Untersuchungen zur Methodik der Darstellung der Succinodehydrase im histologischen Schnitt

Goebel, A.; Puchtler, Holde

doi:10.1007/bf00954773

Cited by 34 publications

(4 citation statements)

References 68 publications

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“…Parallel sections with histochemical demonstration of succinate dehydrogenase [26] were used for the identification of the periportal and perivenous zone.…”

Section: Microdissectionmentioning

confidence: 99%

“…Cryostat sections (10pm) of the liver samples frozen in isopentane were prepared in a cryotom at -2O"C. Lyophilization, microdissection and determination of sample dry weight (200 -500 ng) were carried out according to Lowry and Passonneau [25]. Parallel sections with histochemical demonstration of succinate dehydrogenase [26] were used for the identification of the periportal and perivenous zone.…”

Section: Microdissectionmentioning

confidence: 99%

See 1 more Smart Citation

The Glucose/Glucose‐6‐Phosphate Cycle in the Periportal and Perivenous Zone of Rat Liver

Jungermann¹,

Heilbronn²,

Katz³

et al. 1982

European Journal of Biochemistry

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Periportal and perivenous hepatocytes contain different activities ( V ) of antagonistic key enzymes such as glucokinase and glucose-6-phosphatase. In order to get an insight into the metabolism of the periportal and perivenous area the flux rates (v) of the glucose/glucose-6-phosphate cycle were calculated on the basis of the Michaelis-Menten equation using the measured zonal concentrations of glucose and glucose 6-phosphate, the zonal activities of glucokinase and glucose-6-phosphatase previously reported and the half-saturating substrate concentrations (K,) of the two enzymes found in the literature. The concentrations of glucose were obtained as a first approximation by measuring the concentrations in portal (= periportal) and hepatovenous (= perivenous) blood; those of glucose 6-phosphate were calculated from the levels determined in microdissected periportal and perivenous liver tissue.The calculations showed (a) that the overall cycling rates agreed remarkably well with those reported for intact animals and (b) that during a normal feeding rhythm the periportal zone should catalyze net glucose output and the perivenous zone should mediate net glucose uptake, as proposed by the model of 'metabolic zonation'.Hepatocytes from the periportal (afferent) and perivenous (efferent) zone of the liver parenchyma differ in their enzyme equipments and subcellular structures [I, 21. This heterogeneity led to the model of 'metabolic zonation' [3,4]. It was proposed that the periportal hepatocytes, which are rich in glucose-6-phosphatase [5, 61, fructose-I ,6-bisphosphatase [7. 81 and phosphornolpyruvate carboxykinase [9], predominantly catalyze glucogenesis and that the perivenous cells, which are rich in glucokinase [7, 101 and pyruvate kinase [9], mainly mediate glycolysis.In the present investigation the cytosolic concentrations of glucose and of glucose-6-phosphate were measured in order to calculate the flux rates of the glucose/glucose-6-phosphate cycle in the periportal and perivenous zone of rat liver under different physiological conditions. The flux rates were to be determined using the measured zonal concentrations of glucose and glucose 6-phosphate, the zonal activities of glucokinase and glucose-6-phosphatase, as reported previously [5, 71, and the half-saturating substrate concentrations, as known from the literature [I 1 -151.It was found that the glucose concentrations in the periportal and perivenous zone were the same or formed a slight gradient depending on the metabolic situation, while the glucose-6-phosphate concentrations in the two zones were not significantly different under various conditions. Calculation of the flux rates revealed that normally the periportal zone

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“…Parallel sections with histochemical demonstration of succinate dehydrogenase [26] were used for the identification of the periportal and perivenous zone.…”

Section: Microdissectionmentioning

confidence: 99%

Section: Microdissectionmentioning

confidence: 99%

The Glucose/Glucose‐6‐Phosphate Cycle in the Periportal and Perivenous Zone of Rat Liver

Jungermann¹,

Heilbronn²,

Katz³

et al. 1982

European Journal of Biochemistry

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“…Mass density -of urineikg-l" 1 ) The cryostät sections to be stained for succinate dehydrogenase activity (20,21) were incubated at 37 9 C for 15 min in a reagent containing 50 mmol/1 sodium phosphate buffer, pH 7.6, 50 mmol/l sodium succinate, 0.28 mmol/1 tetranitro-blue tetrazolium Chloride, l mmol/1 KCN, 30 mmol/1 NaHCO 3 , 0.13 mmol/1 CaCl 2 , 0.25 mmol/1 MgCI 2 , and 0.20 mmol/1 AlCb.…”

Section: Determination Of Enzyme Catalytic Activitiesmentioning

confidence: 99%

Altered Distribution Pattern of Na+-K+-ATPase and Succinate Dehydrogenase Activities along the Nephron in Human Acute Post-Transplant Renal Failure

Schmid¹,

Mall²,

Bockhorn³

1985

Clinical Chemistry and Laboratory Medicine

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Summary:The catalytic activities of Na+-K + -ATPase and succinate dehydrogenase, marker enzymes for active salt reabsorptive capacity of renal basolateral plasma membranes and for respiratory capacity of mitochondrial cristae membranes, were studied in the maintenance phase of human acute post-transplant renal failure. Biopsies of 4 kidney-allografts taken at transplantation Operation and additionally at different posttransplantation periods, either with good function or in various stages of dysfunction, were compared with the unaffected part of a human kidney nephrectomized due to hypernephroma. In single nephron segments, Na + -K + -ATPase activity was determined after microdissection by microfluorometry, and succinate dehydrogenase activity was determined by a microphotometric procedure in stained cryosections.In intraoperative and postoperative biopsies of a well-functioning allograft, both Na + -K + -ATPase and succinate dehydrogenase activities did not differ from those of normal renal tissue. In contrast, the catalytic activities were found to be decfeased in the distal tubules of 2 anüric allografts when compared with their intraoperative controls. In addition, succinate dehydrogenase activity was reduced in distal tubules of a recovering allograft. Catalytic activities appeared to be unaffected in glomeruli, proximal tubules, and collecting ducts.It is suggested that the predominant distal tubular alterations with regard to these parameters are a consequence of increased distal tubular vulnerability due to circulatory and metabolic conditions. Verändertes Verteilungsmuster der Na + -K+-ATPase-und Succinat-Dehydrogenase-Aktivitäten entlang des Nephrons bei akutem Nierenversagen nach Nierentransplantation beim MenschenZusammenfassung: Die katalytischen Aktivitäten von Na der Erholungsphase war die Succinat-Dehydrogenase-Aktivität ebenfalls vermindert. In den Glomeruli, proximalen Tubuli und Sammelrohren wurden unveränderte katalytische Aktivitäten gemessen.Die bezüglich dieser Kenngrößen vorwiegend distal lokalisierten tubulären Veränderungen sind als Folge einer größeren Vulnerabilität dieser Nephronabschnitte auf Grund der Durchblutungs-und Stoffwechselverhältnisse anzusehen.

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“…The incubations were performed under both aerobic and anaerobic conditions. Essentially, the media and conditions used were those recommended by Sellgman and Rutenberg (15), Padykula (16), Rutenberg, Wolman, and Seligman (17), Rosa and Valardo (18), and Goebel and Puchtler (19), in which the tetrazolium salt was replaced by tellurite and to which sucrose was added. A sample of the incubating medium that was used aerobicaily or anaerobically contained in 20 ml.…”

mentioning

confidence: 99%

Histochemical Demonstration of the Sites of Activity of Dehydrogenase Systems With the Electron Microscope

Barrnett

Palade

1957

The Journal of Cell Biology

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During an attempt to test current, and develop new, histochemical methods applicable to electron microscopy, early success was obtained with a method for demonstrating the activity of dehydrogenase systems. This method depends on the fact that potassium tellurite (K2TeOa) is reduced (hydrogenated) by living tissues to a product of high electron-scattering power. More specifically, this reagent will accept electrons indirectly from respiratory enzyme systems (dehydrogenases and associated enzymes) as metabolites are oxidized by dehydrogenation. The dehydrogenases or transhydrogenases (1) are reversibly oxidized and reduced, whereas the reduced tellurite is stable and insoluble.Klett (2) was the first to notice the reduction of tellurite to a black, insoluble compound by living bacteria and proposed the reaction as a viability criterion. Subsequent studies used this reagent or selenite on bacteria (3), plant cells (4), seeds (5, 6), and yeasts (7), and Lakon (6) attributed the reaction to the activity of dehydrogenases. Recently, Wachstein (8) revived the use of tellurite as a histochemical reagent for demonstrating the presence of endogenous dehydrogenase systems in fresh animal tissues.The tellurite reaction has certain features which render it potentially adaptable to electron microscopy. For instance, the final product, reduced tellurite, formed during this reaction, is extremely insoluble and hence, can be expected to precipitate in the immediate vicinity of the reaction sites. This metallic precipitate is opaque to electrons, thus satisfying a basic requirement for any product of a histochemical reaction to be used in electron microscopy. Consequently, the tellurite could be adopted if the preparative procedures could be rendered satisfactory for electron microscopy. The requirements to be met in enzyme histochemistry are numerous and varied. As shown in detail in a recent

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Untersuchungen zur Methodik der Darstellung der Succinodehydrase im histologischen Schnitt

Cited by 34 publications

References 68 publications

The Glucose/Glucose‐6‐Phosphate Cycle in the Periportal and Perivenous Zone of Rat Liver

The Glucose/Glucose‐6‐Phosphate Cycle in the Periportal and Perivenous Zone of Rat Liver

Altered Distribution Pattern of Na+-K+-ATPase and Succinate Dehydrogenase Activities along the Nephron in Human Acute Post-Transplant Renal Failure

Histochemical Demonstration of the Sites of Activity of Dehydrogenase Systems With the Electron Microscope

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