Effect of Thyroid Hormones on the 3-Oxo Acid CoA-Transferase Activity in Rat Brain during Development

Enzyme ◽  
1980 ◽  
Vol 25 (2) ◽  
pp. 106-110 ◽  
Author(s):  
J. Diez-Guerra ◽  
M.C. Aragón ◽  
C. Giménez ◽  
F. Valdivieso
Keyword(s):  
Thyroid Hormones ◽  
Rat Brain ◽  
Transferase Activity ◽  
Coa Transferase

scholarly journals Cloning of rat brain succinyl-CoA:3-oxoacid CoA-transferase cDNA. Regulation of the mRNA in different rat tissues and during brain development

1987 ◽  
Vol 248 (3) ◽  
pp. 853-857 ◽  
Author(s):  
M K Ganapathi ◽  
M Kwon ◽  
P M Haney ◽  
C McTiernan ◽  
A A Javed ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Rat Brain ◽  
Ketone Bodies ◽  
Rat Kidney ◽  
Relative Rate ◽  
Cdna Clones ◽  
Rat Tissues ◽  
Transferase Activity ◽  
Coa Transferase ◽  
Old Rats

3-Oxoacid CoA-transferase, which catalyses the first committed step in the oxidation of ketone bodies, is uniquely regulated in developing rat brain. Changes in 3-oxoacid CoA-transferase activity in rat brain during the postnatal period are due to changes in the relative rate of synthesis of the enzyme. To study the regulation of this enzyme, we identified, with a specific polyclonal rabbit anti-(rat 3-oxoacid CoA-transferase), two positive cDNA clones (approx. 800 bp) in a lambda gtll expression library, constructed from poly(A)+ RNA from brains of 12-day-old rats. One of these clones (lambda CoA3) was subcloned into M13mp18 and subjected to further characterization. Labelled single-stranded probes prepared by primer extension of the M13mp18 recombinant hybridized to a 3.6 kb mRNA. Rat brain mRNA enriched by polysome immunoadsorption for a single protein of size 60 kDa which corresponds to the precursor form of 3-oxoacid CoA-transferase was also found to be similarly enriched for the hybridizable 3.6 kb mRNA complementary to lambda CoA3. Affinity-selected antibody to the lambda CoA3 fusion protein inhibited 3-oxoacid CoA-transferase activity present in rat brain mitochondrial extracts. The 3.6 kb mRNA for 3-oxoacid CoA-transferase was present in relative abundance in rat kidney and heart, to a lesser extent in suckling brain and mammary gland and negligible in the liver. The specific mRNA was also found to be 3-fold more abundant in the brain from 12-day-old rats as compared with 18-day-old foetuses and adult rats, corresponding to the enzyme activity and relative rate of synthesis profile during development. These data suggest that 3-oxoacid CoA-transferase enzyme activity is regulated at a pretranslational level.

scholarly journals Effect of phenylalanine metabolites on the activities of enzymes of ketone-body utilization in brain of suckling rats

1976 ◽  
Vol 160 (2) ◽  
pp. 217-222 ◽  
Author(s):  
J Benavides ◽  
C Gimenez ◽  
F Valdivieso ◽  
F Mayor
Keyword(s):  
Enzyme Activity ◽  
Mental Retardation ◽  
Rat Brain ◽  
Ketone Body ◽  
Lipid Synthesis ◽  
Developing Brain ◽  
Transferase Activity ◽  
Suckling Rats ◽  
Coa Transferase ◽  
The Brain

1. The effects of phenylalanine and its metabolites (phenylacetate, phenethylamine, phenyl-lactate, o-hydroxyphenylacetate and phenylpyruvate) on the activity of 3-hydroxybutyrate dehydrogenase (EC 1.1.1.30) 3-oxo acid CoA-transferase (EC 2.8.3.5) and acetoacetyl-CoA thiolase (EC 2.3.1.9) in brain of suckling rats were investigated. 2. The 3-hydroxybutyrate dehydrogenase from the brain of suckling rats had a Km for 3-hydroxybutyrate of 1.2 mM. Phenylpyruvate, phenylacetate and o-hydroxyphenylacetate inhibited the enzyme activity with Ki values of 0.5, 1.3 and 4.7 mM respectively. 3. The suckling-rat brain 3-oxo acid CoA-transferase activity had a Km for acetoacetate of 0.665 mM and for succinyl (3-carboxypropionyl)-CoA of 0.038 mM. The enzyme was inhibited with respect to acetoacetate by phenylpyruvate (Ki equals 1.3 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). The reaction in the direction of acetoacetate was also inhibited by phenylpyruvate (Ki equals 1.6 mM) and o-hydroxyphenylacetate (Ki equals 4.5 mM). 4. Phenylpyruvate inhibited with respect to acetoacetyl-CoA both the mitochondrial (Ki equals 3.2 mM) and cytoplasmic (Ki equals 5.2 mM) acetoacetyl-CoA thiolase activities. 5. The results suggest that inhibition of 3-hydroxybutyrate dehydrogenase and 3-oxo acid CoA-transferase activities may impair ketone-body utilization and hence lipid synthesis in the developing brain. This suggestion is discussed with reference to the pathogenesis of mental retardation in phenylketonuria.

scholarly journals Butyrate-Producing Bacteria, Including Mucin Degraders, from the Swine Intestinal Tract

2013 ◽  
Vol 79 (12) ◽  
pp. 3879-3881 ◽  
Author(s):  
Uri Y. Levine ◽  
Torey Looft ◽  
Heather K. Allen ◽  
Thad B. Stanton
Keyword(s):  
Intestinal Mucosa ◽  
Intestinal Tract ◽  
Coenzyme A ◽  
Transferase Activity ◽  
Gut Health ◽  
Content Type ◽  
Coa Transferase ◽  
Intimate Association ◽  
Butyrate Production

ABSTRACTTo identify bacteria with potential for influencing gut health, 980 anaerobes were cultured from the swine intestinal tract and analyzed for butyrate production. Fifteen isolates in the orderClostridialesproduced butyrate and had butyryl coenzyme A (CoA):acetate CoA transferase activity. Three of the isolates grew on mucin, suggesting an intimate association with host intestinal mucosa.

Effect of acute and chronic temperature transition on enzymes of cardiac metabolism in white perch (Morone americana), yellow perch (Perca flavescens), and smallmouth bass (Micropterus dolomieui)

1991 ◽  
Vol 69 (1) ◽  
pp. 258-262 ◽  
Author(s):  
Dawn H. Sephton ◽  
William R. Driedzic
Keyword(s):  
Yellow Perch ◽  
Citrate Synthase ◽  
White Perch ◽  
Perca Flavescens ◽  
Smallmouth Bass ◽  
Transferase Activity ◽  
Morone Americana ◽  
Coa Transferase ◽  
Micropterus Dolomieui ◽  
The Impact

White perch (Morone americana), yellow perch (Perca flavescens), and smallmouth bass (Micropterus dolomieui) were acclimated to 5 and 20 °C. There was an increase in ventricle mass relative to body mass in smallmouth bass only following acclimation to 5° C. Maximal in vitro activities of hexokinase, citrate synthase, carnitine acyl CoA transferase (with palmitoyl CoA, palmitoleoyl CoA, and oleoyl CoA as substrates), and total ATPase were assessed in crude heart homogenates. Tissues removed from warm-acclimated animals were tested at 20 and 5 °C; tissues removed from cold-acclimated animals were assessed at 5 °C. Acute temperature transitions were associated with decreases in the activities of hexokinase (Q10 ≈ 1.8), citrate synthase (Q10 ≈ 1.4), and ATPase (Q10 ≈ 1.7). The impact of temperature on carnitine acyl CoA transferases was generally less severe. This suggests that maximal fatty acid oxidation is conserved better than glucose oxidation during a warm to cold transition. Maximal enzyme activities were generally unaffected by the acclimation regime, with the exception of that of carnitine acyl CoA transferase in white perch heart. The substantial increase in carnitine acyl CoA transferase activity when unsaturated CoA derivatives were provided as substrate suggests an increased capacity to oxidize unsaturated fatty acids at low temperature following an acclimation period. Attempts to sustantiate this contention by offering labelled oleic acid to ventricle sheets were thwarted by a high rate of incorporation into the total lipid pool.

scholarly journals Purification and properties of succinyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney

1978 ◽  
Vol 173 (3) ◽  
pp. 759-765 ◽  
Author(s):  
J A Sharp ◽  
M R Edwards
Keyword(s):  
Isoelectric Focusing ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Coenzyme A ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Polyacrylamide Gel ◽  
Transferase Activity ◽  
Coa Transferase

CoA-transferase (succinyl-CoA-3-oxo acid CoA-transferase, EC 2.8.3.5) isolated from sheep kidney was purified to homogeneity. The purified enzyme has a specific activity of approx. 200 units/mg. A mol.wt. of 110000 was obtained by gel filtration on Sephadex G-200, and a lower mol.wt. of 102000 was determined by analytical ultracentrifugation. A sedimentation coefficient of 5.6S was also determined. A subunit mol.wt. of 56000 was obtained by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Isoelectric focusing of sheep kidney extracts indicated the presence of a single band of CoA-transferase activity with pI9.0. However, isoelectric focusing of purified CoA-transferase showed the presence of two peaks of CoA-transferase activity with pI values of 8.7 and 8.4, suggesting the presence of proteolytic activity during purification. Evidence for sheep kidney CoA-transferase being a dimer of two identical subunits has been obtained from sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the amino acid composition, peptide ‘mapping’ and N-terminal analysis.

Influence of thyroid hormones on myelin proteins in the developing rat brain

1975 ◽  
Vol 25 (1) ◽  
pp. 19-27 ◽  
Author(s):  
T. Valcana ◽  
E.R. Einstein ◽  
J. Csejtey ◽  
K.B. Dalal ◽  
P.S. Timiras
Keyword(s):  
Thyroid Hormones ◽  
Rat Brain ◽  
Myelin Proteins ◽  
Developing Rat

scholarly journals Signaling in TRPV1-induced platelet activating factor (PAF) in human esophageal epithelial cells

2010 ◽  
Vol 298 (2) ◽  
pp. G233-G240 ◽  
Author(s):  
Jie Ma ◽  
Karen M. Harnett ◽  
Jose Behar ◽  
Piero Biancani ◽  
Weibiao Cao
Keyword(s):  
Epithelial Cells ◽  
Western Blot ◽  
Transient Receptor Potential ◽  
Platelet Activating Factor ◽  
Calcium Ionophore ◽  
Transferase Activity ◽  
Ionophore A23187 ◽  
Acetyl Coa ◽  
Coa Transferase

Transient receptor potential channel, vanilloid subfamily member 1 (TRPV1) receptors were identified in human esophageal squamous epithelial cell line HET-1A by RT-PCR and by Western blot. In fura-2 AM-loaded cells, the TRPV1 agonist capsaicin caused a fourfold cytosolic calcium increase, supporting a role of TRPV1 as a capsaicin-activated cation channel. Capsaicin increased production of platelet activating factor (PAF), an important inflammatory mediator that acts as a chemoattractant and activator of immune cells. The increase was reduced by the p38 MAP kinase (p38) inhibitor SB203580, by the cytosolic phospholipase A2 (cPLA2) inhibitor AACOCF3, and by the lyso-PAF acetyltransferase inhibitor sanguinarin, indicating that capsaicin-induced PAF production may be mediated by activation of cPLA2, p38, and lyso-PAF acetyltransferase. To establish a sequential signaling pathway, we examined the phosphorylation of p38 and cPLA2 by Western blot. Capsaicin induced phosphorylation of p38 and cPLA2. Capsaicin-induced p38 phosphorylation was not affected by AACOCF3. Conversely, capsaicin-induced cPLA2 phosphorylation was blocked by SB203580, indicating that capsaicin-induced PAF production depends on sequential activation of p38 and cPLA2. To investigate how p38 phosphorylation may result from TRPV1-mediated calcium influx, we examined a possible role of calmodulin kinase (CaM-K). p38 phosphorylation was stimulated by the calcium ionophore A23187 and by capsaicin, and the response to both agonists was reduced by a CaM inhibitor and by CaM-KII inhibitors, indicating that calcium induced activation of CaM and CaM-KII results in P38 phosphorylation. Acetyl-CoA transferase activity increased in response to capsaicin and was inhibited by SB203580, indicating that p38 phosphorylation in turn causes activation of acetyl-CoA transferase to produce PAF. Thus epithelial cells produce PAF in response to TRPV1-mediated calcium elevation.

Sign in / Sign up

Export Citation Format

Share Document