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  • 1
    Electronic Resource
    Electronic Resource
    Cyclic AMP-Dependent Protein Kinase Compartmentalization in Stimulated Exocrine Cells (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 494 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb29503.x
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  • 2
    Electronic Resource
    Electronic Resource
    A contractile nuclear actin network drives chromosome congression in oocytes (2005)
    [s.l.] : Nature Publishing Group
    Nature 436 (2005), S. 812-818 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Chromosome capture by microtubules is widely accepted as the universal mechanism of spindle assembly in dividing cells. However, the observed length of spindle microtubules and computer simulations of spindle assembly predict that chromosome capture is efficient in small cells, but may fail in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature03810
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  • 3
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of L-α-hydroxy acid oxidase in rat liver peroxisomes (1975)
    Springer
    Histochemistry and cell biology 41 (1975), S. 195-206 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of L-α-hydroxy acid oxidase activity in rat liver peroxisomes was studied using slight modifications of the Shnitka and Talibi (1971) method. Best results were obtained with formaldehyde fixation and incubation with glycolate as substrate. Following incubation the copper ferrocyanide reaction product was amplified with 3,3′-diaminobenzidine according to Hanker et al. (1972a, b). Dense reaction product was visible in hepatocyte peroxisomes by light and electron microscopy. Some diffusion of enzyme and/or reaction product into the adjacent cytoplasm occurred around the peroxisomes. Apparent non-specific deposits occurred on the plasmalemma, in the nucleus, and occasionally over mitochondria. Glutaraldehyde fixation severely inhibited enzymatic activity, and the enzyme showed less activity toward L-lactate and DL-α-hydroxybutyrate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00497683
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrastructural and cytochemical studies of acid phosphatase and trimetaphosphatase in rat peritoneal mast cells developing in vivo (1986)
    Springer
    Cell & tissue research 244 (1986), S. 557-563 
    Details
    ISSN: 1432-0878
    Keywords: Mast cell maturation ; Mast cell granules ; Acid hydrolases ; Lysosomes ; Golgi apparatus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ultrastructural and cytochemical features of peritoneal mast cells of the rat were studied. Immature mast cells show specific cytoplasmic granules of different sizes, the smaller ones localized in the Golgi region. The rough endoplasmic reticulum and Golgi apparatus are well developed, and mitochondria are numerous. Nuclei show deep indentations. Acid phosphatase is present in the Golgi saccules, in GERL (Golgi apparatus-endoplasmic reticulumlysosome) and in some small granules. It is not present in mature granules. Trimetaphosphatase is present in the Golgi saccules, in GERL, in most immature granules and in some mature granules. These enzymes appear to be transported and packaged into granules by the Golgi apparatus, suggesting that the specific mast cell granules may be a form of lysosome. The results of this study are consistent with the hypothesis that peritoneal mast cells may be derived from macrophage-like precursors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00212533
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  • 5
    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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  • 6
    Electronic Resource
    Electronic Resource
    Endocytosis of native and cationized ferritin by intralobular duct cells of the rat parotid gland (1987)
    Springer
    Cell & tissue research 249 (1987), S. 577-586 
    Details
    ISSN: 1432-0878
    Keywords: Parotid gland ; Duct cells ; Ferritin ; Endocytosis ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The ability of the intralobular ducts of the rat parotid gland to take up protein from the lumen was examined after retrograde infusion of native and cationized ferritin. At high concentrations (3–10 mg/ml), cells of both intercalated- and striated ducts avidly internalized the tracers. No differences were noted in the mode of uptake or fate of native or cationized ferritin. Large, apical ferritin-containing vacuoles up to 5 μm in size were present in cells of the intercalated ducts after infusion for 15 min. Small, smooth-surfaced spherical or flattened vesicles and tubules containing ferritin were also observed, often in association with the large vacuoles. Ferritin uptake increased with increasing infusion time, up to 1 h. Uptake by the striated ducts was less consistent than by the intercalated ducts, and occurred mainly in small vesicles and tubules. Secondary lysosomes became labeled with ferritin in both cell types. Ferritin was not observed in the Golgi saccules, nor was it discharged from the cells at the basolateral surfaces. At low concentrations (0.3–1 mg/ml), uptake was reduced, especially by cells of intercalated ducts, and differences were noted in the behavior of the two tracers. Cationized ferritin was internalized mainly into vesicles and tubules of cells of striated ducts; little uptake of native ferritin occurred at low concentrations. These results demonstrate that the ductal cells of the salivary glands are capable of luminal endocytosis of foreign proteins. They also suggest that in addition to modifying the primary saliva by electrolyte reabsorption and secretion, and secretion of various glycoproteins, the ductal cells are able to reabsorb proteins secreted by the acinar cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00217329
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  • 7
    Electronic Resource
    Electronic Resource
    Adrenergic and cholinergic nerve terminals in the rat parotid gland. Electron microscopic observations on permanganate-fixed glands (1972)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 173 (1972), S. 131-139 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The innervation of the acinar cells of the rat parotid gland was studied using potassium permanganate fixation. Adrenergic terminals, characterized by the presence of small granular vesicles, and cholinergic terminals, containing small agranular vesicles, made close contact with the acinar cells. Both adrenergic and cholinergic terminals were observed in contact with the same cell, and subsurface cisterns of endoplasmic reticulum were found in relation to the contact areas of both types of endings. In addition, both adrenergic and cholinergic axons were found within the same Schwann cell sheath in the connective tissue spaces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091730202
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  • 8
    Electronic Resource
    Electronic Resource
    Synthesis of secretory and plasma membrane glycoproteins by striated duct cellsof rat salivary glands as visualized by radioautography after 3H-fucose injection (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 195 (1979), S. 317-339 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The ability of the striated ducts of rat salivary glands to incorporate 3H-fucose into glycoprotein was studied by light and electron microscope radioautography. At 3.5 to 20 minutes after intravenous injection, the majority of the radioautographic grains in the ducts of the parotid gland were localized to the Golgi apparatus. By 40 minutes, the percentage of grains over the Golgi apparatus had decreased; a corresponding increase in grains occurred over small (0.1-0.4 μm) apical granules and the highly infolded basal and lateral plasma membranes. By two hours, less than 10% of the label was associated with the Golgi apparatus, while 26% and 28% were attributed to the apical granules and plasma membrane, respectively. By 8 to 12 hours after injection, the number of grains over the apical cytoplasm had decreased, suggesting luminal discharge of the apical granules. In contrast, the basal and lateral plasma membranes remained labeled up to 30 hours after injection as judged by the distribution of grains in light microscope radioautographs. Mitochondria appeared capable of independent incorporation of fucose, accounting for about 20% of the grains from ten minutes to two hours after injection. Comparable results were obtained in the striated ducts of the submandibular and sublingual glands.These results indicate that the striated duct cells readily incorporate 3H-fucose into newly-synthesized glycoproteins. A portion of these are secretory glycoproteins which are packaged and stored in the apical granules, and a portion are membrane glycoproteins which are incorporated into the extensive plasma membrane of these cells.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091950207
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  • 9
    Electronic Resource
    Electronic Resource
    Differential distribution of salivary agglutinin and amylase in the Golgi apparatus and secretory granules of human salivary gland acinar cells (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 230 (1991), S. 307-318 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The secretory granules of salivary glands often display complex internal substructures, yet little is known of the molecular organization of their contents or the mechanisms involved in packaging of the secretory proteins. We used post-embedding immunogold labeling with antibodies to two secretory proteins, agglutinin and α-amylase, to determine their distribution in the Golgi apparatus and secretory granules of the human submandibular gland acinar cells. With monoclonal antibodies specific for carbohydrate epitopes of the agglutinin, reactivity was found in the trans Golgi saccules, trans Golgi network, and immature and mature secretory granules. In the granules, labeling was seen in regions of low and medium electron density, but not in the dense cores. Reactivity seen on the apical and basolateral membranes of acinar and duct cells was attributed to a shared epitope on a membrane glycoprotein. Labeling with a polyclonal antibody to amylase was found in the Golgi saccules, immature and mature secretory granules, but not in the trans Golgi network. In the granules, amylase was present in the dense cores and in areas of medium density, but not in the regions of low density. These results indicate that these two proteins are distributed differently within the secretory granules, and suggest that they follow separate pathways between the Golgi apparatus and forming secretory granules. Small vesicles and tubular structures that labeled only with the antibodies to the agglutinin were observed on both faces of the Golgi apparatus and in the vicinity of the cell membrane. These structures may represent constitutive secretion vesicles involved in transport of the putative membrane glycoprotein to the cell membrane.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092300303
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  • 10
    Electronic Resource
    Electronic Resource
    Intracristal helices in salivary gland mitochondria (1970)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 168 (1970), S. 565-568 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Helical filaments have been found within dilated intracristal spaces of normal rat salivary gland mitochondria. Filament diameter measured 35-45 Å, and the helix diameter and pitch were 140-155 Å. They were found in as many as 25% of the mitochondria of acinar and intercalated duct cells. Helices were not found in mitochondria of the striated duct cells.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1091680408
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