Comparative studies on 3-oxo acid coenzyme A transferase from various rat tissues

Fenselau, Allan; Wallis, Kathleen

doi:10.1042/bj1420619

Cited by 23 publications

(8 citation statements)

References 16 publications

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“…Amongst the non-involved mouse tissues the activity of 3 oxo acid CoA transferase is highest in the heart and lowest in the liver as previously reported (Fenselau & Wallis, 1974;Tisdale & Brennan, 1983 High levels of acetoacetyl CoA thiolase are found in kidney, heart and liver. The lowest level is found in the MAC 16 tumour and this activity is significantly (P<0.003) lower than normal colon.…”

Section: Resultssupporting

confidence: 74%

Metabolic substrate utilization by a tumour cell line which induces cachexia in vivo

Tisdale¹,

Brennan²

1987

Br J Cancer

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The MAC 16 is a chemically induced transplantable adenocarcinoma of the colon which produces extensive weight loss in tumour-bearing mice without a reduction in overall food intake (Bibby et al., 1986). Weight loss appears to be directly related to the size of the tumour and is apparent at small tumour masses (less than 1% of the host body weight). We have considered this tumour to be an appropriate model of human cachexia where weight loss originates from a metabolic effect of the tumour.During the phase of host weight loss in mice bearing the MAC 16 tumour extensive mobilization of adipose tissue occurs with a corresponding rise in the plasma level of free fatty acids (FFA), although there is not a marked ketosis as might be expected in simple starvation (Tisdale et al., 1985). The tumour also has a marked hypoglycaemic effect on the host. We have reduced the host weight loss produced by the MAC 16 tumour by feeding a diet with increasing proportions of energy derived from medium chain triglycerides. In addition this dietary regime produced marked reductions in tumour size, suggesting the inability of the tumour to utilize fat as an energy source .This study compares the rate of substrate utilization and oxidative metabolism of MAC 16Correspondence: M.J. Tisdale.

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Section: Resultssupporting

confidence: 74%

Metabolic substrate utilization by a tumour cell line which induces cachexia in vivo

Tisdale¹,

Brennan²

1987

Br J Cancer

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“…This effect, observed with enzyme preparations from heart, kidney, brain and skeletal muscle from normal adult rats, has not been studied for CoA-transferases from tissues of diabetic animals, where such an inhibition could contribute to the apparently impaired tissue utilization of ketone bodies in these animals and to their development of pathological ketosis (Beatty et al, 1960;Balasse & Havel, 1971;Bates, 1972;Bassler et al, 1973;Ruderman & Goodman, 1974). We have focused our studies on skeletal-muscle CoAtransferase in diabetic rats, because skeletal muscle is the major consuming tissue for ketone bodies (Bassler et al, 1973) and because uncertainty exists about the extent of transferase activity in chronically diabetic rat muscle (Bassler et al, 1973;Williamson et al, 1971 The procedures described previously (Fenselau & Wallis, 1974b;Fenselau et al, 1975) were followed in order to obtain a total homogenate of hindquarter skeletal muscle in either 0.02M-potassium phosphate (pH7.0) or a Tris/KCl solution (pH7.4) containing 50mM-Tris/HCI, 0.1 M-KCI, 5mM-MgSO4, 1 mM-ATP and 1 mM-EDTA. The CoA-transferase activity in the phosphate medium, when necessary, could be concentrated by batchwise adsorption of the enzyme on alumina C, gel (Bio-Rad Laboratories, Richmond, CA, U.S.A.), followed by elution with a smaller volume of 0.25M-potassium phosphate (pH8.0).…”

Section: -Oxomentioning

confidence: 99%

“…Uptake of 02 in the presence and absence of acetoacetate was measured as previously described (Fenselau & Wallis, 1974b). Determination of enzyme kinetic and molecular properties Spectrophotometric measurements of CoA-transferase activity were made by detecting the formation of the Mg2+-acetoacetyl-CoA complex by using the conditions described in detail elsewhere (Fenselau & Wallis, 1974b,c).…”

Section: -Oxomentioning

confidence: 99%

“…Determination of enzyme kinetic and molecular properties Spectrophotometric measurements of CoA-transferase activity were made by detecting the formation of the Mg2+-acetoacetyl-CoA complex by using the conditions described in detail elsewhere (Fenselau & Wallis, 1974b,c). Crude CoA-transferase in the total A. FENSELAU AND K. WALLTS muscle homogenate was electrofocused on a 1 lOmlcapacity isoelectric-focusing apparatus (LKB, Rockville, MD, U.S.A.), by using procedures described previously (Fenselau & Wallis, 1974b;Fenselau etal., 1975).…”

Section: -Oxomentioning

confidence: 99%

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3-oxo acid coenzyme A-transferase in normal and diabetic rat muscle

Fenselau¹,

Wallis²

1976

Biochemical Journal

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The amounts of succinyl-CoA-3-oxo acid CoA-transferase (EC 2.8.3.5) decrease progressively in skeletal muscle in streptozotocin-diabetic rats, reaching after 10 days about 50% of the value in normal rat muscle. Electrofocusing studies indicate the occurrence of partial proteolysis of the enzyme in diabetic muscle. However, several functional parameters relating to acetoacetate utilization, including substrate inhibition, are quite similar for muscle transferase preparations from normal and diseased rats. The development of pathological ketoacidosis is discussed in the light of these observations.

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“…The suckling brain and mammary gland contain lower amounts of 3-oxoacid CoA-transferase mRNA. The enzyme activity is also highest in the adult kidney and heart and about 3-4-fold higher than in suckling brain and mammary gland [1,24]. This suggests that the expression of 3-oxoacid CoA-transferase is Northern blot analysis as described in Fig.…”

Section: Resultsmentioning

confidence: 78%

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

Ganapathi¹,

Kwon²,

Haney³

et al. 1987

Biochemical Journal

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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.

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Comparative studies on 3-oxo acid coenzyme A transferase from various rat tissues

Abstract: 1. Tissue activities, intracellular distribution as well as selected kinetic and molecular properties of succinyl-CoA-3-oxo acid CoA transferase (EC 2.8.3.5), which is an initiator of ketone body usage, were examined in rat kidney, heart, brain, skeletal muscle and liver.

Cited by 23 publications

References 16 publications

Metabolic substrate utilization by a tumour cell line which induces cachexia in vivo

Metabolic substrate utilization by a tumour cell line which induces cachexia in vivo

3-oxo acid coenzyme A-transferase in normal and diabetic rat muscle

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

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