scholarly journals IMMUNOHISTOCHEMICAL LOCALIZATION OF LACTOPEROXIDASE IN BOVINE TISSUES

1973 ◽  
Vol 21 (9) ◽  
pp. 804-811 ◽  
Author(s):  
TAKAYUKI HARADA ◽  
MITSUO BABA ◽  
SHIGERU MORIKAWA
Keyword(s):  
Mammary Gland ◽  
Fluorescent Antibody ◽  
Acinar Cells ◽  
Cross Reactivity ◽  
Immunohistochemical Localization ◽  
Sublingual Gland ◽  
Alveolar Cells ◽  
Splenic Cells ◽  
Peripheral Leukocytes ◽  
Red Pulp

Distribution of lactoperoxidase in bovine tissues was investigated by using fluorescent antibody techniques, and immunochemical properties of the enzyme were also examined. As a result of immunodiffusion, two antigenic components were found, but no cross-reactivity between lactoperoxidase and hemoproteins such as catalase, cytochrome c, hemoglobin or ferritin was observed. Lactoperoxidase was found mainly in the cytoplasm of alveolar cells of the mammary gland; in those acinar cells, which were morphologically identical to serous cells, of the sublingual gland; in acinar cells of the lacrimal gland; and also in some peripheral leukocytes and in a small number of splenic cells in the red pulp. Lactoperoxidase in the alveolar and ductal spaces and in some of the ductal epithelia of those glands was observed after ethanol or acidified ethanol fixation but not after formalin fixation. It has been demonstrated by both the present and previous work (Morikawa and Harada (1969)) that lactoperoxidase and liver-catalase were distinguishable in bovine tissues when fluorescent antibody techniques were utilized.

scholarly journals IMMUNOHISTOCHEMICAL LOCALIZATION OF CATALASE IN MAMMALIAN TISSUES

1969 ◽  
Vol 17 (1) ◽  
pp. 30-35 ◽  
Author(s):  
SHIGERU MORIKAWA ◽  
TAKAYUKI HARADA
Keyword(s):  
Fluorescent Antibody ◽  
Bovine Liver ◽  
Cross Reactivity ◽  
Immunohistochemical Localization ◽  
Hepatic Cells ◽  
Surface Active Agents ◽  
Erythrocyte Catalase ◽  
Mammalian Tissues ◽  
Splenic Cells ◽  
Proximal Tubuli

The distribution of catalase was investigated in bovine tissues using fluorescent antibody techniques. The immunochemical properties of liver catalase were also examined. Two distinct components of liver catalase in immune system were found. Both of them possessed common antigenicity with erythrocyte catalase. No cross-reactivity was observed by immunodiffusion between catalase and the other hemoproteins such as lactoperoxidase, cytochrome c and hemoglobins. Bovine liver, pancreas, kidney, spleen and peripheral blood were examined. Catalase was located mainly in the cytoplasm of hepatic cells, acinar cells of the pancreas, epithelia of proximal tubuli, splenic cells scattered in the red pulp and some leukocytes. It was not found in any nucleus. Intracorpuscular catalase could be revealed in the erythrocytes treated with surface-active agents but not in frozen sections.

scholarly journals STUDIES ON ALKALINE AND ACID RIBONUCLEASES IN MAMMALIAN TISSUES IMMUNOHISTOCHEMICAL LOCALIZATION AND IMMUNOCHEMICAL PROPERTIES

1967 ◽  
Vol 15 (11) ◽  
pp. 662-673 ◽  
Author(s):  
SHIGERU MORIKAWA
Keyword(s):  
Small Intestine ◽  
Fluorescent Antibody ◽  
Fluorescein Isothiocyanate ◽  
Cross Reactivity ◽  
Immunohistochemical Localization ◽  
Rnase A ◽  
Specific Antibodies ◽  
Mammalian Tissues ◽  
Tetramethylrhodamine Isothiocyanate ◽  
Bovine Pancreas

The distribution of alkaline and acid ribonucleases (RNases) was investigated in bovine tissues using fluorescent antibody techniques. The immunochemical properties of the bovine RNases were also examined. Specific antibodies against acid and alkaline RNase obtained by immunizing rabbits with the corresponding antigens were conjugated with fluorescein isothiocyanate or tetramethylrhodamine isothiocyanate. Anti-alkaline RNase antibody reacted against alkaline RNase-A, and anti-acid RNase antibody reacted against two different acid RNases with no cross-reactivity between alkaline and acid RNases. Phosphate-buffered 10% formalin was the best general fixative among those examined, but some differences in staining results were observed depending upon the tissue and fixative employed. Two different patterns of distribution of alkaline RNase in pancreas and kidney were observed depending upon the fixative employed. The localization of RNases in bovine pancreas, liver, small intestine, kidney, spleen, lymph node, thymus, adrenal and heart were investigated and the physiologic roles of the RNases were discussed.

scholarly journals Neurofibromin expression by normal salivary glands

2021 ◽  
Vol 17 (1) ◽  
Author(s):  
Eloá Borges Luna ◽  
Pâmella Pinho Montovani ◽  
Rafaela Elvira Rozza-de-Menezes ◽  
Karin Soares Cunha
Keyword(s):  
Salivary Gland ◽  
Salivary Glands ◽  
Acinar Cells ◽  
Staining Intensity ◽  
Neurofibromatosis 1 ◽  
Tissue Type ◽  
Sublingual Gland ◽  
Minor Salivary Glands ◽  
Expression Levels ◽  
Ductal Cells

AbstractIntroductionNeurofibromin, a protein encoded by theNF1gene, is mutated in neurofibromatosis 1, one of the most common genetic diseases. Oral manifestations are common and a high prevalence of hyposalivation was recently described in individuals with neurofibromatosis 1. Although neurofibromin is ubiquitously expressed, its expression levels vary depending on the tissue type and developmental stage of the organism. The role of neurofibromin in the development, morphology, and physiology of salivary glands is unknown and a detailed expression of neurofibromin in human normal salivary glands has never been investigated.AimTo investigate the expression levels and distribution of neurofibromin in acinar and ductal cells of major and minor salivary glands of adult individuals without NF1.Material and methodTen samples of morphologically normal major and minor salivary glands (three samples of each gland: parotid, submandibular and minor salivary; and one sample of sublingual gland) from individuals without neurofibromatosis 1 were selected to assess neurofibromin expression through immunohistochemistry. Immunoquantification was performed by a digital method.ResultsNeurofibromin was expressed in the cytoplasm of both serous and mucous acinar cells, as well as in ducts from all the samples of salivary glands. Staining intensity varied from mild to strong depending on the type of salivary gland and region (acini or ducts). Ducts had higher neurofibromin expression than acinar cells (p = 0.003). There was no statistical association between the expression of neurofibromin and the type of the salivary gland, considering acini (p = 0.09) or ducts (p = 0.50) of the four salivary glands (parotid, submandibular, minor salivary, and sublingual gland). Similar results were obtained comparing the acini (p = 0.35) and ducts (p = 0.50) of minor and major salivary glands. Besides, there was no correlation between the expression of neurofibromin and age (p = 0.08), and sex (p = 0.79) of the individuals, considering simultaneously the neurofibromin levels of acini and duct (n = 34).ConclusionNeurofibromin is expressed in the cytoplasm of serous and mucous acinar cells, and ductal cells of salivary glands, suggesting that this protein is important for salivary gland function.

Fluorescent antibody techniques have allowed for the direct identification and enumeration of individual bacteria in environmental samples without requiring prior growth in culture media (Bahlool and Schmidt 1980, Cloete and Steyn 1988, Macario et al. 1989). The technique involves the use of specific antibodies raised against surface markers of defined pure cultures that are either labelled directly with fluorescent dye molecules or via a fluorescent secondary antibody. This approach has yielded important insights into the spatial distribution of microorganisms, but it suffers from a number of disadvantages. For example, expression of the antigen may be influenced by environmental factors; false-positive and false-negative results may be obtained due to cross-reactivity or lack of reaction; non-specific binding of antibodies may result in high levels of background fluorescence; and production of specific antibodies requires a pure culture of the organism of interest (Cloete and de Bruyn Various recombinant DNA techniques have subsequently been developed that are independent of cultivation methods (Fig. 1). These techniques provide ways of detecting and quantifying specific phylogenetic groups of microbes on 16S rDNA sequences, and relevant structural genes provide ways of monitoring microbial populations of environmental and industrial systems. In addition to these tools, a number of emerging technologies such as the use of biomarker genes are being increasingly used to monitor with great precision and accuracy the behaviour of microbes in the environment.

2003 ◽  
pp. 218-219
Keyword(s):  
Recombinant Dna ◽  
Culture Media ◽  
Specific Binding ◽  
Fluorescent Antibody ◽  
False Negative ◽  
Cross Reactivity ◽  
Phylogenetic Groups ◽  
Specific Antibodies ◽  
Negative Results ◽  
Recombinant Dna Techniques

scholarly journals Immunohistochemical localization of melatonin in the rat Harderian gland.

1976 ◽  
Vol 24 (11) ◽  
pp. 1173-1177 ◽  
Author(s):  
G A Bubenik ◽  
G M Brown ◽  
L J Grota
Keyword(s):  
Acinar Cells ◽  
Harderian Gland ◽  
Immunohistochemical Localization ◽  
Mature Male ◽  
Male Rats ◽  
Secretory Cells ◽  
Yellow Fluorescence ◽  
Double Antibody

Using fluorescence and double antibody techniques, melatonin was localized immunohistologically in the secretory cells of the Harderian gland of mature male rats. The presence and quantity of melatonin in the acinar cells seem to correlate with the amount of porphyrins inside the lumen. The specificity was proven by disappearance of yellow fluorescence after saturation of antibody with melatonin or after use of nonspecific antibody only.

scholarly journals ENZYME-LABELED ANTIBODIES FOR THE LIGHT AND ELECTRON MICROSCOPIC LOCALIZATION OF TISSUE ANTIGENS

1967 ◽  
Vol 33 (2) ◽  
pp. 307-318 ◽  
Author(s):  
Paul K. Nakane ◽  
G. Barry Pierce
Keyword(s):  
Acid Phosphatase ◽  
Basement Membrane ◽  
Fluorescent Antibody ◽  
Enzymatic Reaction ◽  
Immunohistochemical Localization ◽  
Fluorescent Antibody Technique ◽  
Reaction Products ◽  
Electron Microscopic ◽  
Antibody Technique ◽  
Tissue Antigens

Enzymes, either acid phosphatase or horseradish peroxidase, were conjugated to antibodies with bifunctional reagents. The conjugates, enzymatically and immunologically active, were employed in the immunohistochemical localization of tissue antigens utilizing the reaction product of the enzymatic reaction as the marker. Tissues reacted with acid phosphatase-labeled antibodies directed against basement membrane were stained for the enzyme with Gomori's method, and those reacted with peroxidase-labeled antibody were stained with Karnovsky's method. The reaction products of the enzymes localized in the basement membrane. Unlike the preparations of the fluorescent antibody technique, enzyme-labeled antibody preparations were permanent, could be observed with an ordinary microscope, and could be examined with the electron microscope. In the latter, specific localization of antibody occurred in the basement membrane and in the endoplasmic reticulum of cells known to synthesize basement membrane antigens. The method is sensitive because of the amplifying effect of the enzymatic activity. The ultrastructural preservation and localization were better with acid phosphatase-labeled antibody than with peroxidase-labeled antibody, but acid phosphatase conjugated antibody was unstable and difficult to prepare. Peroxidase-antibody conjugates were stable and could be stored for several months at 4°C, or indefiniely in a frozen state.

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