Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Subcutaneous implantation of demineralized bone matrix (DBM) from rat initiates a sequence of developmental events that results in endochondral bone formation. This investigation examined the modification of the osteoinductive potential of DBM during the initial stages of this developmental cascade. Diffusion chambers (DC), constructed with filters of known pore size, permitting or excluding cells from entering the chambers, and containing DBM were subcutaneously implanted into Long-Evans male rats for specific time periods (1-7 days). DC were recovered and the osteoinductive potential of the matrix from these chambers was then tested by subcutaneous implantation and assaying the resulting day 11 plaque tissue enzymatically for alkaline phosphatase activity, and histologically for evidence of chondrogenesis and osteogenesis. The possible modification of DBM by local systemic factors (enzymatic degradation) or contact by polymorphonuclear leukocytes (PMNs) was also investigated. We have concluded from this study that the osteoinductive potential of DBM has a half-life of 5-7 days following implantation and although the enzymes collagenase, elastase, and trypsin abolished this activity, pepsin significantly enhanced it. Culture of PMNs with matrix prior to its implantation appeared to have little effect. Furthermore, during the initial stages of matrix-induced endochondral bone formation, DBM serves as both the instructive inducer and permissive substratum required in this process.
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PMID:In vivo analysis of the half-life of the osteoinductive potential of demineralized bone matrix using diffusion chambers. 250 25

The author examined a group of 143 patients with osteomalacia of different origin before treatment and after adequate treatment with vitamin D, using laboratory tests, assessment of body weight and muscular strength (grip of the dominant hand). After treatment there was a significant rise of calcaemia, phosphataemia and calciuria and a drop of alkaline phosphatase activity. The body weight increased within the first month of treatment on average by 1.27 kg, during the second month by another 1.15 kg. The patients gained a total of 2.42 kg. The muscular strength increased during the first month on average by 3.23 kg and during the second month by another 2.16 kg, i.e. a total of 5.39 kg. From these results it may be concluded that vitamin D may have a certain anabolic effect if used in pharmacological does either due to an increased nutrient absorption from the gut because of hypertrophy of the intestinal wall or indirectly via hypercalcaemia which increases the hydrochloric acid secretion in the stomach as well as pepsin secretion, and promotes activation of trypsin and lipase in the duodenum and moreover causes retardation of the intestinal transit. The increased muscular strength in due to a rise of calcaemia, improved muscle contraction and probably also due to the mentioned nutritional factors. There may be also the factor of an improved lifestyle due to the immunomodulating action of vitamin D and disappearance of bone pain.
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PMID:[Anabolic effects of vitamin D in patients with osteomalacia]. 263 59

The vascular extracellular matrix (ECM) plays an important role in the histopathology of cerebral microcirculation, but its characterization is still incomplete. For that reason we investigated paraffin-embedded and cryostat sections of intracerebral and meningeal vessels from eight normotensive and six hypertensive humans using monospecific affinity-purified polyclonal antibodies against human/monkey amino-terminal procollagen I + III peptide (P I P, P III P), collagen IV (7-S and NC1 domains), VI, and laminin (P 1 fragment) by applying peroxidase-antiperoxidase- and alkaline phosphatase-antialkaline phosphatase techniques. In normotensives, laminin and collagen IV were codistributed in the basal lamina of meningeal and intraparenchymal vessels. Collagen VI was only present in the adventitia of meningeal vessels and larger intraparenchymal arteries and veins, whereas it was absent from cortical vessels including capillaries. Intensive staining for collagen VI was observed in the choroid plexus, the superficial glia and sheath of cranial nerves. In hypertensives, the basement membrane constituents laminin and collagen IV appeared ubiquitously increased. Here, collagen VI was also deposited in the broadened vascular intima and media of larger arteries and in cortical vessels. In both groups collagen VI and P III P appeared to be codistributed. Our results indicate that significant qualitative change sin ECM of cerebral blood vessels are taking place during the development of hypertension, such as (1) an atypical deposition or an increase of collagen VI which by interconnecting collagen fibrils (I and III) might exert a stabilizing (sclerosing) function in the ECM, and (2) a thickening of vascular basement membranes caused by an accumulation of its major components laminin and collagen IV.
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PMID:Altered expression of collagen type VI in brain vessels of patients with chronic hypertension. A comparison with the distribution of collagen IV and procollagen III. 323 76

Proteins of the isolated brush border membrane of Hymenolepis diminuta were hydrolyzed in vitro by chymotrypsin, papain, pepsin, subtilopeptidase A (= subtilisin Carlsberg), and trypsin. Neither proteolytic nor amidase activity was demonstrable in the isolated membrane using proteinaceous (casein and hemoglobin) or chromogenic (benzoyl-arginine-p-nitroanilide and succinyl-alanyl-alanyl-propyl-phenylalanine p-nitroanilide) substrates, and the membrane preparation did not inhibit the proteolytic and amidase activities of these enzymes. Thus, the isolated tegumental membrane of H. diminuta is not inherently resistant to the action of proteolytic enzymes, and it does not inhibit proteolytic activity. In control incubations containing only buffer, the alkaline phosphatase activity of the brush border membrane decreased in a time dependent manner, but in the presence of chymotrypsin, subtilopeptidase A, and trypsin, the membrane retained greater alkaline phosphatase activity (pepsin and papain could not be tested for this effect on alkaline phosphatase activity). A similar time dependent decrease in activity was also noted for each of the proteolytic enzymes in control assays, but subtilopeptidase A and papain retained greater activity in the presence of the isolated membrane preparation when these assays were compared to controls.
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PMID:Hymenolepis diminuta: interactions of the isolated brush border membrane with proteolytic enzymes. 330 86

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli is described. Rabbit anti-human chorionic gonadotropin serum (0.2 ml) was digested with pepsin to convert IgG to F(ab')2 and applied to a column of human chorionic gonadotropin-Sepharose 4B, followed by elution at pH 2.5. The affinity-purified anti-human chorionic gonadotropin F(ab')2 was mixed with non-specific goat F(ab')2 (0.5 mg) as a carrier, reduced with 2-mercaptoethylamine to split F(ab')2 to Fab' and conjugated to beta-D-galactosidase using N,N'-o-phenylenedimaleimide. The affinity-purified rabbit anti-human chorionic gonadotropin Fab'-beta-D-galactosidase conjugate was separated from non-specific goat Fab'-beta-D-galactosidase conjugate and unconjugated beta-D-galactosidase by affinity chromatography on a column of goat (anti-rabbit IgG) IgG-Sepharose 4B using 4 M urea. The amount of the affinity-purified conjugate obtained was 56-69 micrograms. The detection limit of human chorionic gonadotropin by a sandwich enzyme immunoassay technique was improved 30-fold by using the affinity-purified conjugate as compared with that before affinity-purification. This method is applicable to the conjugation with alkaline phosphatase from calf intestine and probably also other enzymes which are stable in 4 M urea.
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PMID:A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. 391 Jun 49

Cultured heart muscle cells, but not HeLa cells, oxidize long-chain fatty acids in medium containing dialyzed serum. Addition of chicken serum dialysate (or non-dialized serum) stimulated palmitic acid oxidation by HeLa cells 10 to 20 fold. This serum activity was not eliminated by lipid extraction, ethanol or acid precipitation, alkaline phosphatase treatment, or autoclaving. About 80% was lost after any one of the following treatments: 6N HCl at 110 degrees C for 16 hr, pepsin, Dowex cation exchange at pH 3, or 1N KOH at 100 degrees C for 1 hr. Serum activity was separated into five or more peaks by gel filtration with Sephadex G-10. Each of these peak fractions was further purified by HPLC using a cyanopropyl-bonded resin. Carnitine, which is important for the transport of long-chain fatty acids into mitochondria for oxidation, also stimulated the oxidation of palmitate. However, these serum factors are not known precursors to carnitine since its immediate precursor 4-n-trimethylaminobutyrate, did not stimulate palmitate oxidation. Total carnitine, including that in acylcarnitine compounds, was approximately 15 microM in the chicken sera to give approximately 0.7 microM in the medium. Based on the fraction of total activity accountable by carnitine and fractional stability to acid, alkali, and pepsin, about 75% of the activity is from non-carnitine compounds. Only one of the factors appears to be carnitine or an acylcarnitine derivative. Several lines of evidence suggest that the other factors are peptide compounds.
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PMID:Serum factors that stimulate fatty acid oxidation: properties of factors. 394 93

The distribution and activities of phosphatases and oxidative enzymes have been determined with the help of histochemical methods in the kidney of the Prussian Carp, a stenohaline freshwater-fish. In addition to fish maintained in freshwater aquaria, a group of the animals used has been adapted to seawater of moderate salinity. The following pattern of enzyme reaction intensities has been observed in the various kidney structures: Strong reactions of alkaline phosphatase in the nephron are confined to the glomerular capillary convolute and the brush border of proximal segments. Equally enzyme activities are observed in the connective tissue sheath of the collecting duct -- archinephric duct system. Acid phosphatase can be detected in all segments of the nephronic tubule, strong activities are found in the proximal segment (P I), in the epithelium of the archinephric duct, and, especially, in the interstitial tissue. ATPase reacts strongly positive in epithelial cells of the distal tubule and the collecting duct -- archinephric duct system. ATPase reactions are inhibited by Ouabain, and therefore can be regarded as reactions of Na--K-ATPase. Mitochondrially bound oxidative enzymes, connected with the citric acid cycle and the respiratory chain, show very strong reaction intensities in the distal tubule and the collecting duct- archinephric duct system, while the glomeruli generally exhibit negative reactions. Lactate -- and malate dehydrogenases are found to react weakly to negatively throughout the whole kidney. Maintenance in seawater does not deeply affect the enzyme pattern of the kidney of the Prussian carp, with exception of some oxidative enzymes, reacting weaker in the distal tubule and the collecting duct-archinephric duct system. In addition, the epithelial cells of the archinephric duct of seawater adapted fish show a marked apical localization of reaction products for these enzymes. Possible relations between enzyme histochemistry and fish kidney physiology are discussed, in connection with comparative aspects of the enzyme histochemistry of the vertebrate kidney. A short review of normal histology and function of the kidney of the Prussian carp is added.
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PMID:[Phosphatases and oxidative enzymes in the kidney of the Prussian carp (Carassius auratus gibelio Bloch) adapted to salt water]. 625 47

A method is presented for isolating osteoblasts from newborn mouse calvaria without the use of digestive enzymes. The procedure is based on the ability of osteoblasts to migrate from bone onto small glass fragments (Jones, S.J., and A. Boyde, 1977, Cell Tissue Res., 184:179-193). The isolated cells were cultured for up to 14 d in Dulbecco's modified Eagle's medium supplemented with 10% fetal calf serum and 50 micrograms/ml of ascorbic acid. 7-d cultures were incubated for 24 h with [3H]proline. High levels of collagen synthesis relative to total protein were found, as measured by collagenase digestion of medium and cell layer proteins. Analysis of pepsin-digested proteins from the same cultures by SDS PAGE showed that type I collagen was predominantly produced with small amounts of type III and V (alpha 1 chains) collagens. Osteoblasts grown in the presence of beta-glycerophosphate were able to initiate mineral deposition in culture. Electron microscopic analysis of the cultures revealed the presence of needle-shaped apatite-like crystals associated with collagen fibrils and vesicles in the extracellular space. Mouse skin fibroblasts cultured under identical conditions failed to initiate mineralization. Electron histochemical studies revealed the presence of alkaline phosphatase activity, associated with osteoblast membranes, matrix vesicles and on or near collagen fibrils. Thus these isolated osteoblasts retained in culture their unique property of initiating mineralization and therefore represent a model of value for studying the mineralization process in vitro.
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PMID:Osteoblasts isolated from mouse calvaria initiate matrix mineralization in culture. 683 75

The growth of group A human, bovine, equine and porcine rotaviruses were enhanced by pretreatment of virus with pancreatin, trypsin, protease, alkaline phosphatase or pepsin and incorporation of these enzymes in maintenance medium. In contrast, alpha-amylase or lipase inhibited the growth of equine and porcine rotaviruses. The other enzymes, adenosine deaminase, lactase, lysozyme, ribonuclease or triose-phosphate isomerase gave little or no change in the growth of all four rotaviruses.
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PMID:Effect of enzymes on the growth of human and animal rotaviruses. 754 24

We developed a non-radioactive method of ligand western blotting for specific detection of active forms of serine proteases. The method consists of three steps: (i) separation of proteins by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel, followed by blotting of proteins to nitrocellulose membrane; (ii) binding of a specific ligand, such as soybean trypsin inhibitor labeled with biotin, to protease on the membrane; and (iii) detection of the protease-inhibitor complex by color reaction (or chemiluminescence) developed by streptavidin-conjugated peroxidase (or alkaline phosphatase). By using this method, plasmin and trypsin (serine proteases) were detected, but papain (thiol protease) or pepsin (acidic protease) was not. Plasmin was detectable up to less than 4 ng. Inactive precursors of serine protease, i.e. plasminogen and trypsinogen, did not exhibit visible bands until they were activated by treatment with streptokinase or trypsin, respectively. We applied this method to clinical samples, and succeeded in detecting plasminogen, after conversion to plasmin with streptokinase treatment, in as little as 5 microliters of serum or trypsin, as it was in 10 microliters of pancreatic juice.
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PMID:Ligand western blotting for specific detection of active forms of proteases. 766 77


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