scholarly journals HISTOCHEMICAL DEMONSTRATION OF N-ACETYL-β-GLUCOSAMINIDASE EMPLOYING NAPHTHOL AS-BI N-ACETYL-β-GLUCOSAMINIDE AS SUBSTRATE

1965 ◽  
Vol 13 (5) ◽  
pp. 355-360 ◽  
Author(s):  
MASANDO HAYASHI
Keyword(s):  
Enzyme Activity ◽  
Lysosomal Enzymes ◽  
Rat Kidney ◽  
Histochemical Demonstration ◽  
Frozen Sections ◽  
Aqueous Methanol ◽  
Hepatic Cells ◽  
Cytological Localization ◽  
Convoluted Tubules ◽  
Methanolic Ammonia

The N-acetyl-β-glucosaminide of naphthol AS-BI (7-bromo-3-hydroxy-2-naphth- o-anisidide) was obtained by reacting the anisidide with acetochloroglucosamine in aqueous alkaline acetone. After removal of O-acetyl groups with methanolic ammonia and recrystallization from aqueous methanol, the compound may be used as a substrate for N-acetyl-β-glucosaminidase. Formol-calcium fixed frozen sections were incubated with 0.5 mM substrate in the presence of hexazonium pararosanilin or fast garnet GBC at pH 5.2. Staining appeared in the cytoplasm mostly as discrete granules at the presumed site of enzyme activity and was inhibited in the presence of N-acetylglucosaminolactone. In the rat kidney a number of spherical granules which stained for the enzyme were observed in the proximal portion of the proximal convoluted tubules. In the liver staining was recognized as small granules localized at the pericanalicular cytoplasm of parenchymal hepatic cells. The general cytological localization in these tissues was quite similar to that of other lysosomal enzymes. The limitations of the technique were briefly discussed.

scholarly journals Freeze substituted tissue in 5'-nucleotidase histochemistry. Comparative histochemical and biochemical investigations.

1979 ◽  
Vol 27 (12) ◽  
pp. 1582-1587 ◽  
Author(s):  
K Klaushofer ◽  
H von Mayersbach
Keyword(s):  
Enzyme Activity ◽  
Sensitivity And Specificity ◽  
Rat Liver ◽  
Freeze Substitution ◽  
High Sensitivity ◽  
Histochemical Demonstration ◽  
Frozen Sections ◽  
Enzyme Localization ◽  
Fresh Frozen ◽  
Preparation Techniques

The suitability of freeze-substitution in n-butanol and paraffin embedding of tissues for the histochemical demonstration of 5'-nucleotidase was investigated and compared with commonly used preparation techniques, such as fresh frozen sections and cryostate sections of cold formalin and glutaraldehyde-fixed rat liver. The influences of each step of the preparation techniques on the enzyme activity were controlled by a quantitative radiochemical assay. Freeze substitution was revealed to be superior to the commonly used preparation techniques with respect to: 1) high sensitivity and specificity of the histochemical 5'-nucleotidase reaction (this is based on the fact that incubation media with very low lead concentrations (0,6 mM/1) can be used); 2) excellent morphological appearance of the tissues showing cytological details of enzyme localization; 3) unlimited storage of the tissue materials and ease of sectioning.

A Comparison of the Histochemical Enzyme Pattern in Normal and Varicose Veins

1987 ◽  
Vol 2 (3) ◽  
pp. 135-158 ◽  
Author(s):  
Bernhardt Haardt
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Lysosomal Enzymes ◽  
Adenosine Triphosphatase ◽  
Varicose Veins ◽  
Histochemical Demonstration ◽  
Saphenous Veins ◽  
The Media ◽  
Enzyme Pattern

In order to study enzyme activity in the walls of healthy and diseased veins, sections were taken from the stripped varicose long saphenous veins of eight patients. These were subjected to histochemical enzyme investigations. These methods were used to determine levels and localization of lactate dehydrogenase, alkaline phosphatase, adenosine triphosphatase and the lysosomal enzymes, β-glucuronidase, non-specific esterases and acid phosphatase. The method and our findings are described. The results of these histochemical investigations demonstrate an increase in lysosomal enzyme activity in the walls of varicose veins as compared to that of normal veins. This increase is greater in the media than in the intima. Enzymes responsible for energy metabolism demonstrated contradictory behaviour, with decline in the activity of such enzymes in the walls of varicose veins. This decline in enzyme activity was more marked in the intima than in the media and was especially noticeable in the histochemical demonstration of Ca++-adenosine triphosphatase.

scholarly journals An immunohistochemical study of aspartate, glutamate, and taurine in rat kidney.

1994 ◽  
Vol 42 (5) ◽  
pp. 621-626 ◽  
Author(s):  
N Ma ◽  
E Aoki ◽  
R Semba
Keyword(s):  
Amino Acids ◽  
Renal Cortex ◽  
Rat Kidney ◽  
Renal Medulla ◽  
Loop Of Henle ◽  
Immunoperoxidase Method ◽  
Collecting Tubules ◽  
Convoluted Tubules ◽  
Thin Portion ◽  
Intrarenal Distribution

Biochemical studies have revealed considerable amounts of free amino acids in the kidney. We examined the intrarenal distribution of three amino acids (aspartate, glutamate, and taurine) in the rat kidney with an immunoperoxidase method. In the renal cortex, all three amino acids were concentrated in the renal corpuscles and in the epithelia of the collecting tubules. Immunostaining of the collecting tubules was more intense in the principal cells than in the intercalated cells. The distal convoluted tubules were also immunostained with aspartate- and glutamate- specific antibodies but not with the taurine-specific antibody. In the renal medulla, the immunoreactivity specific for aspartate and for glutamate was similar; it was weak in the thick portion of the loop of Henle and strong in the collecting tubules. Immunoreactivity specific for taurine was restricted to regions within the epithelia of the thin portion of the loop of Henle and the collecting tubules. The significance of the accumulated amino acids as osmoregulatory agents is discussed.

scholarly journals ON THE LOCALIZATION OF SOME PHOSPHATASES IN THREE DIFFERENT SEGMENTS OF THE PROXIMAL TUBULES IN THE RAT KIDNEY

1967 ◽  
Vol 15 (8) ◽  
pp. 456-469 ◽  
Author(s):  
N. O. JACOBSEN ◽  
F. JØRGENSEN ◽  
Å. C. THOMSEN
Keyword(s):  
Adenosine Triphosphate ◽  
Rat Kidney ◽  
Adenosine Monophosphate ◽  
Adenosine Diphosphate ◽  
Proximal Tubules ◽  
Reaction Pattern ◽  
Cytoplasmic Bodies ◽  
Acid And Alkaline Phosphatase ◽  
Convoluted Tubules

The distribution of several phosphatases in three segments of the proximal tubules was studied in frozen sections of glutaraldehyde-fixed rat kidneys. Two segments of the convoluted tubules were identified by in vivo injection of trypan blue. By increasing the concentration of adenosine triphosphate to 3 mM in the Wachstein and Meisel ATPase medium, a clear segmental differentiation in the reaction pattern of the brush border, cytoplasmic bodies and basal infoldings of the proximal tubules was obtained. The specificity of the reaction was investigated by substituting adenosine diphosphate, adenosine monophosphate or β-glycerophosphate for adenosine triphosphate in the incubation medium and by employing cyanide or fluoride as inhibitors. The reaction pattern was also compared with the localization of acid and alkaline phosphatase activities. In addition, the distribution of glucose 6-phosphatase activity was studied which showed differences in the three segments of the proximal tubules.

A Study of the Histochemical Demonstration of Cytochrome Oxidase

1964 ◽  
Vol s3-105 (72) ◽  
pp. 497-502
Author(s):  
R. G. BUTCHER ◽  
J. V. DIENGDOH ◽  
J. CHAYEN
Keyword(s):  
Enzyme Activity ◽  
Cardiac Muscle ◽  
Cytochrome Oxidase ◽  
Histochemical Demonstration ◽  
Lugol’S Iodine ◽  
Liver And Kidney

Burstone's procedure for the histochemical demonstration of cytochrome oxidase has been studied and applied to sections prepared by freezing in hexane and cutting by the controlled-temperature freezing-sectioning technique. The method has been modified by the inclusion of a treatment with Lugol's iodine to yield a stronger colour, which is stable for at least several weeks and which localizes the enzyme activity more precisely. The variants of the reaction have been compared in their effect on cardiac muscle, liver, and kidney of the rat.

scholarly journals The effect of different doses levels of silver nanoparticles (AgNPs) on the kidney and liver in Albino male Rat. Histopathological study

2014 ◽  
Vol 11 (4) ◽  
pp. 1503-1509
Author(s):  
Baghdad Science Journal
Keyword(s):  
Silver Nanoparticles ◽  
Body Weight ◽  
Male Rat ◽  
Central Vein ◽  
Average Particle ◽  
Ag Nps ◽  
Hepatic Cells ◽  
Liver And Kidney ◽  
Collecting Tubules ◽  
Convoluted Tubules

Objective: In this study ,the effects of silver nanoparticles (Ag NPs)were investigated on the liver and kidney tissues. Methodology: The produced nanoparticles have an average particle size of about 30 nm. Eighteen male albino rats were used by dividing them into three groups, each group comprise 6 rats. First group(control group) given food and water like other groups by liberty. Second group was tail injected by (AgNPs) at dose of (0.4 mg/kg. body weight/day). Third group was injected by (AgNPs) at dose of (0.6 mg/kg. body weight/day) for 15 days. All animals were sacrified at the end of experiment. The liver and kidney tissues specimens were fixed in 10% formalin and histological preparations were carried out then stained with H&E. Pathological changes in liver and kidney tissues were showed. Results: Histopathological studies revealed the harmful effect of the silver nanoparticles uses on the liver and kidney rats, second group that treated with Ag NPs (0.4 mg/kg.body.weight/day), kidney sections showed enlargement of collecting tubules, increase in interstitial tissue medulla, necrosis and enlargement in proximal and distal convoluted tubules. Liver showed enlargement of the central vein and degeneration of hepatic cells. Third group that treated with Ag NPs (0.6 mg/kg. body weight/day); kidney sections showed hyperplasia of the interstitial connective tissue of renal medulla with hemorrhages, renal cortex showed, degenerative changes and necrosis of proximal and distal convoluted tubules. Liver section showed congestion and necrosis of hepatic cells. Conclusion: Silver nanoparticles cause damage in liver and kidney tissues. Recommendation: Further study is needed for the effect of Ag NPs on the other tissues.

scholarly journals Regulation of glucocorticoid receptor function and angiotensin-converting enzyme activity

1997 ◽  
Vol 43 (4) ◽  
pp. 51-54
Author(s):  
P. P. Golikov
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzyme Activity ◽  
Glucocorticoid Receptors ◽  
Converting Enzyme ◽  
Receptor Function ◽  
Angiotensin Converting Enzyme Activity ◽  
Mammalian Tissues ◽  
Shock Proteins ◽  
Convoluted Tubules ◽  
Direct Biosynthesis

The central link in the mechanism of action of glucocorticoids is specific cytoplasmic glucocorticoid receptors (GH). Their synthesis is programmed by 1 gene of chromosome 5 [44]. The direct biosynthesis of GR occurs in the endoplasmic reticulum of the cytoplasm [12]. In the cytoplasm, GRs bind to heat shock proteins (HSP, chaperone proteins) mol. mass of 50, 70, 90 kD [20, 59]. Like the mass of the GR – HSP complex is 300 kD [14]. In the absence of glucocorticoids, GRs are localized mainly in the cytoplasm [30, 63]. In 1 cell contains from 5000 to 100 000 specific GH. GRs have been found in many mammalian tissues [13], however, certain tissues do not contain GRs: the intermediate pituitary, Kupffer and endothelial cells of the liver, renal glomeruli, and proximal convoluted tubules [12, 31].

scholarly journals THE STAGES IN CALCIFICATION OF THE RAT KIDNEY AFTER THE ADMINISTRATION OF URANIUM NITRATE

1953 ◽  
Vol 97 (5) ◽  
pp. 681-694 ◽  
Author(s):  
Lewis K. Dahl
Keyword(s):  
Ferrous Iron ◽  
Rat Kidney ◽  
Cellular Damage ◽  
Appreciable Amount ◽  
Wide Range ◽  
Uranium Nitrate ◽  
Speed Of Evolution ◽  
Dose Levels ◽  
Convoluted Tubules ◽  
Inner Cortex

The anatomical and histochemical alterations in rat kidneys after the parenteral administration of uranium nitrate [UO2(NO3)2·6H2O] have been studied. The histological effects produced by this agent over a wide range of dose levels were nearly identical in character and differed principally in their speed of evolution. The deposition of calcium always began at foci in the cytoplasm of the cells of the proximal convoluted tubules of the inner cortex. It remained intracellular until the cell boundaries were destroyed. Deposits of calcium could be found before any other cellular damage could be demonstrated by histological examination. Later, when degeneration and necrosis were present, the foci of calcification were imperfectly related to them in location or degree. In contrast, the amount of calcification was correlated with the dose of uranium nitrate, being greatest in the kidneys of rats that received 20 mg./kg., next greatest in the 30 mg./kg. rats, less in the 10 mg./kg. rats, and slight in those that received 2 mg./kg. Histochemical stains for ferric and ferrous iron, chondroitinsulfate, and polysaccharides gave results that were negative or unrelated to the deposits of calcium, thus making it unlikely that these substances held any appreciable amount of calcium in the tissue. Yet it is clear that some anion other than phosphate must be combined with part of the calcium; the results with the alizarin and von Kóssa stains confirmed an earlier result (1) in showing that the first deposits of calcium are formed without comparable accumulations of phosphate.

Histochemical Demonstration of Certain DPN-Linked Dehydrogenases and of Aldolase in the Red and White Fibres of Pigeon Breast-Muscle

1962 ◽  
Vol s3-103 (61) ◽  
pp. 41-46
Author(s):  
J. C. GEORGE ◽  
C. L. TALESARA
Keyword(s):  
Enzyme Activity ◽  
Histochemical Demonstration ◽  
Breast Muscle ◽  
Strictly Anaerobic ◽  
Anaerobic Conditions ◽  
High Concentration ◽  
Hydrogen Acceptor ◽  
Localization Pattern ◽  
Important Link

The distribution and localization-pattern of certain DPN-linked dehydrogenases (malic, lactic, D-glucose, glutamic, and a-glycerophosphate) were demonstrated histochemically in the red and white fibres of pigeon breast-muscle by using neotetrazolium as the hydrogen acceptor, under strictly anaerobic conditions. All the dehydrogenases studied showed distinctly higher enzyme activity in the narrow red fibres than in the broad white fibres. That of a-glycerophosphate was, however, found to be appreciably more abundant than other dehydrogenases in the broad fibres. A high concentration of aldolase, which forms an important link in the chain of enzymes in glycolysis, was histochemically demonstrated in the broad, white, glycogen-loaded fibres.

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