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 activities of eight enzymes (glutamate dehydrogenase, sorbital dehydrogenase, malate dehydrogenase, lactate dehydrogenase, alpha-hydroxy butyrate dehydrogenase, gamma-glutamyl transpeptidase, alkaline phosphatase and creatine kinase) were determined in tissue homogenates of liver, kidney, spleen, lung, small intestine, cardiac muscle and skeletal muscle, from 15 Large White pigs of three different ages (1.5 weeks, 18--22 weeks and 113 weeks). The results showed that variation in tissue enzyme concentration due to differences in sex is minimal. Variation due to differences in age, however, appears to be of greater importance, particularly when considering young animals. These age differences may affect the interpretation of plasma enzyme changes due to tissue damage, and the use of additional enzyme assays as an aid to interpretation in these cases is advisable.
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PMID:Enzyme activities in tissues of clinically normal Large White pigs. Variations with age and sex. 60 99

Trans-1,2-dichloroethylene (t-DCE), an industrial solvent, proved to be moderately toxic when studied in small laboratory animals. In adult female rats brief (8 h) and prolonged (8 h daily, on 5 consecutive days a week, for more than 16 weeks) inhalation of 200 ppm--the current TLV/MAC in various countries--produced histological evidence of slight to severe fatty degeneration of the liver lobules and Kupffer cells. In addition marked pulmonary hyperaemia and alveolar septal distention were noted. Fibrous swelling of the cardiac muscle (with striation) just barely maintained) and hyperaemia remained detectable for as long as 14 h post-exposure, but only occurred at 3000 ppm/8 h. A concentration of 1000 ppm/8 h was required to produce a fall in blood albumin, urea nitrogen, alkaline phosphatase activities and erythrocyte count. The cited concentrations failed to produce prenarcotic symptoms of narcosis (central nervous system (CNS) depression). The LD50 was found to be 6.0 ml/kg i.p. and 1.0 ml/kg p.o. for female rats, and 3.2 ml/kg i;p. for female mice. In some of the rats killed in these experiments the organ changes were found to be identical to those observed after inhalation.
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PMID:Toxicity studies on trans-1,2-dichloroethylene. 85 30

We have raised monoclonal antibodies (Mab) to the Mr 55,000 desmin polypeptide, electrophoretically purified from cytoskeletal preparations of isolated bovine heart Purkinje fibers. One of the Mabs, 39AB6, revealed desmin only in cow Purkinje fibers and did not react with desmins from other muscle cells, including ventricular cardiac muscle, striated muscle and smooth muscle, as revealed by both immunoblotting and immunocytochemistry. Desphosphorylation of electrophoretically separated polypeptides on nitrocellulose with alkaline phosphatase did not affect the binding of the Mab. The present results show that there are cell-type specific antigenic determinants in intermediate proteins of the desmin type.
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PMID:Monoclonal antibody to desmin purified from cow Purkinje fibers reveals a cell-type specific determinant. 169 90

The local and systemic pathological changes induced by an i.m. injection of 100 micrograms of Bothrops asper venom in mice were studied histologically and by following the changes in serum levels of enzymes, proteins, ATP and lactate, as well as alterations in hematocrit and clotting time. B. asper venom induced a rapid and marked increase in serum levels of creatine kinase, aspartate aminotransferase and lactate dehydrogenase, but not alanine aminotransferase or alkaline phosphatase. A local myonecrosis and hemorrhage was observed, with the lungs collapsing by 24 hr and the kidneys showing glomerular congestion and vacuolar degeneration of tubular cells. Only minor histopathological changes were observed in cardiac muscle and liver. Both ATP and lactate blood levels decreased after venom injection, whereas there were no changes in serum protein concentration. Blood incoagulability was observed 1 and 3 hr after envenomation. Antivenom neutralized venom-induced increases in serum enzyme levels following preincubation with venom, indicating that antivenom contains antibodies against tissue-damaging toxins. However, when antivenom was administered i.v. at different time intervals after venom injection, neutralization was only partial, with the exception of defibrinating activity, which was totally neutralized even after a delay of 1 hr in administering antivenom.
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PMID:Histopathological and biochemical alterations induced by intramuscular injection of Bothrops asper (terciopelo) venom in mice. 281 6

A cytosolic phosphoprotein phosphatase of Mr = 95,000 purified from bovine cardiac muscle, which contains a catalytic subunit of Mr = 35,000, is known to be associated with a Mg2+-activated p-nitrophenyl phosphatase activity. We have found that the enzyme preparation is also active toward phosphotyrosyl-IgG and -casein phosphorylated by pp60v-src, the transforming gene product of Rous sarcoma virus. The properties of this phosphotyrosyl protein phosphatase activity closely resemble those of the p-nitrophenyl phosphatase activity but sharply differ from those of the phosphorylase phosphatase activity. Comparative studies of the activities of the Mr = 95,000 phosphatase, bovine kidney alkaline phosphatase, and ATP X Mg-dependent phosphatase toward phosphoseryl, phosphothreonyl, and phosphotyrosyl proteins and p-nitrophenyl phosphate under various conditions have been carried out. The results indicate that the Mr = 95,000 enzyme exhibits higher activity toward phosphoseryl and phosphothreonyl proteins than toward phosphotyrosyl proteins, while the kidney alkaline phosphatase preferentially dephosphorylates phosphotyrosyl proteins. ATP X Mg-dependent phosphatase is inactive toward phosphotyrosyl proteins.
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PMID:Characterization of a phosphotyrosyl protein phosphatase activity associated with a phosphoseryl protein phosphatase of Mr = 95,000 from bovine heart. 630 59

Cell fractions enriched in cardiac muscle cells (myocytes), on the one hand, and in non-myocytes, on the other, were prepared by dissociation of rat ventricular tissue with collagenase. Amine oxidase activities in homogenates of these cell fractions and also in homogenates of the corresponding undissociated ventricular tissue were compared. In addition, the activity of alkaline phosphatase (AP), an enzyme found predominantly associated in the heart with non-myocytes, particularly capillary endothelial cells, was also measured. No significant difference in the activity of MAO-A (assayed with 1 mM 5-hydroxytryptamine) was found between myocyte and non-myocyte fractions. In contrast, the activities of alkaline phosphatase (AP) and also the semicarbazide-sensitive amine oxidase (SSAO), assayed with 1 microM benzylamine (BZ), were both significantly higher in non-myocytes, by several-fold, than in myocyte fractions. Studies of the inhibition by clorgyline of 1 mM BZ metabolism confirmed that both MAO-A and MAO-B can also contribute to BZ oxidation in the rat heart. These experiments indicated different ratios of MAO-A: MAO-B in the various cell fractions. The ratios of the percentage contributions of MAO-A and MAO-B, respectively, to the total metabolism of 1 mM BZ were 78:20 (myocytes), 43:52 (non-myocytes) and 57:32 (undissociated tissue). These results suggest that MAO-B, in addition to AP and SSAO, may be associated preferentially with non-myocyte constituents of the rat heart. Although cardiac myocytes appear to contain predominantly MAO-A, this enzyme form is also localized, with high activity, to the non-myocyte fraction. However, since the non-myocyte fraction is heterogeneous in its cell content, containing vascular components of the coronary microcirculation, as well as other cells of connective tissue origin, the exact cellular localization of the enzyme activities within this fraction has not yet been defined.
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PMID:Monoamine oxidase activities of dissociated cell fractions from rat ventricular muscle. 646 72

Biotin carboxylases in mammalian cells are regulatory enzymes in lipogenesis and gluconeogenesis. In this study, endogenous biotin in skeletal and cardiac muscle was detected using avidin conjugated with alkaline phosphatase and applied in high concentrations to muscle sections. The avidin binding was subsequently visualized by histochemical demonstration of the alkaline phosphatase activity. All cardiac muscle cells showed high affinity for avidin with only the nuclei and the intercalated discs remaining unstained. In skeletal muscle a diffuse reaction could be detected in the sarcoplasm of the muscle fibres. A granular reaction was noted in the same fibres that showed activity for succinic dehydrogenase. The specificity of the coloured reaction product in the muscle sections was investigated and is suggested to be caused by avidin binding to biotin moieties in mitochondria and the cytosol. Mitochondrial and cytosolic preparations of skeletal muscle were electrophoresed in sodium dodecyl sulphate gels. After blotting and incubation with conjugated avidin, two bands with molecular weights of 75 kDa and 130 kDa respectively were evident in the mitochondrial preparation. It is suggested that the 75-kDa band represents comigration of the biotin-containing subunits of propionyl-CoA carboxylase and methylcrotonyl-CoA carboxylase. The 130-kDa band may represent the biotin-containing pyruvate carboxylase. In the cytosolic preparation a 270-kDa band was stained in blots that had been incubated with conjugated avidin; this band is suggested to represent acetyl-CoA carboxylase. A 190-kDa cytosolic band might be a cleavage product of acetyl-CoA carboxylase. We propose that using alkaline phosphatase-conjugated avidin it is possible to detect the mitochondrial and cytosolic biotin-dependent carboxylases in striated muscle.
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PMID:Biotin carboxylases in mitochondria and the cytosol from skeletal and cardiac muscle as detected by avidin binding. 816 85

A wide range of pharmacological actions has been attributed to the anthracyclins. In this study we examined their effect on serum lipids in experimental animals in parallel with histological alterations. Three Wistar rat groups were injected with doxorubicin, epirubicin or normal saline once a week for 12 weeks. Total serum lipids, cholesterol, triglycerides, HDL-cholesterol, transaminases, proteins and alkaline phosphatase were assayed weekly. A proportion of the animals were sacrificed at the same time points and the cardiac muscle, large vessels, liver and abdominal muscle were stained and examined under light microscopy. Serum lipids were found to increase gradually, starting after 8 weeks of drug administration, until the end of the experiment. Tissue damage was noted in the cardiac muscle, abdominal muscle and large vessels, also following an increasing trend. Doxorubicin had a more pronounced effect than epirubicin on both serum lipid increase and tissue destruction. These alterations may contribute to anthracyclin-related cardiac damage.
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PMID:An increase of serum lipids after cumulative doses of doxorubicin and epirubicin in experimental animals. 904 2

It has recently been shown that several members of the tetraspan superfamily, including CD9 and CD63, associate with each other and with beta1 integrins. In this study, we examined the distribution of a recently identified tetraspan, PETA-3 (CD151), and of CD9, CD63, alpha5beta1, and the integrin beta1 chain in normal human tissues by the indirect immunoperoxidase and alkaline phosphatase-anti-alkaline phosphatase techniques. PETA-3 showed a broad distribution and was expressed by endothelium, epithelium, Schwann cells, and dendritic cells and by skeletal, smooth, and cardiac muscle. Expression in skin was mostly restricted to the basal cells of the epidermis and was downregulated on differentiation. In the small intestine, PETA-3 was expressed by crypt and villous enterocytes with a mostly basolateral distribution, but was not detectable on the brush border. CD9 was expressed on the plasma membrane of enterocytes in crypts and at the bases of the villi whereas CD63 demonstrated a unique granular appearance concentrated in the apical cytoplasm below the brush border. The findings of this study show co-localization of PETA-3 with CD9, CD63, alpha5beta1, and beta1 in particular tissues, demonstrating that tetraspan/integrin complexes may occur. However, the lack of co-localization of these antigens in other tissues also implies distinct roles for these molecules.
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PMID:Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. 911 Dec 30

Effect of fenvalerate on cell architecture, tissue biochemical parameters and its residual concentration was studied in broiler chicks following dermal application at 0.1 and 1% in ethanol once daily for 31 days. It did neither produce loss of body weight nor clinical signs of toxicity. Kidney contained maximal residue followed by heart, fat, liver and brain after 0.1%; and fat contained maximal residue followed by kidney, heart, liver and brain after 1% application. Fenvalerate (0.1%) increased the aspartate aminotransferase (AST) (except brain), alanine aminotransferase (ALT), alkaline phosphatase (AP), acid phosphatase (AcP) (only brain) activities, glycogen level (only liver) in liver, kidney, heart and brain tissues; and 1% increased the AST (except brain), ALT, AcP (except liver and kidney), AP (only heart), glycogen (only liver) and decreased AP (except heart), AcP (only kidney), cholesterol (except liver and heart), and acetylcholinesterase (AChE) (liver and brain) of liver, kidney, heart and brain tissue homogenates respectively. Histopathological examination in general showed aggregation of mononuclear cells in liver, around the kidney tubules and cardiac muscle fibre. In addition, fibrosis in the periportal area of liver, proliferation of ureter and tubular degeneration, and congestion of endocardial vessels were also observed. The intensity of cellular changes was more marked after 1% dermal application.
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PMID:Effect of short-term dermal toxicity of fenvalerate on residue, cell architecture and biochemical profiles in broiler chicks. 931 26


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