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  • Articles  (167)
  • Articles: DFG German National Licenses  (167)
  • Cell & Developmental Biology  (167)
  • Genetics
  • Wiley-Blackwell  (167)
  • Nature Publishing Group (NPG)
  • Springer Science + Business Media
  • 1995-1999  (167)
  • 1960-1964
  • Natural Sciences in General  (167)
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  • Articles  (167)
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  • Articles: DFG German National Licenses  (167)
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  • Wiley-Blackwell  (167)
  • Nature Publishing Group (NPG)
  • Springer Science + Business Media
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  • 1
    Electronic Resource
    Electronic Resource
    Quantitative immunocytochemical study of secretory protein expression in parotid glands of rats chronically treated with isoproterenol (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 106-117 
    Details
    ISSN: 1059-910X
    Keywords: Acinar cells ; Duct cells ; Differentiation ; Immunogold ; Amylase ; Proline-rich proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Chronic treatment of mice and rats with isoproterenol (IPR) causes marked hypertrophy and hyperplasia of the salivary glands, and alters the expression of several secretory proteins. We used quantitative postembedding immunogold labeling to study the cellular responses in the rat parotid gland during daily (up to 10 days) injections of IPR and during recovery (up to 14 days) after cessation of IPR treatment. Labeling densities of acinar cell secretory granules with antibodies to amylase and protein SMG-B1 (cross-reactive with the rat homologue of Parotid Secretory Protein, PSP) fell to 10% of control levels after 8-10 IPR injections, then increased during recovery, paralleling previous biochemical determinations of changes in protein and mRNA levels. With antibodies to proline-rich proteins (PRP), labeling densities initially fell, then subsequently showed considerable variability, but never exceeded control levels. These results contrast with biochemical determinations showing a marked induction of PRP synthesis, and may have both immunological and structural explanations.Occasional intercalated duct cells located close to the acini underwent differentiation toward an acinar-like phenotype as a result of IPR treatment. After 1-2 IPR injections, the secretory granules of these cells labeled with antibodies to amylase and PRP. Subsequently, the granules appeared electron-lucent and were increased in size and number. These observations support earlier work, suggesting that intercalated duct cells may differentiate into other gland cell types.
    Additional Material: 17 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310203
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical investigation of the in vivo endocytosis by renal tubular epithelial cells (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 118-127 
    Details
    ISSN: 1059-910X
    Keywords: In vivo ; Tubular epithelium ; Kidney ; Endocytosis ; Cationic albumin ; Immunocytochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: The internalization and degradation of glomerular filtered serum proteins by the proximal tubular epithelium has been extensively studied by microperfusion methods. By using a cationic probe that easily traverses the glomerular wall into the urinary space, we have performed a morpho-cytochemical and quantitative study of the in vivo endocytotic activity of the proximal tubular epithelial cell. Bovine serum albumin (BSA) was tagged with dinitrophenol (DNP) and cationized to pI over 8. It was introduced into the circulation of normal mice for 5, 10, and 30 minutes and the distribution of the labeling was determined by protein A-gold immunocytochemistry, using specific antiDNP antibodies on tissue sections of routinely aldehyde-fixed, osmiumpostfixed, and Epon-embedded kidneys. Cationic BSA-DNP was detected at the endothelial and epithelial sides of the glomerular basement membrane, and over capillary and tubular basement membranes. In the proximal tubular epithelial cell, labeling was present over microvilli as well as over endosomal and lysosomal compartments, with labeling intensities varying from one compartment to the other. Morphometric evaluations of the labeling demonstrated a progressive incorporation of the probe from microvilli and endocytic compartments at 5 minutes to endocytic and lysosomal compartments at 10 and then 30 minutes. When considering labeling densities, no significant differences were found on microvilli and basolateral membranes between times of circulation; however, the labeling density over endosomal and lysosomal compartments was very intense at 10 minutes compared with 5 minutes, decreasing at 30 minutes. Results from this study validate the cationic albumin tagged with DNP as a tool in the study of the quantitative aspects of protein endocytosis at the ultrastructural level, in the kidney tubular epithelium. © 1995 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310204
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  • 3
    Electronic Resource
    Electronic Resource
    Immunogold localization of actin in the testis and exocrine pancreas: Spatial relationship with tight junctional strands (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 128-140 
    Details
    ISSN: 1059-910X
    Keywords: Actin ; Phospholipids ; Tight junctions ; Pancreas ; Testis ; Immunocytochemistry ; Fracture-label ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: The fracture-label technique was used in conjunction with a monoclonal antibody to actin and the phospholipase A2-colloidal gold (PLA2-CG) method to examine the spatial distribution of actin filaments in relation to the three-dimensional arrangement of tight junctional strands in rat testes and exocrine pancreatic acinar cells. The intimate association of actin filaments with tight junctional strands in the pancreas and testis was also illustrated by a doublelabeling experiment in which freeze-fractured pancreas or testis was labeled with monoclonal antibody-protein A-gold (30 nm gold size) followed by incubation with a PLA2-CG complex (11 nm gold size). Freeze-fracture-exposed tight junctional strands in both testicular and exocrine pancreatic cells labeled by PLA2-CG complex indicated the presence of phospholipids in these cylindrical membranous structures. Immunolabeling of freeze-fractured testes with a monoclonal antibody to actin revealed a narrow band of gold particles juxtaposed to the cytoplasmic aspect of the protoplasmic membrane halves decorated with parallel linear arrays of cylindrical tight junctional strands. Many of the gold particles representing actin antigenic sites were in direct contact with the cross-fractured tight junctional strands. Fracture-label preparations of exocrine pancreas labeled with the monoclonal anti-actin antibody also exhibited a similar labeling pattern at the apex of acinars cells where the tight junction complex is located. Double-labeling experiments revealed the simultaneous labeling of actin and phospholipids in the same fracture-label preparations. Digestion of testicular and pancreatic tissue samples in a free PLA2 solution prior to labeling with the monoclonal antibody or PLA2-CG complex removed not only the gold labeling previously seen over the tight junctional strands but also reduced drastically the immunolabeling for actin that was previously seen associated with the tight junction complex. Taken together, results of the present study showed that actin filaments are structural components of the tight junction strands and are connected to the cytoplasmic aspect of the latter structures. The interaction between this particular cytoskeletal element and the tight junction may be through the binding of a special domain of the actin filament to the phospholipids that partially make up the tight junctional complex. © 1995 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310205
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  • 4
    Electronic Resource
    Electronic Resource
    Cellular functions during activation and damage by pathogens: Immunogold studies of the interaction of bacterial endotoxins with target cells (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 141-158 
    Details
    ISSN: 1059-910X
    Keywords: Immunocytochemistry ; Lipopolysaccharide ; Pneumocyte ; Macrophage ; Microtubules ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Bacterial endotoxins (lipopolysaccharides or LPS) are active components of Gramnegative bacteria that act on numerous cellular functions through the processes of cell activation and damage. The molecular mechanisms involved in the “endotoxic phenomenon” are not defined yet, although extensive studies have been carried out. Immunogold and electron microscopy (EM) have contributed to identify the primary target cells of endotoxins and the subcellular systems that receive the direct action of these bacterial agents. Here, we review our studies on immunogold detection of endotoxins in cellular and subcellular systems. The analysis of the interaction between endotoxins and cells was focussed on the following aspects: (1) morphological characteristics of the LPS aqueous suspensions used in experimental work; (2) binding of endotoxins to the plasma membrane of type II pneumocytes and alveolar macrophages (two of their cellular targets), and influence of the state of aggregation of the LPS; (3) movement and distribution of endotoxins inside the cell, from the plasma membrane to the nucleoplasm; and (4) interaction of LPS with microtubules and its effects on the integrity of the microtubular network. These approaches provide information at the molecular level as well as data for the establishment of physiological models of endotoxicity. © 1995 Wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310206
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  • 5
    Electronic Resource
    Electronic Resource
    Masthead (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995) 
    Details
    ISSN: 1059-910X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310301
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  • 6
    Electronic Resource
    Electronic Resource
    Immunogold labeling of oncogenic and tumor related proteins (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 159-173 
    Details
    ISSN: 1059-910X
    Keywords: Immunogold ; Electron microscopy (EM) ; Oncogene ; Mos ; Met ; Ski ; Muc1 ; Mucin ; Immunocytochemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Immunogold labeling electron microscopy technique has been used to study the ultrastructural localization of oncogenic proteins: Mos, Met, Ski, and the tumor-associated protein, Muc1, as well as their relationship with other tumor-related proteins. By pre- and postembedding immunogold labeling electron microscopy techniques, we showed that the Mos protein pp39mos colocalized with microtubule bundles, suggesting that microtubulin or microtubule-associated protein(s) may be the substrate of Mos. Met protein was labeled at the microvilli of the lumen that are formed in cultured T47D cells, implying its potential involvement in lumen formation. Ski localization experiments revealed a unique globular structure “Ski body” that is present inside the nucleus of interphase chicken embryo fibroblast infected with Ski cDNA FB29 and FB2-29. Ski bodies were also found scattered in the cytoplasm of metaphase FB29 and FB2-29 Ski expressing chicken embryo fibroblasts. In T47D cells, tumor-associated protein Muc1 was associated with both the plasma membrane and the membranes of secretory vesicles in the cytoplasm. In MUC1 infected NIH3T3 cells, however, labeling showed that in addition to the plasma membrane and the membranes of secretory vesicles, some Muc1 gold spheres were seen inside the secretory vesicles, suggesting that the subcellular localization of the protein may vary in different cell types. © 1995 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310207
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  • 7
    Electronic Resource
    Electronic Resource
    Introduction (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 183-183 
    Details
    ISSN: 1059-910X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310302
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  • 8
    Electronic Resource
    Electronic Resource
    Uranium-contaminated soils: Ultramicrotomy and electron beam analysis (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 174-181 
    Details
    ISSN: 1059-910X
    Keywords: Ultramicrotomy ; Transmission electron microscopy ; Uranium in soils ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Uranium-contaminated soils from the U.S. Department of Energy (DOE) Fernald Site, Ohio, have been examined by a combination of backscattered electron imaging (BSE) and analytical electron microscopy with electron diffraction (AEM). The inhomogeneous distribution of particulate uranium phases in the soil required the development of a method for using ultramicrotomy to prepare transmission electron microscopy (TEM) thin sections from the SEM mounts. A water-miscible resin was selected that allowed comparison between SEM and TEM images, permitting representative sampling of the soil. Uranium was found in iron oxides, silicates (soddyite), phosphates (autunites), and uraninite (UO2+x). No uranium was detected in association with phyllosilicates in the soil. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310208
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  • 9
    Electronic Resource
    Electronic Resource
    Morphological analysis of gastro-esophageal diseases by molecular cell techniques (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 184-192 
    Details
    ISSN: 1059-910X
    Keywords: DNA ; In situ hybridisation ; Monoclonal antibodies ; Protein ; RNA ; Western blots ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: The molecular cell sciences have had a great impact in the analysis of the genetic and epigenetic events of esophageal and gastric tumorigenesis. In other regions of the alimentary tract such as the colon, the serial identification of the molecular events in the corresponding morphological lesions is perhaps most advanced. This is, in part, due to the relative ease of the histological characterisation of the premalignant lesions. In this regard the analysis of morphological and molecular adaptation in the alimentary tract is inextricable. This review aims, therefore, to judiciously assess the relative applications of contemporary techniques in investigative histopathology. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310303
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  • 10
    Electronic Resource
    Electronic Resource
    Nucleic acid compartmentalization within the cell nucleus by in situ transferase-immunogold techniques (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 31 (1995), S. 4-21 
    Details
    ISSN: 1059-910X
    Keywords: DNA ; RNA ; Cell nucleus ; Immunogold techniques ; Nuclear organization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: In the present review, we report on recent results obtained by in situ transferaseimmunogold techniques as to the ultrastructural distribution of DNA and RNA within the cell nucleus. Special emphasis is placed on the various nucleolar components and the various enigmatic structures of the extranucleolar region: interchromatin granules, coiled bodies, and simple nuclear bodies. These data are discussed in the light of our current understanding of the functional organization of the cell nucleus. © 1995 Wiley-Liss, Inc.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070310103
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