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  • Electronic Resource  (4)
  • 1985-1989  (1)
  • 1970-1974  (3)
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  • Electronic Resource  (4)
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  • 1
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The rat substantia gelatinosa Rolandi (lamina II) was found to contain synaptic glomeruli at the centre of which was a dark terminal (C-terminal) full of round synaptic vesicles. The C-terminal was presynaptic to several dendritic profiles and to terminals containing sparse pleomorphic synaptic vesicles, and was occasionally postsynaptic at symmetrical contacts to other terminals containing numerous pleomorphic vesicles of which about one-third were elongated. Acid phosphatase activity was observed on, and between, the membranes of the synaptic vesicles of the central bouton, as well as in the hyaloplasm of the peripheral elements of the glomeruli. Dorsal root section caused electrondense degeneration of the central boutons. Acid phosphatase activity disappeared from synaptic vesicle membranes in C-boutons, and gradually filled their dense cytoplasmic matrix. The enzyme disappeared completely from the peripheral profiles. The synaptic glomeruli of the rat gelatinosa are thus a synaptic relay station for primary afferents, whose terminals possess an extralysosomal acid phosphatase possibly concerned with the metabolism of a local synaptic transmitter. Enzyme accumulation in degenerating knobs seems to be an autolytic process distinct from the normal function of this acid phosphatase.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using serial section EM analysis, synaptic organization of glomeruli in lamina II of the dorsal horn of the rat has been examined. Four CI-terminals (small, dark and sinuous), four CIIa (large, light and regular, without neurofilaments) and four CIIb, (with neurofilaments) at the centres of synaptic glomeruli of types I, IIa and IIb, respectively, were serially sectioned and reconstructed. Asymmetrical synapses between the central terminal (C) and dendritic profiles without synaptic vesicles (D) prevailed in all types of glomeruli. Symmetrical dendroaxonic contacts with presynaptic dendrites (V1 → C) occurred practically only in type I glomeruli in which there were also more asymmetrical C → V1 contacts than in type II glomeruli. Symmetrical axoaxonic synapses V2 → C were more abundant in type IIa and IIb glomeruli. Type IIa glomeruli had a significantly larger number of C → D synapses and of all synapses per unit area of C surface, than type IIb glomeruli. Triadic systems with C and D postsynaptic to V2 were nearly as numerous as those involving V1 in type I glomeruli. Triads with V2 were however largely preponderant in type IIa and virtually exclusive in type IIb. It thus seems that each of the three types of glomerulus has its own pattern of synaptic interactions which might reflect specific complexes of feed-forward and feed-back mechanisms. In type I glomeruli, excitation of second-order neurons by nociceptive CI terminals may be controlled in similar proportions by presynaptic dendrites excited within the glomerulus by the C terminal itself, or by peripheral axons excited from outside the glomerulus. This kind of control is likely to prevail in type IIa glomeruli and to be the only efficient modulatory mechanism in type IIb glomeruli.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Synopsis Four acid hydrolases in the secretory cells and the sebum of the preputial sebaceous gland of the rat were incestigated cytochemically. A strong β-glucuronidase activity was found to occur in the matrix of the perinuclear secretion granules, whereas the granule crystalloids were unreactive. The distribution of acid phosphatase at the light microscope level was similar, though the intensity of the reaction was lower and the number of positive granules smaller. By electron microscopy, the final reaction product of acid phosphatase occurred in patches at the periphery of the granule matrix, as well as in the vesicles adjoining the Golgi stacks, from which the perinuclear granules seemed to arise. In the sebum, the two hydrolases occurred in the background material between the unstained crystalloid masses. There was noN-acetyl-β-glucosaminidase or aryl sulphatase activity in the gland. The perinuclear granules appear to be secretory lysosomes which, after discharge from the disaggregating cell, release their acid hydrolases into the sebum.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 132 (1971), S. 109-117 
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Young rats received 1 mCi of leucine-H3 or tyrosine-H3 intraperitoneally and adrenals were fixed in glutaraldehyde-osmium after 10, 60 and 240 minutes. Epon ultrathin sections were coated with Ilford L4 nuclear emulsion for radioautography. Ten minutes after injection of both tritiated amino acids, labeling indicating the sites of protein synthesis was found principally over the endoplasmic reticulum (∼ 57% of the silver grains) and mitochondria (∼ 32%). Distances of silver grain centers to the nearest interface between these two organelles were plotted; the results seemed to confirm that protein synthesis occurred in the endoplasmic reticulum and mitochondria but was more active in the endoplasmic reticulum. Values remained the same at the other time intervals examined, suggesting the formation of sedentary protein. However, values for the Golgi apparatus were low at ten minutes, fairly high at 60 minutes and low again at 240 minutes, suggesting migration of a small fraction of the newly-formed protein through the Golgi apparatus and subsequent discharge. The possibility is raised of this being an exportable protein.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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