whether hyp-bone ASARM peptide levels are reduced after protease treatment. Normal littermates and hyp mice (n = 6) were injected intraperitoneally once a day for 4 weeks with pepstatin, CAO74 or vehicle. Animals were then sacrificed and bones plus serum removed for comprehensive analysis. All hyp mice groups (treated and untreated) remained hypophosphatemic with serum 1,25 vitamin D3 inappropriately normal. Serum PTH was significantly elevated in all hyp mice groups relative to normal mice (P = 0.0017). Untreated hyp mice had six-fold elevated levels of serum alkaline-phosphatase and two-fold elevated levels of ASARM peptides relative to normal mice (P < 0.001). In contrast, serum alkaline phosphatase and serum ASARM peptides were significantly reduced (normalized) in hyp mice treated with CA074 or pepstatin. Serum FGF23 levels remained high in all hyp animal groups (P < 0.0001). Hyp mice treated with protease inhibitors showed dramatic reductions in unmineralized osteoid (femurs) compared to control hyp mice (Goldner staining). Also, hyp animals treated with protease inhibitors showed marked and significant improvements in growth plate width (42%), osteoid thickness (40%) and cortical area (40%) (P < 0.002). The mineralization apposition rate, bone formation rate and mineralization surface were normalized by protease-treatment. High-resolution pQCT mineral histomorphometry measurements and uCT also confirmed a marked mineralization improvement. Finally, the growth plate and cortical bone of hyp femurs contained a massive accumulation of osteoblast-derived ASARM peptide(s) that was reduced in hyp animals treated with CA074 or pepstatin. This study confirms in vivo administration of cathepsin inhibitors improves bone mineralization in hyp mice. This may be due to a protease inhibitor mediated decrease in proteolytic degradation of the extracellular matrix and a reduced release of ASARM peptides (potent mineralization inhibitors).
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PMID:Correction of the mineralization defect in hyp mice treated with protease inhibitors CA074 and pepstatin. 1676 7


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