Endogenous Peroxidase Activity on Mohs Frozen Sections

2018 ◽  
pp. 1
Author(s):  
Matthew R. Donaldson ◽  
L. Arthur Weber
Keyword(s):  
Peroxidase Activity ◽  
Frozen Sections ◽  
Endogenous Peroxidase

Endogenous Peroxidase Activity on Mohs Frozen Sections

2019 ◽  
Vol 45 (5) ◽  
pp. 736-737
Author(s):  
Matthew R. Donaldson ◽  
L. Arthur Weber
Keyword(s):  
Peroxidase Activity ◽  
Frozen Sections ◽  
Endogenous Peroxidase

scholarly journals DEVELOPMENT OF ENDOGENOUS PEROXIDASE IN FETAL RAT SUBMANDIBULAR GLAND

1973 ◽  
Vol 21 (1) ◽  
pp. 42-50 ◽  
Author(s):  
SHOHEI YAMASHINA ◽  
TIBOR BARKA
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Submandibular Gland ◽  
Rough Endoplasmic Reticulum ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Prenatal Development ◽  
Reaction Products ◽  
Cell Type ◽  
Endogenous Peroxidase

The prenatal development of endogenous peroxidase activity in the submandibular gland of rat was investigated by means of the diaminobenzidine-H2O2 histochemical method. The submandibular gland of a 16-day-old fetus was composed of cords of uniform, undifferentiated cells which contained no secretory granules and revealed no peroxidase activity. Peroxidase activity first appeared at the 17th day of gestation in the cisternae of the rough endoplasmic reticulum and nuclear envelope in a few cells. At the 18th day of gestation cells which exhibited reaction products in the rough endoplasmic reticulum and nuclear envelope also contained secretory granules with a strong peroxidase activity. During the last days of gestation the number of peroxidase positive cells, which contained numerous secretory granules, increased. The peroxidase-containing cells are the immediate precursors of the proacinar cells of early postnatal stages. During the same time period, when the peroxidase-containing cells differentiated, a second cell type also differentiated in the cellular cords. The development of this cell type was marked by the appearance of secretory granules stainable with toluidine blue. Through the prenatal development, this cell type revealed no peroxidase activity and was identified with the terminal tubule cell of the newborn. The morphologic and cytochemical findings indicate that terminal tubule cells and proacinar cells are committed cells; the former differentiate toward 2nd order intercalated duct cells and the latter transform to mature acinar cells.

scholarly journals INDUCTION OF ENDOMETRIAL PEROXIDASE SYNTHESIS AND SECRETION BY ESTROGEN AND ESTROGEN ANTAGONIST

1974 ◽  
Vol 62 (2) ◽  
pp. 449-459 ◽  
Author(s):  
Andrew Churg ◽  
Winston A. Anderson
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Peroxidase Activity ◽  
Secretory Granules ◽  
Combined Treatment ◽  
Initial Injection ◽  
Immature Rats ◽  
Glandular Cells ◽  
Endogenous Peroxidase ◽  
Estrogen Antagonist

Synthesis of peroxidase was induced in the uterine epithelium of immature rats by multiple doses over a 24–96-h period of either 17 ß-estradiol, the estrogen-antagonist Parke-Davis CI-628, or a combination of estradiol plus antagonist. Endogenous peroxidase activity first appeared in the cisternae of the rough endoplasmic reticulum of surface epithelial and glandular cells within 24–48 after the initial injection. Uterine peroxidase activity was also visible in the cisternae of the Golgi apparatus, in Golgi-derived secretory granules, and within the uterine and glandular lumen. Some cells of the epithelium produced little or no peroxidase, even after 96 h. Whereas the antagonist appeared to induce synthesis and secretion of peroxidase, neither the antagonist alone nor the combined treatment (estradiol plus antagonist) reproduced the estradiol-mediated growth in organ size and increased lumen diameter.

scholarly journals Factors affecting the sensitivity and specificity of the cytochemical reaction for the anti-horseradish peroxidase antibody in lymph tissue sections.

1980 ◽  
Vol 28 (7) ◽  
pp. 645-652 ◽  
Author(s):  
W Straus
Keyword(s):  
Horseradish Peroxidase ◽  
Lymph Nodes ◽  
Sensitivity And Specificity ◽  
Peroxidase Activity ◽  
Additional Advantage ◽  
Tissue Sections ◽  
Endogenous Peroxidase ◽  
Cytochemical Reaction ◽  
Cold Acetone ◽  
Antibody Reaction

Factors which increase the sensitivity and specificity of the cytochemical reaction for the antibody to horseradish peroxidase (HRP) in precursors of plasma cells and in lymphocytes were studied in sections of popliteal lymph nodes of rats. The lymph nodes were removed 3-5 days after a secondary injection of HRP into the footpads and were fixed for 5 hr in a 4% cold formaldehyde solution (Straus W: Histochemistry 53:273, 1977). Brief postfixation of the frozen sections with cold acetone improved the retention of the antigen at the sites of the antibody in the precursor cells, and it improved the quality of fixation without appreciably weakening the antigen-binding capacity of the antibody. The cytochemical reaction for the anti-HRP antibody was intensified by staining with diaminobenzidine (DAB) and H2O2 at pH 5-6, or by staining at pH 7.4 in the presence of imidazole. Imidazole partially inhibited endogenous peroxidase activity. Pretreatment with phenylhydrazine prevented nonspecific background adsorption of HRP. Phenylhydrazine had the additional advantage of inhibiting most of the endogenous peroxidase activity (Straus W: J Histochem Cytochem 20:949, 1972). The intensity of the antibody reaction in the proplasma cells developing in the medullary cords varied greatly depending on the stage of maturation from lymphocytes and blast cells. Many lymphocytes in the cortex of the lymph node showed a strong perinuclear antibody reaction when the tissue sections were postfixed with cold acetone, and the peroxidase complexed to the antibody was visualized by staining with DAB and H2O2 at pH 5-6. The antibody reaction also occurred at the surgace of many lymphocytes when the tissue sections, postfixed with cold acetone, were stained with DAB and H2O2 at pH 7.4 in the presence of imidazole. Other lymphocytes showed a strong surface, perinuclear, and cytoplasmic antibody reaction after staining at pH 5-6 as well as after staining at pH 7.4, while yet other lymphocytes remained unstained.

scholarly journals DESTRUCTION OF ENDOGENOUS PEROXIDASE ACTIVITY IN ORDER TO LOCATE CELLULAR ANTIGENS BY PEROXIDASE-LABELED ANTIBODIES

1974 ◽  
Vol 22 (1) ◽  
pp. 51-54 ◽  
Author(s):  
E. EARL WEIR ◽  
THOMAS G. PRETLOW ◽  
ANNETTE PITTS ◽  
EDWIN E. WILLIAMS
Keyword(s):  
Peroxidase Activity ◽  
Endogenous Peroxidase

scholarly journals A COMPARATIVE CYTOCHEMICAL STUDY OF MICROBODIES (PEROXISOMES) IN GREAT ALVEOLAR CELLS OF RODENTS, RABBIT AND MONKEY

1972 ◽  
Vol 20 (3) ◽  
pp. 180-191 ◽  
Author(s):  
EVELINE E. SCHNEEBERGER
Keyword(s):  
Endoplasmic Reticulum ◽  
Peroxidase Activity ◽  
Guinea Pigs ◽  
Smooth Endoplasmic Reticulum ◽  
Alveolar Cells ◽  
Cytochemical Study ◽  
Peroxidatic Activity ◽  
Endogenous Peroxidase ◽  
Light Staining

Lungs from rodents, lagomorphs and primates were briefly fixed in purified glutaraldehyde and incubated with diaminobenzidene and peroxide at pH 7.6 for the demonstration of peroxidase activity and at pH 9.0 for the demonstration of peroxidatic activity of catalase. Great alveolar cells of all animals except the rabbit contained round to elongated microbodies that stained at pH 9.0. In mice, rough and smooth endoplasmic reticulum and the perinuclear cisternae of these cells were also stained. At pH 7.6 there was no staining of great alveolar cells in any species, except in mice, where a light staining of the endoplasmic reticulum, perinuclear cisternae and microbodies persisted. In rodents, microbodies ranged in diameter from 0.13 µ in mice to 0.22 µ in guinea pigs. In monkeys they measured approximately 0.15 µ. Microbodies were not identified with certainty in rabbit great alveolar cells. In rodents the ratio of microbodies to mitochondria was roughly 1:1, whereas in primates it was roughly 1:2. Using appropriate inhibitors it was concluded that staining at pH 9.0 was due to peroxidatic activity of catalase within peroxisomes. Extraperoxisomal staining in mice was attributed to endogenous peroxidase.

scholarly journals THE FINE STRUCTURAL LOCALIZATION OF ENDOGENOUS AND EXOGENOUS PEROXIDASE ACTIVITY IN KUPFFER CELLS OF RAT LIVER

1970 ◽  
Vol 47 (1) ◽  
pp. 247-262 ◽  
Author(s):  
H. Dariush Fahimi
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Kupffer Cells ◽  
Peroxidase Activity ◽  
Biological Significance ◽  
Peritoneal Macrophages ◽  
Structural Localization ◽  
Cytochemical Demonstration ◽  
Endogenous Peroxidase ◽  
High Concentrations

Endogenous peroxidase activity has been demonstrated in sections of rat liver fixed briefly by glutaraldehyde perfusion and incubated in Graham and Karnovsky's medium for cytochemical demonstration of peroxidase activity (29). In 25–40% of sinusoidal cells, an electron-opaque reaction product is localized in segments of the endoplasmic reticulum, including the perinuclear cisternae, a few Golgi vesicles and saccules and in some large membrane-bounded granules. This staining is abolished after prolonged fixation or boiling of tissue sections in glutaraldehyde, and in the absence of H2O2 or DAB from the incubation medium. Furthermore, the reaction is inhibited completely by sodium azide and high concentrations of H2O2, and partially by KCN and aminotriazole. Among the different cells in hepatic sinusoids, the nonphagocytic "fat-storing" cells (39) are always peroxidase negative, whereas the lining cells in process of erythrophagocytosis are consistently peroxidase positive. The possible biological significance of endogenous peroxidase in Kupffer cells is discussed. In addition, the uptake of exogenous horseradish peroxidase by Kupffer cells has been investigated. The exogenous tracer protein, which in contrast to endogenous peroxidase of Kupffer cells is not inhibited by prolonged aldehyde fixation, is taken up by micropinocytosis and remains confined to the lysosomal system of Kupffer cells. The significance of these observations in respect to some recent studies suggesting localization of exogenous peroxidases in the endoplasmic reticulum of Kupffer cells and peritoneal macrophages (22, 23) is briefly discussed.

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