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  • 1
    Electronic Resource
    Electronic Resource
    Differential expression of moesin in cells of hematopoietic lineage and lymphatic systems (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 33-41 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Moesin is a member of the ERM family consisting of ezrin, radixin, and moesin. The protein is located in the plasma membrane similarly to ezrin and radixin, and is thought to regulate cellular movements and morphological changes. Using monoclonal antibody CR-22, the specificity of which against human moesin was confirmed by immunoprecipitation and western blotting analysis, we immunohistochemically stained various formalin-fixed and paraffin-embedded human tissues, in particular, clots of bone marrow and lymphatic tissues, to examine moesin expression in cells of hematopoietic lineage and lymphatic systems. In the bone marrow, moesin was expressed in myeloid cells, while little staining was detected in erythroid cells. Moesin was highly expressed in both the center and the periphery of mature megakaryocytes. In the lymphatic tissues, moesin was strongly expressed by T-lymphocytes in the paracortex. In the mantle zone, the periphery of the germinal center, moesin was expressed by small lymphocytes which were identified as B-lymphocytes. Furthermore, in areas of inflammation, moesin was expressed in both the center and the periphery of neutrophils, whereas in some neutrophils in distant areas, moesin was localized at the cellular periphery. These results suggest that differential expression of moesin in these cells is involved in their morphology and specialized functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050262
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  • 2
    Electronic Resource
    Electronic Resource
    New monoclonal antibodies against gastric gland mucous cell-type mucins: a comparative immunohistochemical study (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 113-119 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The immunohistochemical reactivity of monoclonal antibodies raised against rat and pig gastric mucins (HIK1083, PGM36, and PGM37) was investigated in normal gastrointestinal tracts obtained from fish, amphibians, reptiles, birds, and mammals (including humans). These monoclonal antibodies exhibited highly selective reactivity with class III mucins, as identified by paradoxical concanavalin A stain, in the gastrointestinal tract of vertebrates. All three monoclonal antibodies reacted with the mucous neck cells and pyloric gland cells of amphibians, reptiles and mammals, the cardiac glands of reptiles and mammals, and Brunner’s glands of mammls. The deep crypt secretory cells of the rat colon and certain goblet-type cells deep in crypts in the pig colon differed from the above pattern only in that they did not show immunoreactivity with monoclonal antibody PGM36. These data suggest that the development of class III mucin is a fundamental evolutionary characteristic of vertebrate gastric mucins. These monoclonal antibodies should prove useful for the investigation of cell differentiation among gastrointestinal mucous cells and for the biochemical analysis of gastrointestinal mucins in different species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050272
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  • 3
    Electronic Resource
    Electronic Resource
    Expression of N-acetylglucosamine Residues in Developing Rat Fundic Gland Cells (2000)
    Springer
    Journal of molecular histology 32 (2000), S. 187-193 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The development of rat fundic gland was studied by immunohistochemistry using a recently developed monoclonal antibody, HIK 1083, at both light and electron microscope levels. Antibody HIK 1083 recognized oligosaccharides with a non-reducing terminal α-linked N-acetylglucosamine (GlcNAc) residue. In the developing rat fundic gland, cells expressing α-GlcNAc residues were discernible from day 19.5 of gestation and continued to exist till adult. The distribution of the α-GlcNAc expressing cells was consistent with that described previously for cells reacting to Griffonia simplicifolia lectin (GSA-II) in all developmental stages. These cells were located at the bottom of the fundic gland when they first appeared. With the elongation and maturation of the gland, these cells moved upwards and were finally restricted in the neck region of the gland. Combining previous reports and the present electron microscopical observations, HIK 1083-positive cells in the adult rat fundic gland are mucous neck cells. The interaction between antibody HIK 1083 and GSA-II lectin was investigated. GSA-II prevented the subsequent binding of HIK 1083, while HIK 1083 did not prevent GSA-II binding to mucous neck cells. Our results suggested that α-GlcNAc residues exist in rat fundic gland from day 19.5 of gestation and continue to exist till adult. Cells expressing α-GlcNAc residues appeared as typical mucous neck cells from postnatal four weeks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004051408239
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  • 4
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of plasma retinolbinding protein and prealbumin in human pancreatic islets (1986)
    Springer
    Journal of molecular histology 18 (1986), S. 164-168 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary This study was undertaken, employing the immunoenzyme method, to confirm the presence of retinol-binding protein in human pancreatic islets, and to compare its distribution with that of prealbumin, insulin, glucagon, somatostatin and pancreatic polypeptide. It was found that most islet cells contained retinol-binding protein, although centrally located cells showed stronger reactivity than those in the peripheral region. The distribution of each of the five polypeptides differed from that of retinolbinding protein, indicating that these peptides did not cross-react with anti-retinol-binding protein antibody. Islet cells which contained prealbumin, on the other hand, were mostly classified as A cells. Further studies are necessary to confirm whether the islet cells produce retinol-binding protein or only store it.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01676116
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  • 5
    Electronic Resource
    Electronic Resource
    Alternating laminated array of two types of mucin in the human gastric surface mucous layer (1992)
    Springer
    Journal of molecular histology 24 (1992), S. 86-92 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Attempts have been made to develop a procedure for preserving and analysing the surface mucous layer of the human stomach in paraffin sections. Histologically normal gastric mucosae were obtained from 20 surgically removed stomachs. Of the different fixatives tested, Carnoy's solution gave rise to the most satisfactory results. In Haematoxylin-Eosin stained sections, the surface mucous layer appeared as a thick eosinophilic layer coating the gastric mucosal surface and measured 55.4±2.5 μm in the fundus and 21.8±1.0 μm in the pylorus respectively. A dual staining method consisting of galactose oxidase-cold thionine Schiff and paradoxical concanavalin A staining was applied to the surface mucous layer in order to reveal the distribution pattern of mucins secreted by two types of mucous cell in the gastric mucosa: surface mucous cells and gland mucous cells. As a result of this staining, an alternating laminated layer was visualized which consisted of the particular two types of mucin. In five cases, the surface mucous layer was examined in unfixed frozen sections. This layer was only partially preserved but revealed the same laminated structure. These results indicated that gland mucous cell mucins contribute to form the surface mucous layer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01082444
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  • 6
    Electronic Resource
    Electronic Resource
    Histone H3 messenger RNA in situ hybridization for identifying proliferating cells in formalin-fixed rat gastric mucosa (1997)
    Springer
    Journal of molecular histology 29 (1997), S. 867-873 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To devise a more sensitive method for identifying proliferative cells in routinely formalin-fixed, paraffin-embedded tissues, we applied an in situ hybridization (ISH) technique for the detection of histone H3 mRNA in rat gastric mucosa and amplified the signal by a silver intensification method. ISH was performed using a Fluorescein-labelled, single-stranded DNA probe for the human histone H3 gene. To determine the optimal conditions for detecting H3 mRNA in rat gastric mucosa, we tested the effect of changing conditions, such as fixation time and digestion time, by a proteinase before hybridization. Next, the proliferation indices obtained using H3 ISH were compared with those obtained using bromodeoxyuridine (BrdU) immunohistochemistry. In normal rat gastric mucosa, H3 ISH- and BrdU-positive cells were confined to the neck region of both fundic and pyloric mucosa. The two labelling indices were almost the same. In all the serial sections studied, H3 ISH-positive cells were almost always BrdU-positive too. Taken together, these results indicate that the H3 ISH technique is useful for the evaluation of proliferative activity in gastric epithelial cells by virtue of its detection of S-phase cells
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026493924641
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  • 7
    Electronic Resource
    Electronic Resource
    Establishment of monoclonal antibodies against carbohydrate moiety of gastric mucins distributed in the different sites and layers of rat gastric mucosa (1996)
    Springer
    Glycoconjugate journal 13 (1996), S. 857-864 
    Details
    ISSN: 1573-4986
    Keywords: gastric mucin ; monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Eight monoclonal antibodies (MAbs), designated RGM21 ∼ RGM42, were generated against mucin purified from the rat gastric mucosa. By applying ELISA, all of these MAbs were proved to react not only with the purified mucin, but also with the oligosaccharide mixture obtained from the antigenic mucin by alkaline borohydride treatment. Treatment of the mucin-attached ELISA well with trypsin, sodium periodate or galactose oxidase prior to the addition of the MAb was applied to characterize these MAbs. Histochemical observation indicated that all these MAbs were able to stain the formalin fixed-paraffin embedded sections of the rat gastroduodenal mucosa. Although each of these MAbs reacted with distinct mucus-producing cells localized in particular regions of the gastroduodenal mucosa, their staining specificity could generally be classified into four groups. These MAbs might be useful for estimating the physiological and pathological changes of mucins in the gastric mucosa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00702350
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  • 8
    Electronic Resource
    Electronic Resource
    Ultrastructural carbohydrate cytochemistry of gastric epithelium (1978)
    Springer
    Journal of molecular histology 10 (1978), S. 309-331 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis On examination with ultrastructural methods for visualizing thevicinal glycols and acid groups of complex carbohydrates, the most superficial surface epithelium of the rat gastric corpus displayed biphasic mucous droplets consisting of a cortex of hexose-rich (i.e. periodate-reactive) neutral mucosubstance and an uncharacterized denser core plus monophasic droplets with the neutral mucosubstance. In many surface epithelial cells of the foveolae, the biphasic and monophasic droplets with the neutral mucosubstance intermingled in varying proportions with monophasic droplets showing uniform periodate reactivity, a variable degree of dialyzed ironbinding—demonstrative of acidic glycoconjugate, and high iron—diamine affinity—demonstrative of sulphomucin. Deep foveolar epithelium displayed only monophasic droplets, most of which contained acidic periodate-reactive complex carbohydrate. Underiying cells, designated isthmus cells, exhibited monophasic or occasional biphasic granules containing sulphated, hexose-rich mucosubstance. Nascent droplets or granules near the Golgi zone differed from the mature organelles in the distribution of the glycoconjugate. Mucous neck cells occupied a deeper stratum and displayed a uniform population of monophasic mucous droplets with a loose meshwork of neutral mucosubstance. Techniques for demonstrating hexoses ultrastructurally stained all Golgi cisternae in the mucigenic epithelium, showing increasing reactivity toward the maturing face. Distinctive cistemae with moderate reactivity in the Golgi complex of isthmus cells were interpreted as GERL. Acidic mucosubstances were visualized only in the inner, mature cisternae of the Golgi complex of cells storing acidic glycoconjugates, and not in cisternae interpretable as GERL. The apical plasmalemma of isthmus cells uniquely exhibited abundant sulphated glycoconjugate and that of parietal cells revealed a less prominent, periodic neutral mucosubstance. Lateral and basal plasmalemmae varied from unstained to slightly reactive; basement membranes showed moderate reactivity with methods for visualizing complex carbohydrates. Abundance of glycogen further characterized surface epithelial cells of the corpus and of some parietal cells
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01007562
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  • 9
    Electronic Resource
    Electronic Resource
    Histochemical demonstration of sugar residues by lectin and immunocytochemical techniques for blood group antigens in human colon (1987)
    Springer
    Journal of molecular histology 19 (1987), S. 454-464 
    Details
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Goblet cell mucin in 39 human colons was studied by methods specific for various sugar residues, including staining with three lectins,Dolichos biflorus agglutinin (DBA, specific for blood group A antigen),Griffonia simplicifolia agglutinin-I (GSA-I, B) and peanut agglutinin (PNA, T antigen), and immunostaining for A, B, H and T. Isoantigens A, B or H were found only in the right colon. GSA-I reactive goblet cells occurred in the right colon of both blood group A and B patients and possibly contained isoantigens. However DBA reactive cells were found in all cases. Prior neuraminidase digestion imparted anti-A, GSA-I and DBA reactivities to the cells lining the lower crypts in all cases. This pretreatment also imparted PNA and anti-T reactivities to goblet cells, only the latter reactivity being eliminated by galactose oxidase. Goblet cell mucin in transitional mucosa revealed decreased A and B, and increased H antigens. Enhanced galactose oxidase—Schiff (GOS) and anti-T reactivities were also noted. The present results revealed that some lectin reactions of goblet cells might be related to blood group antigens but others were not, and that different techniques for demonstrating reputedly the same sugar residues produced different results, indicating a need for proper evaluation of their specificity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01675757
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  • 10
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    In vitro activity of arbekacin against clinical isolates of methicillin-resistant Staphylococcus aureus in a hospital. (1994)
    Springer Nature
    Details
    Publication Date: 1994-01-01
    Print ISSN: 0021-8820
    Electronic ISSN: 1881-1469
    Topics: Chemistry and Pharmacology , Medicine
    Published by Springer Nature
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