scholarly journals THE EFFECTS OF ALDEHYDE FIXATION ON ACID PHOSPHATASE ACTIVITY IN TISSUE BLOCKS

1965 ◽  
Vol 13 (6) ◽  
pp. 476-483 ◽  
Author(s):  
DAVID T. JANIGAN
Keyword(s):  
Acid Phosphatase ◽  
Aldehyde Group ◽  
Histochemical Demonstration ◽  
Histochemical Staining ◽  
Staining Reaction ◽  
Intense Staining ◽  
The Third ◽  
Enzyme Recovery ◽  
Liver And Kidney ◽  
Soluble State

The effect of various aldehydes on phosphatase(s) of rat liver and kidney hydrolyzing the monophosphates of β-glycerol, phenol, p-nitrophenol and naphthol AS-TR at pH 5.0 was determined. Biochemical data were correlated with histochemical staining results. On the basis of enzyme recovery after fixation, the aldehydes could be divided into 3 broad groups: (1) well over 50 per cent after hydroxyadipaldehyde and glyoxal; (2) near 50 per cent after formaldehyde and methacrolein; and (3) well below 50 per cent after crotonaldehyde, glutaraldehyde, and acrolein. Acid phosphatase(s) hydrolyzing all 4 substrates showed a similar differential response to fixation by 4 aldehydes, but individual recovery values with naphthol AS-TR phosphate were distinctly lower. Tissues immersed in the first aldehyde group were soft, showed poor morphologic preservation, and a large percentage of the activity was in a soluble state; these features were reflected in the histochemical demonstration of acid phosphatase by an intense staining reaction which was judged to be unsatisfactory. The reverse held true for tissues fixed in aldehydes of the third group, using glutaraldehyde in the staining tests Evidence is presented suggesting that acid phosphatase staining results after formaldehyde fixation is dependent in part on the duration of fixation.

scholarly journals IDENTIFICATION OF PEROXISOMES IN THE RAT ADRENAL CORTEX

1972 ◽  
Vol 20 (3) ◽  
pp. 173-179 ◽  
Author(s):  
MARGARET E. BEARD
Keyword(s):  
Acid Phosphatase ◽  
Adrenal Cortex ◽  
Zona Fasciculata ◽  
Positive Staining ◽  
Staining Reaction ◽  
Dense Matrix ◽  
Zona Reticularis ◽  
Liver And Kidney ◽  
Branched Structures ◽  
Electron Dense Matrix

Organelles with the ultrastructure and cytochemical characteristics of peroxisomes (microbodies) have been identified in cells of the zona fasciculata and zona reticularis of the rat adrenal cortex. These peroxisomes appear as small, elliptical to spherical or branched structures, enclosed by a single membrane and composed of a moderately electron-dense matrix. They do not possess a nucleoid or core of the type found in peroxisomes of liver and kidney. These organelles show a strongly positive staining reaction with the diaminobenzidine technique for peroxidatic activity of catalase. This staining is inhibited by aminotriazole. In cytochemical preparations revealing acid phosphatase activity, lysosomes are strongly stained and peroxisomes are free of reaction product.

A histochemical study of calcium storage in the foot of the freshwater gastropod, Helisoma duryi eudiscus (Pilsbry)

1968 ◽  
Vol 46 (5) ◽  
pp. 987-990 ◽  
Author(s):  
S. P. Kapur ◽  
M. A. Gibson
Keyword(s):  
Alkaline Phosphatase ◽  
Staining Intensity ◽  
Histochemical Demonstration ◽  
Staining Reaction ◽  
Connective Tissues ◽  
Intense Staining ◽  
Freshwater Gastropod ◽  
Helisoma Duryi ◽  
The Matrix ◽  
And Storage

Shortly after hatching, calcium appears in the form of numerous spherules within the connective tissue of the foot of Helisoma. Concomitantly, there is a change in the histochemical demonstration of sulfated mucopolysaccharides, glycogen, and alkaline phosphatase. The sulfated mucopolysaccharide component of the mucous glands and the mucous coating of the foot increase in staining intensity. Similarly, the glycogen content of the foot epithelium and subepithelial connective tissues increases in staining intensity. Also, alkaline phosphatase first appears and exhibits an intense staining reaction within the foot epithelium. It is suggested that the coincidental appearance of these substances is related to the percutaneous absorption and storage of calcium. It is proposed that the sulfated mucopolysaccharides absorb calcium from the environment, that this calcium–mucous complex is hydrolyzed by the alkaline phosphatase, that the released calcium becomes bound to the fibers and sulfated mucopolysaccharides forming the matrix of the spherules, and that the calcium is accumulated in the form of such spherules.

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

scholarly journals ras Oncogene p21 expression is increased in premalignant lesions and high grade bladder carcinoma.

1985 ◽  
Vol 161 (5) ◽  
pp. 1213-1218 ◽  
Author(s):  
M V Viola ◽  
F Fromowitz ◽  
S Oravez ◽  
S Deb ◽  
J Schlom
Keyword(s):  
Bladder Carcinoma ◽  
Premalignant Lesions ◽  
Low Grade ◽  
Staining Reaction ◽  
High Grade ◽  
Ras Oncogene ◽  
Intense Staining ◽  
Bladder Urothelium ◽  
Normal Bladder ◽  
Ras P21

ras Oncogene p21 antigen is present in the most superficial cells of the normal bladder urothelium, as demonstrated by immunohistochemical staining. The pattern and intensity of p21 staining of cells in epithelial hyperplasia and low grade bladder carcinoma were similar to that seen in the normal urothelium. In contrast, epithelial cells in "premalignant" (dysplastic) lesions and high grade carcinomas exhibited an intense staining reaction for p21 antigen. ras p21 may be a useful marker for the malignant potential of both premalignant lesions and carcinomas of the bladder.

scholarly journals Peroxisomes in pulmonate gastropods.

1977 ◽  
Vol 25 (5) ◽  
pp. 319-328 ◽  
Author(s):  
E Dannen ◽  
M E Beard
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Positive Reaction ◽  
Smooth Endoplasmic Reticulum ◽  
Positive Staining ◽  
Staining Reaction ◽  
Arion Ater ◽  
Morphologic Characteristics ◽  
Granular Matrix

Organelles with the morphologic characteristics of peroxisomes have been found in the cells of the kidney sac of two terrestrial pulmonate gastropods. Arion ater and Ariolimax columbianus. These peroxisomes appear in profile as circles or ellipses, 0.25 micron in diameter and 0.3-0.8 micron long; They have a finely granular matrix and a single-limiting membrane; the organelles are extensively associated with smooth endoplasmic reticulum. Some Ariolimax peroxisomes contained structures reminiscent of nucleoids while those of Arion did not. The peroxisomes of Arion ater show a strongly-positive staining reaction with the 3,3'-diaminobenzidine technique, which is inhibited in the presence of aminotriazole. Peroxisomes of Ariolimax columbianus did not show a positive reaction, despite a number of variations of the 3,3'-diaminobenzidine protocol. Speculations are made concerning the biochemical reasons for this cytochemical behavior. Peroxisomes in both tissues were negatively stained while lysosomes were positively stained in acid-phosphatase incubations.

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.

The properties of acidic compartments in developing schistosomula ofSchistosoma mansoni

Parasitology ◽  
2003 ◽  
Vol 127 (3) ◽  
pp. 253-264 ◽  
Author(s):  
B. H. AL-ADHAMI ◽  
J. THORNHILL ◽  
A. AKHKHA ◽  
M. J. DOENHOFF ◽  
J. R. KUSEL
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Histochemical Staining ◽  
Transformation Process ◽  
Percentage Area ◽  
Red Dye ◽  
Energy Dependent ◽  
Acidic Compartments ◽  
Phosphatase Enzyme

A variety of fluorescent probes have been used to study the acidic compartments in cercariae and schistosomula ofSchistosoma mansoni. Freshly transformed schistosomula treated with the LysoTracker Red dye specific for lysosomes showed large acid-containing compartments (0·5–10 μm in size). The uptake of the dye is an energy-dependent process that depends on the metabolic activity of schistosomula. The compartments were quantified individually with respect to area, quantity of fluorescence and the total number/schistosomulum. Under normal conditions these compartments were not found in untreated cercariae, but appeared in cercariae slightly damaged by poly-L-lysine. The formation of these compartments seemed to be related to the development of cercariae into schistosomula as the number of compartments and uptake of fluorescence increased with time after transformation. Also, the method of transformation as well as thein vitroincubation of the parasite affected the percentage area of compartments/schistosomulum. Acid phosphatase enzyme activity was assessed using an endogenous phosphatase probe. Living and fixed schistosomula displayed the presence of enzyme activity in compartments of the same size and distribution as the acid-rich compartments. This was confirmed by histochemical staining showing deposition of enzyme-generated lead at the sites of phosphatase activity. We suggest that the development of acidic compartments is important during the transformation process or as a consequence of damage.

THE INTRACELLULAR LOCALIZATION OF LIVER AND KIDNEY SARINASE

1958 ◽  
Vol 36 (1) ◽  
pp. 21-24 ◽  
Author(s):  
Peter A. Adie ◽  
Jules Tuba
Keyword(s):  
Guinea Pig ◽  
Intracellular Localization ◽  
Particulate Fraction ◽  
The Third ◽  
Liver And Kidney ◽  
Cell Fractions ◽  
Hydrolysis Of

The cells of the liver and kidneys from three species known to be comparatively susceptible to sarin (rabbit, guinea pig, and monkey) and two species known to be less susceptible (rat and mouse) have been fractionated into their cell constituents (nuclei, mitochondria, microsomes, and non-particulate fraction). Each fraction has been tested for sarinase activity. The non-particulate fraction had the highest activity, the microsomes the second highest, the mitochondria the third highest, and the nuclei the lowest. The significance of the differences found in the distribution of sarinase activity in the cell fractions is discussed.Monkey cell fractions were also tested with ethyl N,N-dimethylphosphoramidocyanidate (tabun) as the substrate. The results were similar to those obtained with sarin, suggesting that the same enzyme was responsible for the hydrolysis of both substrates.

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