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Disease
Symptom
Drug
Enzyme
Compound
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Query: EC:1.3.5.1 (
succinate dehydrogenase
)
8,177
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The zonal distribution of enzyme activities was measured by quantitative cytochemistry in cryosections of liver from three normal children and five infants with idiopathic hepatitis of infancy. Optimal conditions for cytochemical reactions were first validated in rat liver and subsequently used in human livers to quantify zonal activities of acid phosphatase (AP),
succinate dehydrogenase
(
SDH
),
glutamate dehydrogenase
(
GDH
), glucose-6-phosphatase (G6P) and NADPH-dehydrogenase (ND). In normal rat and human livers, activities were greater for
SDH
and G6P in periportal and for
GDH
and ND in perivenular hepatocytes, while AP was evenly distributed along the sinusoids. In five infants with idiopathic hepatitis of infancy (IHI), a similar trend of distribution was observed for the two mitochondrial (
SDH
and
GDH
) and the two microsomal (G6P and ND) enzymes, although the distribution gradient was less pronounced than, in normal livers. AP showed a mildly greater periportal than perivenular activity. This preliminary study shows that a similar metabolic zonation exists for these enzymes in human livers as is observed in rats.
...
PMID:The application of quantitative cytochemistry to study the acinar distribution of enzymatic activities in human liver biopsy sections. 254 21
The activity of 7 mitochondrial enzymes, fumarase, NAD-malate dehydrogenase (MDH), citrate synthase (CS), valine dehydrogenase (VDH),
succinate dehydrogenase
(
SDH
),
glutamate dehydrogenase
(
GDH
), pyruvate dehydrogenase complex (PDHC) has been measured in platelet preparations from patients affected by Friedreich's ataxia (FA), dominant and non-dominant olivopontocerebellar atrophy (DOPCA, NDOPCA) and normal individuals. Significant decreases of
GDH
(P less than 0.01), PDHC (P less than 0.01), VDH (P less than 0.05) and
SDH
(P less than 0.05) activities were observed in FA patients. Significant decreases of
GDH
(P less than 0.01), PDHC (P less than 0.01), VDH (P less than 0.05),
SDH
(P less than 0.05) and CS (P less than 0.05) activities were Observed in ND-OPCA patients, whereas in DOPCA patients only
GDH
activity was significantly (P less than 0.05) decreased. In 8 of 10 patients with FA and in all patients with NDOPCA the activity of one or more of 4 enzymes, i.e.
GDH
, VDH,
SDH
, PDHC, was lower than the lowest of control values. Four of 6 patients with DOPCA had
GDH
activity lower than the lowest of control values. These results indicate that abnormalities of mitochondrial metabolism is a constant element in hereditary ataxia and suggest that the alteration primary leading to the different types of ataxias should be related to mitochondrial oxidative metabolism, at least at a regulatory level.
...
PMID:Abnormalities of mitochondrial enzymes in hereditary ataxias. 281 70
Isolated rat kidney cortex mitochondria were incubated at pH 7.4 in the presence or absence of a CO2/bicarbonate buffer (28 mM) to investigate the pH-independent role of bicarbonate on glutamine and glutamate metabolism. Changes in the concentration of key intermediates and products during the incubations were used to calculate metabolite flux rates through specific mitochondrial enzymes. With 1 mM glutamine and 2 mM glutamate as substrates, bicarbonate caused an inhibition of glutamate oxalacetate transaminase flux and a stimulation of glutamate deamination. The same effects were also produced with addition of either aminooxyacetate or malonate. These effects of bicarbonate were prevented when 0.2 mM malate was included as an additional substrate. Bicarbonate ion was identified as a potent competitive inhibitor of rat kidney cortex
succinate dehydrogenase
. These results indicate that aminooxyacetate, malonate, and bicarbonate all act to stimulate glutamate deamination through a suppression of glutamate transamination, and that the control by transamination of glutamate deamination is due to alterations in alpha-ketoglutarate metabolism. In contrast, in mitochondria incubated with glutamine in the absence of glutamate, bicarbonate was found to inhibit
glutamate dehydrogenase
flux. This effect was found to be due in part to the lower intramitochondrial pH observed in incubations with bicarbonate. These findings indicate that bicarbonate ion, independent of pH, may have an important regulatory role in renal glutamine and glutamate metabolism.
...
PMID:Effect of bicarbonate on glutamine and glutamate metabolism by rat kidney cortex mitochondria. 286 61
Early iron deficiency in rat does not affect the weight or the protein, DNA, and RNA content but results in a slight reduction in gamma-aminobutyric acid (GABA) (13%, p less than 0.01) and glutamic acid (20%, p less than 0.001) content of the brain. The activities of the two GABA shunt enzymes,
glutamate dehydrogenase
and GABA-transaminase, and of the NAD+-linked isocitrate dehydrogenase (ICDH) were inhibited whereas the glutamic acid decarboxylase, mitochondrial NADP+-linked ICDH, and
succinic dehydrogenase
activities remained unaltered in brain. On rehabilitation with the iron-supplemented diet for 1 week, these decreased enzyme activities in brain attained the corresponding control values. However, the hepatic nonheme iron content increased to about 80% of the control, after rehabilitation for 2 weeks. A prolonged iron deficiency resulting in decreased levels of glutamate and GABA may lead to endocrinological, neurological, and behavioral alterations.
...
PMID:Effect of early iron deficiency in rat on the gamma-aminobutyric acid shunt in brain. 287 Nov 28
Changes in the activity of three mitochondrial enzymes in rat liver after in vitro ischemia have been determined by enzyme histochemical methods. The changes were correlated with the appearance in the electron microscope of flocculent densities in the mitochondria indicative of irreversible cell injury. The flocculent densities were observed in rat liver after about 2 h of ischemia in vitro at 37 degrees C. At the same time the activity of
glutamate dehydrogenase
, localized in the mitochondrial matrix, started to decrease. However, the activities of
succinate dehydrogenase
localized in the inner membrane of mitochondria, as well as monoamine oxidase of the mitochondrial outer membrane did not change at that stage. It is concluded from the results of this study and those of others that flocculent densities are formed by denaturation of proteins of the mitochondrial matrix in which
glutamate dehydrogenase
takes part. It should be considered more as a sign than as the cause of cell death.
...
PMID:A histochemical study of changes in mitochondrial enzyme activities of rat liver after ischemia in vitro. 287 57
Rat pancreatic endocrine tumours were induced by administration of streptozotocin plus nicotinamide. Fifteen to eighteen months later tumours with wet weights of 0.1 to 224 mg were isolated. These tumours were compared with normal rat pancreatic islets. Insulin release from perifused tumours was stimulated by D-glucose, L-leucine, 2-ketoisocaproate, and D-glyceraldehyde, potentiated by theophylline and inhibited by norepinephrine. Compared with isolated rat pancreatic islets, however, insulin secretory responsiveness to glucose stimulation and insulin content were reduced in tumour tissue. Hypoglycaemia in tumour bearing rats and impaired diffusion of insulin out of the tumours may explain this difference. The pattern of enzyme activities observed in tumour tissue was typical for pancreatic endocrine tissue. The activities of
succinate dehydrogenase
, the two types of the monoamine oxidase, and alpha-glucosidase were in the normal range in tumour tissue. Only the activities of 5'nucleotidase and
glutamate dehydrogenase
were decreased. Immunocytochemical analysis of the tumours revealed that they contained an average of 91% B-cells. In addition 8% of D-cells were encountered. Proportions of A-cells and PP-cells ranged below 1%. Thus this endocrine tumour of the pancreas with a high proportion of functionally intact B-cells is an interesting model for studying regulation of secretion and endocrine tumour development.
...
PMID:Secretory, enzymatic, and morphological characterization of rat pancreatic endocrine tumours induced by streptozotocin and nicotinamide. 299 5
Acute cooling of rats led to stimulation of NAD+-dependent isocitrate dehydrogenase (ICDH),
succinate dehydrogenase
(
SDH
) and
NAD(P)+
-transhydrogenase (TH) but did not affect the NADP+-ICDH activity in liver, heart and skeletal muscle mitochondria. After pretreatment of the animals with propranolol the stimulating effect was decreased, thus suggesting that endogenous catecholamines and beta-adrenoreceptors are of importance in activation of NAD+-ICDH,
SDH
and TH. The effects of cooling, noradrenaline and cAMP did not summarize. Role of catecholamines in stimulation of mitochondrial oxidative enzymes under conditions of cooling is discussed.
...
PMID:[Stimulation of mitochondrial oxidative enzymes in acute cooling and its catecholamine mechanisms]. 302 85
The damaging effects of ADP/Fe/NADPH-induced lipid peroxidation were studied on the enzymes and membranes of rat liver mitochondria. Succinate, an inhibitor of mitochondrial lipid peroxidation, prevented or delayed most of the damage caused by the peroxidation on different mitochondrial structures and functions. There were marked abnormalities on the electrophoretic pattern of mitochondrial proteins during the course of lipid peroxidation. The disappearance of particular polypeptide bands and the accumulation of high-molecular-weight aggregates could be observed. Succinate was found to delay these effects. As a consequence of lipid peroxidation the succinate oxidase activity of mitochondria was decreased. The
succinate dehydrogenase
enzyme and the component(s) of the respiratory chain were inactivated. Succinate prevented the inactivation of
succinate dehydrogenase
but did not protect the other components of terminal oxidation chain. From the matrix enzymes the
glutamate dehydrogenase
retained its full activity but the NADP-linked isocitrate dehydrogenase was inactivated. The mitochondrial membranes became permeable to large protein molecules. Succinate prevented the inactivation of isocitrate dehydrogenase and delayed the release of protein molecules from mitochondria.
...
PMID:Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation. 303 29
Two main groups of quantitative methods are used in the brain to relate enzymatic processes to cellular structures, i.e. the methods of microchemistry and microscopic histochemistry. Microchemistry tries to quantify enzyme activities in very small brain regions by miniaturizing biochemical methods, whereas microscopic histochemistry applies staining procedures to tissue sections, preserving the structural relationship that is present in situ and giving topological information on the distribution of enzymes which is indispensable in structural heterogeneous tissue as is the brain. The present review deals preferentially with microscopic methods and, in particular, with scanning microphotometry (image plane scanning). Using this technique two measuring procedures can be applied for the quantification of enzyme activities, i.e. end-point and kinetic (continuous monitoring) measurements which are described in detail. Methods for the microphotometric demonstration of certain important dehydrogenases (isocitrate dehydrogenases,
succinate dehydrogenase
, NAD-linked malate dehydrogenase,
glutamate dehydrogenase
and glycerol 3-phosphate dehydrogenase), of cytochrome c oxidase, hexokinase and acetylcholinesterase are presented. These methods were adapted for giving optimal demonstration of enzyme activities in the rat hippocampus. The examples are given to illustrate the aptitude and possibilities of this technique in the quantification of enzymes in the complex matrix of the brain.
...
PMID:Quantitative enzyme histochemistry in the brain. 306 15
Within the uterine glands, the following enzymes were demonstrated by histochemical methods after 30, 58, 80, 100, and 110 d of pregnancy, respectively: beta-N-acetyl-hexosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, acid phosphatase, alkaline phosphatase, esterases, cytochrome oxidase, 5-nucleotidase, leucine aminopeptidase, adenosine triphosphatase, diaphorases (NADH, NADPH), glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase,
succinate dehydrogenase
, isocitrate dehydrogenase (NAD, NADP), beta-hydroxybutyrate dehydrogenase, glycero-3-phosphate dehydrogenase, NAD-glycero-3-phosphate dehydrogenase,
glutamate dehydrogenase
(NAD, NADP), lactate dehydrogenase. The results show that the activities of G-6-PDH, 6-PGDH, and cytochrome oxidase increase within secreting cells during the 2nd half of pregnancy. The activities of the other enzymes remained almost unchanged during the period of investigation. The description of our results distinguishes between gland neck, middle, and distal part of the secretory unit, respectively. In general, the enzyme activities are similar within the middle and distal gland segments, but lower in the epithelia of the neck region. The activity of dehydrogenases was medium to intensive within the middle and distal gland segments, but only low to medium within the neck portion. Of the hydrolases, the acid phosphatase, ATPase, leucine aminopeptidase, and beta-galactosidase demonstrated an intensive activity within activity secreting cells. The enzyme activities of the gland epithelia are compared with these of the uterine surface epithelia and the histochemical results are discussed in context with their significance in histiotrophic nutrition.
...
PMID:[Enzyme histochemistry of the pig placenta. III. Histotopics of enzymes in the uterine epithelium]. 309 49
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