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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 152 (1978), S. 243-259 
    ISSN: 1432-0568
    Keywords: Oviduct epithelium ; Fine structure ; Cytodifferentiation ; Ciliogenesis ; Aging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The fine structure of the oviduct epithelium of the newborn to the old mouse was studied with an electron microscope. Just after birth, epithelial cells lining the ampulla of the mouse oviduct are simple columnar in shape and of one type in fine structure. They contain numerous free ribosomes, an extremely poor rough endoplasmic reticulum, and a small Golgi complex. In the 3-day-old mouse, the epithelial cells are differentiated neither into ciliated nor secretory cells, and are characterized by the appearance of many autolysosomes and a solitary cilium. The ciliary cells differentiates 5 days after birth. Ciliogenesis is frequently observed at 5–10 days. The important role of the fibrous granules for ciliogenesis and that of the Golgi apparatus for membranogenesis of the cilia are described and discussed. The secretory cell having mucous secretory materials is differentiated at 23 days. In the epithelial cell lining the ampulla of the aged (22 to 24-month-old) mouse oviduct, large autolysosomes and vacuoles 2–6 μm in diameter occur in the ciliated cell, though cilia and other cell organelles are well preserved. In the old mouse the secretory granules almost disappear and the rough endoplasmic reticulum is strikingly dilated in the secretory cell. No features showing the transformation between the secretory cell and the ciliary one are seen in the mouse oviduct.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 107 (1970), S. 104-110 
    ISSN: 1432-0878
    Keywords: Thyroid ; Peroxidase ; Localization ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structural localization of a peroxidase activity in the rat thyroid follicular epithelial cell was studied by histochemistry at electron microscopic level. The reaction product is recognized chiefly in the cisternae of the elements of granular endoplasmic reticulum and of nuclear envelope. Golgi vesicles or apical small vesicles, mitochondria, and dense granules are sometimes positive for this reaction. The relationship between the fine structural localization of peroxidase and the site of the iodination of thyroglobulin is discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 121 (1971), S. 301-318 
    ISSN: 1432-0878
    Keywords: Thyroid ; Bats ; Hibernation ; Influence of TSH ; Arousal
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine structure of thyroids of hibernating and aroused bats, Myotis lucifugus, was observed with the electron microscope. (1) In the hibernating bat for 5 months the thyroid follicular epithelial cell is markedly attenuated and the rough endoplasmic reticulum and Golgi apparatus are very poor in development, while the mitochondria are larger and distributed throughout the cytoplasma. Intracellular colloid droplets are difficult to find. Homogeneously dense small granules suggesting primary lysosomes are numerous. Half an hour to 2 hours after injection of 100 μc of 125I, very few silver grains are recognized in a follicle lumen electron microscopic autoradiographically. (2) Half an hour to 2 hours after the intraperitoneal injection of 1 unit of thyroid stimulating hormone (TSH) into hibernating bats, several colloid droplets, many small smooth-surfaced vesicles and a few coated vesicles appear in the apical cytoplasm of the thyroid follicle epithelial cell. The small vesicles are gathered around the large droplet, and some of them are fused with it. The rough endoplasmic reticulum does not show any marked reaction. These facts suggest the possibility that the luminal colloid is reabsorbed in the form of large droplets as well as in the form of small vesicles. Dense granules (lysosomes) gathered near the colloid droplets and some of the colloid droplets themselves become heterogeneously dense. Half an hour to 2 hours after injection of 100 μc of 125I simultaneously with TSH into hibernating bats, silver grains which are markedly increased in number, as compared with those of the non-treated hibernating animal, are recognized in the follicle lumen electron microscopic autoradiographically. (3) At 2–3 hours after injection of TSH into the hibernating bat, the appearance of crystals in over half of the colloid droplets is characteristic. Each crystal consists of aggregates of numerous needle-like filaments, about 65 Å in diameter, running parallel with one another. Center to center distances between these filaments cut in longitudinal section are about 150 Å. The filaments are arranged regularly along two or three axes. These crystals are considered to be altered thyroglobulin. (4) The follicular epithelial cells of aroused bats (24° C, laboratory room in winter) from the hibernation show heterogeneity in their fine structure. Some cells seem active, and the others look inactive. In 15-day aroused bats, though most cells are flattened and the rough endoplasmic reticulum is sparse, a few cells show a fairly well developed rough endoplasmic reticulum with somewhat dilated cisternae. Large colloid droplets occur sometimes in a few cells. Lysosomal dense granules, reduced in number as compared with those of hibernating animals, are considered to originate from the Golgi apparatus. In 30 and 40-day aroused bats, the rough endoplasmic reticulum of most cells becomes more enlarged, and some follicular cells are quite similar to those of non-hibernating bats obtained in the field. In 60-day aroused bats, all the follicular epithelial cells show quite the same feature as the active thyroid cell of non-hibernating mammals.
    Type of Medium: Electronic Resource
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