Inhibitory effect of regucalcin on protein phosphatase activity in the nuclei of rat kidney cortex

2001 ◽  
Vol 83 (1) ◽  
pp. 111-120 ◽  
Author(s):  
Yoshiko Morooka ◽  
Masayoshi Yamaguchi
Keyword(s):  
Phosphatase Activity ◽  
Protein Phosphatase ◽  
Rat Kidney ◽  
Inhibitory Effect ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Inhibitory effect of sugars on amino acid accumulation by slices of rat kidney cortex

1962 ◽  
Vol 65 (3) ◽  
pp. 567-568 ◽  
Author(s):  
Stanton Segal ◽  
Samuel Thier ◽  
Maurice Fox ◽  
Leon Rosenberg
Keyword(s):  
Amino Acid ◽  
Rat Kidney ◽  
Inhibitory Effect ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Acid Accumulation ◽  
Amino Acid Accumulation

Inhibitory Effect of Lithium on p-Aminohippurate Transport in Rat Kidney Cortex in vitro

1985 ◽  
Vol 8 (3) ◽  
pp. 179-188 ◽  
Author(s):  
Munekazu Gemba ◽  
Akemi Tachibana ◽  
Kumi Sugihara ◽  
Mitsuhiko Hori ◽  
Mayumi Nakajima
Keyword(s):  
Rat Kidney ◽  
Inhibitory Effect ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Inhibitory effect of unconjugated bilirubin on p-aminohippurate transport in rat kidney cortex slices

1982 ◽  
Vol 693 (2) ◽  
pp. 265-272 ◽  
Author(s):  
María M. Elías ◽  
Elbio J. Comín ◽  
Marta E. Grosman ◽  
Susana A. Galeazzi ◽  
Emilio A. Rodriguez Garay
Keyword(s):  
Rat Kidney ◽  
Inhibitory Effect ◽  
Unconjugated Bilirubin ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Cortex Slices ◽  
Kidney Cortex Slices

scholarly journals Acceleration of gluconeogenesis from propionate by dl-carnitine in the rat kidney cortex

1969 ◽  
Vol 111 (1) ◽  
pp. 69-81 ◽  
Author(s):  
M. J. Weidemann ◽  
H. A. Krebs
Keyword(s):  
Carbon Dioxide ◽  
Rat Kidney ◽  
Inhibitory Effect ◽  
Kidney Cortex ◽  
Bicarbonate Concentration ◽  
Rat Kidney Cortex ◽  
Propionate Metabolism ◽  
Glucose Synthesis ◽  
High Concentrations ◽  
Cortex Slices

1. The rate of gluconeogenesis from propionate in rat kidney-cortex slices was stimulated up to 3·5-fold by dl-carnitine and by bicarbonate, and was inhibited by inorganic phosphate or high concentrations of propionate (above 3mm). 2. The stimulatory effect of carnitine was dependent on the bicarbonate concentration and could be replaced at low propionate concentration by addition of 25mm-bicarbonate–carbon dioxide buffer. At low bicarbonate concentration the carnitine concentration can be rate-limiting. 3. All observations are in accordance with the view that the action of carnitine is in principle the same as that established for other fatty acids in other tissues, namely that carnitine promotes the appearance of propionyl-CoA within the mitochondrion by acting as a carrier. 4. The accelerating effects of carnitine and bicarbonate and the inhibitory effect of phosphate can be explained on the basis of the known properties of key enzymes of propionate metabolism, i.e. the reversibility of the reactions leading to the formation of methylmalonyl-CoA from propionyl-CoA. 5. 5mm-Propionate caused a five- to ten-fold fall in the free CoA content of the tissue. This fall can account for the inhibition of respiration and gluconeogenesis caused by high propionate concentration. 6. Relatively large quantities of propionyl-l-carnitine (15% of the propionate removed) were formed when dl-carnitine was present; thus the ‘activation’ of propionate proceeded at a faster rate than the carboxylation of propionyl-CoA. The metabolism of added propionyl-l-carnitine was accompanied by glucose synthesis. 7. The appearance of radioactivity from [2−14C]propionate in both glucose and carbon dioxide was as expected on account of the randomization of C-2 and C-3 of propionate, i.e. the formation of succinate as an intermediate. 8. The maximum rate of glucose synthesis from propionate (93·3±3·3μmoles/g. dry wt./hr.) was not affected by dietary changes aimed at varying the rate of caecal volatile fatty acid formation in the rat. 9. Inhibition of gluconeogenesis by high propionate concentration was not found in those species where the rate of caecal or ruminal propionate production is high under normal conditions (rabbit, sheep and cow).

scholarly journals Gluconeogenesis in developing rat kidney cortex

1969 ◽  
Vol 111 (2) ◽  
pp. 181-185 ◽  
Author(s):  
A. Zorzoli ◽  
I. J. Turkenkopf ◽  
V. L. Mueller
Keyword(s):  
Phosphatase Activity ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Rat Kidney ◽  
Maximum Activity ◽  
Kidney Cortex ◽  
Tissue Slices ◽  
Rat Kidney Cortex ◽  
Glucose Synthesis ◽  
Developing Rat ◽  
Glucose Formation

1. Gluconeogenesis in developing rat kidney cortex was studied by assaying the activities of two enzymes, glucose 6-phosphatase and phosphoenolpyruvate carboxykinase, and by measuring glucose formation in tissue slices. 2. Glucose 6-phosphatase and phosphoenolpyruvate carboxykinase are present in late foetal (21–22-day-old) tissue and increase rapidly postnatally. Maximum activity of phosphoenolpyruvate carboxykinase occurs at 7 days of age, followed by a decline to the adult level. Glucose 6-phosphatase activity rises during the first 2 postnatal weeks and then declines. 3. Late foetuses synthesize glucose from both pyruvate and l-glutamate. The rate increases during the first 2 weeks to above adult levels. Synthesis is always higher from pyruvate than from glutamate. 4. The effect of 24hr. starvation was studied in perinatal animals. The results indicate that the ability to increase the rate of glucose synthesis as a result of starvation is not present at birth, but develops some time after the second postnatal day.

scholarly journals Increase of Na/Pi-cotransport encoding mRNA in response to low Pi diet in rat kidney cortex.

1994 ◽  
Vol 269 (9) ◽  
pp. 6637-6639
Author(s):  
A. Werner ◽  
S.A. Kempson ◽  
J. Biber ◽  
H. Murer
Keyword(s):  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

Cytochrome P-450K of rat kidney cortex microsomes: Further studies on its interaction with fatty acids

1973 ◽  
Vol 158 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Åke Ellin ◽  
Sten Orrenius ◽  
Åke Pilotti ◽  
Carl-Gunnar Swahn
Keyword(s):  
Fatty Acids ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Rat Kidney Cortex

scholarly journals Studies on the orientation of brush-border membrane vesicles

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Rat Kidney ◽  
Freeze Fracture ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Immunological Methods ◽  
Kidney Cortex ◽  
Asymmetric Distribution ◽  
Rat Kidney Cortex

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.

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