scholarly journals Glycerol metabolism in the neonatal rat

1970 ◽  
Vol 118 (3) ◽  
pp. 531-536 ◽  
Author(s):  
R. G. Vernon ◽  
D. G. Walker
Keyword(s):  
Kinase Activity ◽  
Neonatal Period ◽  
Glycerol Kinase ◽  
Neonatal Rat ◽  
Glycerol Metabolism ◽  
Kidney Slices ◽  
Period 2 ◽  
Liver And Kidney ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The possible role of glycerol as a precursor in neonatal gluconeogenesis in the rat was investigated by recording the activities of glycerol kinase and l-glycerol 3-phosphate dehydrogenase in the liver, kidney and other tissues around birth and during the neonatal period. 2. Blood glycerol concentrations in the neonatal rat are high. 3. There is a marked increase after birth in the ability of both liver and kidney slices to convert glycerol into glucose plus glycogen that correlates with the increase in glycerol kinase activity. 4. High hepatic and renal l-glycerol 3-phosphate dehydrogenase activities are also found in the neonatal period. 5. The marked capacity for neonatal gluconeogenesis from glycerol thus demonstrated and the role of glycerol kinase in its control are discussed.

scholarly journals Role of calcium ions and cyclic nucleotides in regulation of somatotroph functional activity in rats of different age

1994 ◽  
Vol 40 (4) ◽  
pp. 42-45
Author(s):  
V. P. Fedotov ◽  
V. I. Gudoshnikov ◽  
T. V. Mamayeva
Keyword(s):  
Neonatal Period ◽  
Secretory Activity ◽  
Neonatal Rat ◽  
Ionophore A23187 ◽  
Nucleotide Analogs ◽  
Adult Rats ◽  
Clear Cut ◽  
Derivatives Of ◽  
Camp And Cgmp

Somatotropic hormone (STH) biosynthesis and secretion were studied in primary adenohypophyseal cultures of neonatal, prepubertal, and adult rats. It was shown by disc PAAG electrophorqsiS of products synthesized in incubation of neonatal rat hypophyseal cells that L-'4C leucin incorporates predominantly in the STH containing fraction. The share of prelabeled STH secreted into the culture virtually did not depend on the age of animals, this indicating the maturity of mechanisms of basal somatotroph secretion as early as in the neonatal period of development. Ca-regulating agents (ionophore A23187, EGTA) caused quantitatively similar changes of somatotroph secretory activity in cultures of hypophyseal cells from rats of different ages. At the same time, clear-cut age-specific features of stimulating effect of dibutyryl derivatives of cAMP and cGMP on secretion of immunoreactive STH were detected. The results indicate that somatotropic function in neonatal hypophysis is a dominant one and demonstrates increased reactivity to secretogenic action of cyclic nucleotide analogs.

scholarly journals Glycerol-Mediated Repression of Glucose Metabolism and Glycerol Kinase as the Sole Route of Glycerol Catabolism in the Haloarchaeon Haloferax volcanii

2009 ◽  
Vol 191 (13) ◽  
pp. 4307-4315 ◽  
Author(s):  
Katherine E. Sherwood ◽  
David José Cano ◽  
Julie A. Maupin-Furlow
Keyword(s):  
Glucose Metabolism ◽  
Glycerol Kinase ◽  
Activity Level ◽  
Haloferax Volcanii ◽  
Glycerol Metabolism ◽  
Pcr Analysis ◽  
Carbon Utilization ◽  
Gene Encoding ◽  
Upstream Gene ◽  
Glycerol 3 Phosphate Dehydrogenase

ABSTRACT Although glycerol is the primary carbon source available to halophilic heterotrophic communities, little is known regarding haloarchaeal glycerol metabolism. In this study, a gene encoding a glycerol kinase homolog (glpK; HVO_1541) was deleted from the genome of the haloarchaeon Haloferax volcanii by a markerless knockout strategy. The glpK mutant, KS4, readily grew on yeast extract-peptone complex medium and glucose minimal medium but was incapable of growth on glycerol. Glycerol kinase activity was dependent on the glpK gene and readily detected in cells grown on glucose and/or glycerol, with the activity level higher in medium supplemented with glycerol (with or without glucose) than in medium with glucose alone. An analysis of carbon utilization revealed that glycerol suppressed the metabolism of glucose in both the parent H26 and glpK mutant strains, with catabolite repression more pronounced in the glycerol kinase mutant. Transcripts specific for glpK and an upstream gene, gpdA, encoding a homolog of glycerol-3-phosphate dehydrogenase subunit A, were upregulated (8- and 74-fold, respectively) in the presence of glycerol and glucose compared to those in the presence of glucose alone. Furthermore, glpK was transcriptionally linked to the gpdC gene of the putative glycerol-3-phosphate dehydrogenase operon (gpdABC), based on the findings of reverse transcriptase PCR analysis. The results presented here provide genetic and biochemical evidence that glycerol metabolism proceeds through a glycerol kinase encoded by glpK and suggest that a glycerol-3-phosphate dehydrogenase encoded by the upstream gpdABC operon is also involved in this pathway. Furthermore, our findings reveal a unique example of glycerol-induced repression of glucose metabolism in H. volcanii.

Influence of choline and ethanolamine administration on choline and ethanolamine phosphorylating activities of mouse liver and kidney

1979 ◽  
Vol 57 (7) ◽  
pp. 981-985 ◽  
Author(s):  
R. K. Upreti
Keyword(s):  
Substrate Concentration ◽  
Mouse Liver ◽  
Kinase Activity ◽  
De Novo ◽  
Choline Kinase ◽  
Male Mice ◽  
De Novo Synthesis ◽  
Ethanolamine Kinase ◽  
Liver And Kidney

The administration of ethanolamine to adult male mice resulted in a significant increase in ethanolamine kinase activity in liver and kidney. Similarly, choline administration resulted in a significant increase in choline kinase activity in liver and kidney. The administration of ethanolamine resulted in enhancement of choline kinase activity concomitantly with ethanolamine kinase activity in liver and kidney. The administration of choline, however, did not result in any significant increase in ethanolamine kinase activity in liver or kidney. Cycloheximide administration along with choline–ethanolamine prevented the increase in kinase activity in liver and kidney. The results obtained have been discussed in relation to the regulatory role of choline kinase and ethanolamine kinase by de novo synthesis in response to enhanced substrate concentration, the secondary nature of choline kinase induction on ethanolamine administration, and possible distinction between choline kinase and ethanolamine kinase.

Contributions of liver and kidneys to glycerol production and utilization in the dog

1996 ◽  
Vol 271 (6) ◽  
pp. E1118-E1124 ◽  
Author(s):  
S. F. Previs ◽  
S. K. Martin ◽  
J. W. Hazey ◽  
M. V. Soloviev ◽  
A. P. Keating ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Kinase Activity ◽  
Baseline Period ◽  
Glycerol Kinase ◽  
Classical Concept ◽  
Glycerol Production ◽  
Glycerol Utilization ◽  
Liver And Kidney ◽  
Anesthetized Dogs

The classical concept holds that liver and kidneys are the main sinks of glycerol released by adipose tissue. However, rates of glycerol appearance (Ra) exceed the rate of glycerol delivery to liver and kidneys. We measured the hepatic and renal contributions to glycerol production and utilization in anesthetized dogs that were fasted either overnight or for 24 h after 3 days on a carbohydrate-free diet. Dogs were infused with [2H5]glycerol, and the concentration and 2H enrichment of glycerol were measured across liver and kidney. After a baseline period, either norepinephrine or glucose plus insulin was infused to alter the rate of glycerol production. Our study shows that the production of glycerol by liver and kidneys amounted to 4-9% and 4-7% of the Ra of glycerol, respectively. Uptake of glycerol by liver and kidneys amounted to 26-30 and 10-19% of the Ra of glycerol, respectively. Thus, contrary to the classical concept, the bulk of glycerol utilization occurs in nonhepatic, nonrenal tissues that have very low glycerol kinase activity per gram.

scholarly journals Tripartite Regulation of the glpFKD Operon Involved in Glycerol Catabolism by GylR, Crp, and SigF in Mycobacterium smegmatis

2019 ◽  
Vol 201 (24) ◽  
Author(s):  
Hyun-Ju Bong ◽  
Eon-Min Ko ◽  
Su-Yeon Song ◽  
In-Jeong Ko ◽  
Jeong-Il Oh
Keyword(s):  
Energy State ◽  
Transcriptional Activator ◽  
Glycerol Kinase ◽  
Receptor Protein ◽  
Upstream Region ◽  
Glycerol Metabolism ◽  
Dihydroxyacetone Phosphate ◽  
Content Type ◽  
Cellular Energy ◽  
Glycerol 3 Phosphate Dehydrogenase

ABSTRACT The glpD (MSMEG_6761) gene encoding glycerol-3-phosphate dehydrogenase was shown to be crucial for M. smegmatis to utilize glycerol as the sole carbon source. The glpD gene likely forms the glpFKD operon together with glpF and glpK, encoding a glycerol facilitator and glycerol kinase, respectively. The gylR (MSMEG_6757) gene, whose product belongs to the IclR family of transcriptional regulators, was identified 182 bp upstream of glpF. It was demonstrated that GylR serves as a transcriptional activator and is involved in the induction of glpFKD expression in the presence of glycerol. Three GylR-binding sites with the consensus sequence (GKTCGRC-N3-GYCGAMC) were identified in the upstream region of glpF by DNase I footprinting analysis. The presence of glycerol-3-phosphate was shown to decrease the binding affinity of GylR to the glpF upstream region with changes in the quaternary structure of GylR from tetramer to dimer. Besides GylR, cAMP receptor protein (Crp) and an alternative sigma factor, SigF, are also implicated in the regulation of glpFKD expression. Crp functions as a repressor, while SigF induces expression of glpFKD under energy-limiting conditions. In conclusion, we suggest here that the glpFKD operon is under the tripartite control of GylR, SigF, and Crp, which enables M. smegmatis to integrate the availability of glycerol, cellular energy state, and cellular levels of cAMP to exquisitely control expression of the glpFKD operon involved in glycerol metabolism. IMPORTANCE Using genetic approaches, we first revealed that glycerol is catabolized through the glycolytic pathway after conversion to dihydroxyacetone phosphate in two sequential reactions catalyzed by glycerol kinase (GlpK) and flavin adenine dinucleotide (FAD)-containing glycerol-3-phosphate dehydrogenase (GlpD) in M. smegmatis. Our study also revealed that in addition to the GylR transcriptional activator that mediates the induction of the glpFKD operon by glycerol, the operon is regulated by SigF and Crp, which reflect the cellular energy state and cAMP level, respectively.

142-OR: Unique Role of the a4 Component for S6-Kinase Activity in Metabolic Regulation and Anti-apoptotic Effect in Brown Adipose Tissue

Diabetes ◽  
2019 ◽  
Vol 68 (Supplement 1) ◽  
pp. 142-OR
Author(s):  
MASAJI SAKAGUCHI ◽  
SHOTA OKAGAWA ◽  
SAYAKA KITANO ◽  
TATSUYA KONDO ◽  
EIICHI ARAKI
Keyword(s):  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Metabolic Regulation ◽  
Kinase Activity ◽  
S6 Kinase ◽  
Unique Role ◽  
Brown Adipose ◽  
Apoptotic Effect

Role of the mitogenic property and kinase activity of p60src in tumor formation by Rous sarcoma virus.

1984 ◽  
Vol 49 (2) ◽  
pp. 325-332 ◽  
Author(s):  
F Poirier ◽  
P Jullien ◽  
P Dezelee ◽  
G Dambrine ◽  
E Esnault ◽  
...  
Keyword(s):  
Rous Sarcoma Virus ◽  
Kinase Activity ◽  
Tumor Formation ◽  
Rous Sarcoma ◽  
Sarcoma Virus
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