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  • 1
    Electronic Resource
    Electronic Resource
    Ultrastructural cytochemistry of the human adrenal medulla (1977)
    Springer
    Histochemistry and cell biology 54 (1977), S. 9-26 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A cytochemical study of the human adrenal medulla showed that it is made up of two cell types, the adrenaline (A-) and noradrenaline (N-) storing cells. A- and N-storing granules were argentaphobic when ultrathin sections of Araldite-embedded medullae were stained according to the periodic acid-thiocarbohydrazide silver proteinate technique of Thiery. A small amount of glycogen (which disappeared after digestion with alpha amylase) in the form of B-particles, as well as lysosomes were, however, visualized by this technique. The entire core of A granules was markedly positive after ultrathin sections of glutaraldehyde-fixed, glycol methacrylate-(GMA-) embedded medullae were stained with phosphotungstic acid (PTA) at a low pH (0.3). The N granules, in contrast, were mostly unreactive. PTA stained a large part of the Golgi complex of A cells, whereas it generally had no such effect on that of the N cells. In both cell types, the cell coat, lysosomes and multivesicular bodies reacted to PTA. The periodic acid —schiff (PAS) technique showed A but not N granules in semithin sections of GMA- or Araldite-embedded medullae. The PTA and PAS stains were abolished by acetylation, restored by saponification, unchanged by methylation and greatly diminished by sulfation or by digestion with beta glucuronidase after oxidation by perchloric acid. These results indicate that in man the A granules and the Golgi complex of A cells, unlike the same structures in N cells, are rich in glycoproteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493325
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  • 2
    Electronic Resource
    Electronic Resource
    Ultrastructural radioautography of synthesis and migration of proteins and catecholamines in the rat adrenal medulla (1982)
    Springer
    Cell & tissue research 225 (1982), S. 293-314 
    Details
    ISSN: 1432-0878
    Keywords: Ultrastructural radioautography ; Protein and catecholamine synthesis ; Adrenal medulla
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The synthetic pathways of proteins and catecholamines in the rat adrenal medullary cells were compared systematically at the ultrastructural level, within a 24 h period, with 2 tracers, L-tyrosine 3,5-3H and L-3,4-dihydroxy [ring 2,5,6-3H] phenylalanine (L-dopa3H). Young rats were injected with either of these tracers and sacrificed in pairs at close time intervals. With L-tyrosine 3H, the label was about equal over rough endoplasmic reticulum (RER) and secretory granules at 2 min after injection and remained almost constant in intensity over the secretory granules throughout the period of observation. A peak of radioactivity was also observed in the Golgi complex between 5 and 20 min after injection. This indicates that L-tyrosine 3H participates in the synthesis of both granule proteins and catecholamines as confirmed by the results obtained after injection of L-dopa 3H. With this tracer, radioactivity over RER, Golgi complex, cytosol and cell surface remained very low at all times and was undetectable at several time intervals. In contrast, radioactivity over secretory granules was very high at all time intervals. The present results thus confirm that in both adrenaline- and noradrenaline-storing cells, the protein moiety of chromaffin granules is synthetized in the RER, packaged in the Golgi complex and rapidly found in newly formed secretory granules. Following either L-tyrosine 3H or L-dopa 3H injection, catecholamine synthesis occurs only in or in close vicinity to chromaffin granules in both cell types at all time intervals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214683
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  • 3
    Electronic Resource
    Electronic Resource
    Ultrastructural radioautography of the incorporation of tritiated leucine by the rat adrenal medulla in vivo (1978)
    Springer
    Cell & tissue research 193 (1978), S. 179-199 
    Details
    ISSN: 1432-0878
    Keywords: Adrenal medulla ; Protein synthesis ; Ultrastructural radioautography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sections of tissues from the adrenal medullae of young rats were subjected to radioautography after a single intravenous injection of L-leucine 4,5 3H to identify the sites of synthesis and follow the migration of newly-formed proteins in both adrenaline-storing (A) and noradrenaline-storing (N) cells. As early as 2 min after injection of leucine 3H, the label was highest in the rough endoplasmic reticulum (RER) of A and N cells, suggesting that cisternal ribosomes are sites of protein synthesis. By 5 and 10 min, much of the label had migrated from the RER into the Golgi complex of both cell types. Some label was already present over the secretory granule matrix (chromogranins) by 2 min but the peak was reached at 1 h in both A and N cells. By 4 h, the label over the secretory granules had diminished, indicating a release of newly-synthetized chromogranins outside the cells. The label over the hyaloplasm was relatively high at 2 min but it decreased rapidly to low levels. In contrast, the label over the cell surface continually increased to reach the highest levels among all organelles at 4 h in both cell types. The pattern of increment of the label over the cell surface suggests that the newly-formed proteins of these sites are also synthetized in the RER, pass through the Golgi complex and are transported in the hyaloplasm, before reaching the surface of A and N cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00209033
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  • 4
    Electronic Resource
    Electronic Resource
    Synthesis and migration of proteins and glycoproteins in juxtaglomerular cells of sodium-deficient rats (1982)
    Springer
    Cell & tissue research 222 (1982), S. 53-67 
    Details
    ISSN: 1432-0878
    Keywords: Protein and glycoprotein synthesis ; Juxtaglomerular cells ; Kidney
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Sections of juxtaglomerular cells from sodium-deficient rats were subjected to radioautography after a single intravenous injection of L-tyrosine3,5 3H or of L-fucose 3H to identify the sites of synthesis and to follow the migration of newly-formed proteins and glycoproteins. As early as 2 min after injection of L-tyrosine 3H, the label was highest in the rough endoplasmic reticulum (RER), suggesting that cisternal ribosomes are sites of protein synthesis. By 60 min, much of the label had migrated from the RER to the Golgi complex. Some radioactivity was already present over specific granules by 2 min but a peak was reached at 4h. The label over myofilaments was evident at all time intervals, indicating a certain incorporation of tyrosine into their contractile and/or structural proteins. The label over the cell surface peaked at 4h. After injection of L-fucose 3H, there was an early and important relative specific radioactivity in the Golgi complex at 5 min with a peak at 20 min and a decrease thereafter. The label increased slightly but steadily in secretory granules and cell surface to reach maxima at 4 h. A low level of radioactivity was recorded in mitochondria at all time intervals. After injection of both fucose 3H and tyrosine 3H, the label was detected at relatively low levels in the cytosol. These results suggest that renin, as the major secretory glycoprotein of juxtaglomerular cells, is synthetized in the RER, packaged in the Golgi complex and found relatively rapidly in newly-formed secretory granules. Part of the fucose and tyrosine labels is also associated with the thick cell coat of these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00218288
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