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J W Suttie

Publications and source records attributed to J W Suttie.

16 recordsLinked to original sources
PubMed1978

Metabolism and transport of gamma-carboxyglutamic acid.

gamma-Carboxyglutamic acid residues have beeh shown to be present in prothrombin, the other vitamin K-dependent clotting factors, and more recently in bone and kidney proteins. This amino acid is formed by a posttranslational vitamin K-dependent carboxylation of glutamyl residues in polypeptide precursors of these protens. It has now been demonstrated that this amino acid, either in the free or peptide-bound form, is not metabolically degraded by the rat, but is quantitatively excreted in the urine. In nephrectomized rats, the tissue concentration of intravenously administered gamma-carboxyglutamic acid is increased, but there is still no evidence of any oxidative metabolism of this amino acid. These amino acid is transported by kidney slices against a concentration gradient, but does not accumulate in liver, intestinal or brain tissues. Preliminary data suggest that gamma-carboxyglutamic acid may be concentrated by a carrier system different from that utilized by other amino acids.

Aminoisobutyric Acids↗
PubMed1978

Vitamin K-dependent carboxylase: evidence for a hydroperoxide intermediate in the reaction.

Vitamin K is an essential cofactor for a microsomal carboxylase that converts glutamyl residues in endogenous precursor proteins to gamma-carboxyglutamyl residues in completed proteins. The same microsomal preparations convert vitamin K to its 2,3-epoxide, and it has been suggested that these two reactions (carboxylation and epoxidation) are coupled. Glutathione peroxidase, which reduces hydrogen peroxide and organic hydroperoxides, inhibits both of these reactions in a prepartion of microsomes solubilized by Triton X-100. Catalase has no effect. In the absence of vitamin K, and in the presence of NADPH, tert-butyl hydroperoxide acts as a weak vitamin K analog. At lower concentrations, tert-butyl hydroperoxide is an apparent competitive inhibitor of vitamin K for both the carboxylase and epoxidase reactions. These data are consistent with the hypothesis that both of these vitamin K-requiring reactions involve a common oxygenated intermediate, and that a hydroperoxide of the vitamin is the species involved.

Animals↗
PubMed1978

Bovine dental fluorosis: histologic and physical characteristics.

Incisor teeth from 5- to 6-year-old Holstein-Friesian cattle maintained on a ration averaging 40 ppm F annually from 4 months of age were analyzed by a variety of histologic techniques. These techniques included photomicroscopy, microradiography, protein staining, and microhardness testing. The features of fluorotic enamel that were noted were: hypomineralized outer enamel, coronal cementum hyperplasia, disrupted subsurface pigment band, hypoplastic pits, puckered incremental lines, periodic radiolucent regions, positive protein staining, and decreased microhardness of the outer enamel. These results were similar to the lesions of dental fluorosis observed in other species, and explain the external appearance of fluorotic bovine teeth observed under field conditions.

Animals↗
PubMed1978

Electron probe microanalysis of fluorotic bovine teeth.

Incisor teeth were obtained from adult cattle which since 4 months of age to 5 or 6 years were maintained on rations containing a yearly average of 40 ppm F in the forage. Microchemical analyses were performed on the fluorotic bovine incisors. The microdistribution of fluoride varied markedly at different sites within the same tooth. Fluoride concentrations varied with the depth from the tooth surface and were influenced by the concentrations of fluoride present in the forage during amelogenesis, and the presence of hypoplastic pits and hyperplastic coronal cementum in enamel. The cementum in these lesions contained remarkably high concentrations of fluoride, and it was less calcified and more porous than adjacent enamel.

Animals↗
PubMed1978

Relationship between vitamin K-dependent carboxylation and vitamin K epoxidation.

It has been postulated that the liver microsomal conversion of vitamin K hydroquinone to its 2,3-epoxide (epoxidase activity) is coupled in some obligatory fashion to the vitamin K-dependent carboxylation (carboxylase activity) event also occurring in microsomes. This hypothesis is supported by the observations that the requirements for the two reactions are similar and that conditions that promote increased carboxylation increase the epoxidase activity. It has now been shown that both of these reactions are localized in the rough microsomal fraction of a cellular homogenate, and that both activities appear to be located on the luminal rather than the outer surface of microsomal membrane vesicles. The epoxidase activity has been found to be enriched as the microsomal carboxylase activity is fractionated, and a microsomal inhibitor of the carboxylase activity had been shown to also inhibit the epoxidase activity. The enzyme glutathione peroxidase inhibits both of these activities, suggesting that a hydroperoxide of the vitamin might be an intermediate for both reactions. The organic hydroperoxide t-butyl-OOH has also been shown to have weak vitamin K-like activity in an in vitro system. These data strengthen the hypothesis that these two reactions are related, perhaps through a common intermediate, but do not provide a definite molecular role for this interrelationship.

1-Carboxyglutamic Acid↗
PubMed1976

Vitamin K-dependent carboxylase. Requirements of the rat liver microsomal enzyme system.

Vitamin K is required in an enzymatic reaction which carboxylates glutamyl residues in a microsomal protein precursor of plasma prothrombin to form gamma-carboxyglutamic acid residues. The partial requirements of this microsomal, vitamin K-dependent carboxylase system have been determined. A requirement of the system for cytosolic factors appears to be due primarily to the presence of reduced pyridine nucleotides or a reduced pyridine nucleotide-generating system in the cytosol. The hydroquinone of vitamin K has been demonstrated to be the enzymatically active form of the vitamin. When vitamin K1 hydroquinone is added to the carboxylase system, no NAD(P)H is needed for maximum activity. The carboxylase activity is half-maximally stimulated by 0.25 mug of vitamin K1/ml in the presence of cytosolic components but requires at least 10 times as much vitamin when microsomes are incubated in a cytosol-free buffer. Menadione is inactive as a vitamin source in this system, and the carboxylase activity is inhibited by the 2-chloro analog of vitamin K1 and by Warfarin. The ATP analog, AMP-P(NH)P, inhibited the carboxylase activity, but a dependence on exogenous ATP or an ATP-generating system could not be demonstrated. Carboxylase activity was found to be dependent on an O2-containing gas phase, and upon the HCO3- concentration.

Animals↗