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At least 1,441 records · Page 80Linked to original sources
PubMed1989

Metabolic effects of salmon glucagon and glucagon-like peptide in coho and chinook salmon.

Different doses of glucagon and glucagon-like peptide (GLP) isolated from coho salmon, Oncorhynchus kisutch were tested in vivo and in vitro on juvenile coho and chinook (O. tshawytscha) salmon. Results obtained suggest an involvement of these peptides in the regulation of plasma glucose, plasma fatty acids, liver glycogen, and the hepatic enzymes: glycogen phosphorylase, pyruvate kinase, triacylglycerol lipase, and glucose-6-phosphate dehydrogenase. Metabolic effects were more enhanced in summer than either in spring or in autumn. GLP was less effective than glucagon in stimulating glycogenolysis in vivo. Salmon glucagon, especially in low concentrations, was generally more potent metabolically than mammalian (porcine/bovine) glucagon. The interaction between glucagon-family peptides and insulin seems to be different from the one described in mammals: glucagon and GLP either lowered plasma circulating levels of insulin or showed no effect. Only at the time of parr-smolt transformation did GLP slightly elevate plasma insulin levels in coho salmon.

Animals↗
PubMed1984

Activity of enzymes related to carbohydrate metabolism in the HT 29 colon adenocarcinoma cell line and tumor.

Activity of several enzymes of the glycogen and carbohydrate metabolism is studied in HT 29 colon adenocarcinoma cell line and in HT 29 tumors developed in nude mice, by reference to the normal human colon mucosa. Activity of glycogen synthase, glycogen phosphorylase, pyruvate kinase, fructose-1,6-diphosphatase, glucose-6-phosphate dehydrogenase and lactate dehydrogenase is found to be increased in both the cultured cells and the tumors. It indicates that the biochemical strategy of malignant cells, due to the neoplastic transformation process, involves specific changes in the carbohydrate metabolism of tumor as well as in vitro growing correspondent cell line.

Adenocarcinoma↗
PubMed1993

Analysis of purine metabolic enzymes in human CD4 Leu 8- and CD4 Leu 8+ lymphocyte subpopulations.

1. Specific activities of adenosine deaminase, purine nucleoside phosphorylase, adenosine kinase, 5'-nucleotidase, S-adenosyl-L-homocysteine hydrolase, AMP deaminase, adenine phosphoribosyl transferase, and hypoxanthine phosphoribosyl transferase were analyzed in human CD4 T-lymphocyte subsets. 2. CD4 Leu 8- (helper/inducer) and CD4 Leu 8+ (suppressor/inducer) subpopulations were obtained by panning or fluorescence activated cell sorting techniques using specific monoclonal antibodies. 3. A 45% decrease of 5'-NT AMP activity in the CD4 Leu 8- cells (suppressor/inducer) compared with CD4 total cell population. 4. No statistical significant differences in enzyme activity were found between the subsets analyzed in other purine enzymes. 5. These results suggest that the distribution of purine metabolic enzymes is homogeneous in CD4 Leu 8- and CD4 Leu 8+ T-lymphocyte subpopulations.

5'-Nucleotidase↗
PubMed1985

Degenerative processes in skeletal muscle of Cd2+-treated rats and Cd2+ inhibition of mitochondrial Ca2+ transport.

In rat skeletal muscle, chronic exposure to 50 ppm Cd2+ in drinking water produced both ultrastructural and functional damage, which took place successively and increased gradually with duration of treatment. Ultrastructurally, the first effect was a regression of the sarcoplasmic reticulum, mitochondrial cristae, and glycogen granules. Then, the number of mitochondria diminished and a degeneration of myofilaments appeared. During the 9-month course of treatment, however, the terminal cisternae and the lateral saccules of sarcoplasmic reticulum remained, and the Z lines maintained their tight and rigorously parallel appearance. Functionally, the activities of two cytosolic Ca2+-sensitive enzymes (lactate dehydrogenase and malate dehydrogenase) decreased. Their partial restoration by EGTA and EDTA suggested the presence of inhibitory divalent cations in the cytosol of treated rats. Cd2+ also inhibited Ca2+ transport in mitochondria through the uncoupling of oxidative phosphorylation. Hence, an increase of Ca2+ concentration of the cytosol of Cd2+-treated rats, activating degradative enzymes such as phospholipases, proteases and phosphorylase b kinase, can be incriminated. A direct inhibitory action of Cd2+ on the activities of lactate dehydrogenase and malate dehydrogenase also occurred. Direct action of Cd2+ on certain other Ca2+-sensitive enzymes, thereby aggravating the indirect damage induced through increasing the Ca2+ concentration in cytosol, is hypothesized. In mitochondria, a Cd2+ activation of phospholipase A2 and/or a Ca2+-sensitive protease is a unique possibility, since Ca2+ accumulation was prevented by cytosolic Cd2+.

Administration, Oral↗
PubMed1987

The polycation-stimulated protein phosphatases: regulation and specificity.

Four classes of protein phosphatases are presumed to play an important role in dephosphorylating the major proteins involved in the control of general metabolism. Based on the enzyme-directed regulation of activity they have been classified as ATP,Mg-dependent-, polycation-stimulated-, Mg2+-dependent protein phosphatases and calcineurin. We have recently purified from rabbit skeletal muscle four distinct PCS protein phosphatases, classified according to the apparent molecular weight of the native enzymes in gel filtration at an early stage of the purification as: PCSH (390 kDa), PCSM (250 kDa) and PCSL (200 kDa) phosphatases. The PCSH phosphatase could be resolved into a 3(65:55 35 kDa)-subunit PCSH1 phosphatase and a 2(65:35 kDa)-subunit PCSH2 enzyme probably derived from the PCSH1 phosphatase, both characterized as specific deinhibitor phosphatases. PCSM phosphatase, a 3(72:65 35 kDa)-subunit enzyme, shows a high degree of stimulation with a low concentration optimum of polycations and is sensitive to a Ca2+-dependent protease, which brings about a five- to ten-fold increase in inhibitor-1 phosphatase activity. PCSL phosphatase is characterized by a 2(65:35 kDa)-subunit structure, a low intrinsic deinhibitor phosphatase activity and a low degree of stimulation of phosphorylase phosphatase activity requiring high concentrations of polycations. At low concentrations of polycations the stimulation of phosphorylase phosphatase activity of the PCS enzymes is enzyme-directed, since it occurs at concentrations far below the substrate concentration. The degree of stimulation is also typical for each type of enzyme (PCSM greater than PCSH1 greater than PCSH2 greater than PCSL greater than PCSC) and dependent on the polycation used; at the optimum concentration the most effective polycations (polylysine, protamine, histone H1) stimulate the phosphorylase phosphatase activity to about the same extent. Polycation concentrations above the optimum are less effective on phosphorylase phosphatase activity and can even become inhibitory to the basal activity. Whether this effect is enzyme- or substrate-directed (or both) is not known. The stimulation by polycations could be completely lost following preincubation of the PCS phosphatase with polycations. This deactivation is time-, temperature- and concentration-dependent. However the polycations did not affect the basal phosphorylase phosphatase activity. In addition to phosphorylase a and inhibitor-1, casein, myosin light chains and phosphorylase b kinase (alpha-subunit) are choice substrates for these enzymes.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1988

Identification of a third form of protein phosphatase 1 in rabbit skeletal muscle that is associated with myosin.

A third form of protein phosphatase 1 has been identified in skeletal muscle which is distinct from the species composed of the catalytic subunit complexed to the glycogen-binding subunit (protein phosphatase 1G) or inhibitor-2 (protein phosphatase 1I). The third form has an apparent molecular mass of 110 kDa, is not immunoprecipitated by antibody prepared against the glycogen-binding subunit, does not interact with glycogen and is devoid of inhibitor-2. It is tightly bound to myosin and is therefore termed protein phosphatase 1M.

Animals↗
PubMed1988

Purine and pyrimidine metabolism in human muscle and cultured muscle cells.

Using radiochemical methods, we determined the activities of various enzymes of purine and pyrimidine metabolism in homogenates of human skeletal muscle and of cultured human muscle cells. Results show a large discrepancy between the enzyme activities in muscle and cultured cells. With regard to purine metabolism, adenylate (AMP) deaminase activity was only 1-3% in cultured cells compared to that in muscle, whereas the activity of adenosine deaminase, purine-nucleoside phosphorylase, adenosine kinase, adenine phosphoribosyltransferase and hypoxanthine phosphoribosyltransferase was 7-15-fold higher in the cultured cells. The enzymes of pyrimidine metabolism, orotate phosphoribosyltransferase, orotidine 5'-monophosphate decarboxylase and uridine kinase showed activity of 100-200-fold higher in cultured cells than in adult muscle. The differences in enzyme activity are probably related to the low differentiation stage and the absence of contractile activity in the cultured muscle cells. Care must be taken when using these cells as a model for studying purine and pyrimidine metabolism of adult myofibers.

5'-Nucleotidase↗