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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 513 (1987), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 256 (1989), S. 573-580 
    ISSN: 1432-0878
    Keywords: Epididymis ; Epithelium ; Monolayer culture ; Histochemistry ; Electron microscopy ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary N-acetylglucosaminidase (NAG), acid phosphatase (ACP) and alkaline phosphatase (AKP) were localised histochemically in fixed cells from the 37-day-old rat epididymis grown in static monolayer culture for 2–8 days. ACP and NAG were cytosolic enzymes found in perinuclear positions, whereas staining of AKP was consistent with a membranous position. These enzymes were also examined in frozen tissue sections of the epididymis, from rats of the equivalent age, where NAG had intense activity in both supra- and infra-nuclear cytoplasm and ACP was more active apically. For the first time AKP was localised along basolateral membranes of the epithelium and in the lumen of the mid-caput region. The monolayer in culture was of principal cells only and they maintained their polarity and ultrastructural characteristics, but the height of the cells was reduced compared to that obtained in situ.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 253 (1988), S. 631-637 
    ISSN: 1432-0878
    Keywords: Epididymal ultrastructure ; Transcytosis ; Protein transport ; Fluid-phase endocytosis ; Epididymal arterial perfusion ; Rat (Sprague-Dawley) ; Golden hamster ; Mouse (CB6/F1)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The transport of protein across the cells of the epididymal epithelium was studied using horseradish peroxidase. Transient vascular perfusion of the epididymis of the rat and golden hamster was achieved by pulsatile retrograde infusion into the testicular artery. Peroxidase was found in the interstitium and in the epithelium, located in vesicles, vacuoles and multivesicular bodies of principal, clear and apical cells. Similar findings were obtained in mice after systemic injection of the tracer. In the rat, discharge to the lumen was confirmed by the appearance of enzyme activity in luminal fluid from the caput epididymidis after local injection. The extent of transport amounted to no more than what has been considered leakage in physiological experiments, and the time-course of appearance complemented that found by electron microscopy. The level of transcytosis after pulsatile administration of peroxidase in vivo, as judged from the occurrence of tracer in the epithelium, was much less than that obtained during constant immersion in vitro. The protein was present in multivesicular bodies of principal cells and in vesicles of clear cells at short times after presentation in vitro, when it could not have arrived by endocytosis from the lumen. This suggests that routing of basal endocytic vesicles to the lysosomal apparatus occurs.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 248 (1987), S. 527-530 
    ISSN: 1432-0878
    Keywords: Epididymal ultrastructure ; Peroxidase ; Protein transport ; Fluid-phase endocytosis ; Sprague-Dawley rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Experiments were performed to clarify the debate over the entry of circulating proteins into the epididymal lumen by use of the marker horseradish peroxidase (HRP). Epididymal tubules from the caput epididymidis of the rat were immersed in medium TC 199 containing HRP (3.5 mg/ ml) for 5 min to 3 h at 33° C. Sections were examined for the presence of tracer within the epithelial cells by electron microscopy. From 5 min to 3 h, vesicles containing peroxidase reaction products were found throughout the cytoplasm of the principal cells. Vesicles occurred close to both the basal and apical membranes, and many were found opening into the interstitial space and lumen, depending on the length of incubation. By 5 min labelled vesicles were infrequently found in the apical part of the cells. Reaction product was observed in the epididymal lumen adhering to the microvilli from 30 min of incubation onwards. At all periods of incubation peroxidase was present at the base of the epithelium and between the cells, but it was never found within the tight junctional complexes, and no reaction deposits were found within epithelial cells of tubules incubated in the absence of peroxidase. It is concluded that large molecules leaving the capillaries may enter the epididymal lumen in the caput by means of fluid-phase endocytosis.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 256 (1989), S. 567-572 
    ISSN: 1432-0878
    Keywords: Epididymis ; Monolayer culture ; Directed secretion ; Phosphatases ; Glucosaminidase ; Rat (Sprague-Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A cell culture system is characterised for monolayers of immature rat epididymal epithelial cells grown on permeable supports. Cover of the filters was achieved by days 4–5 and was maintained for 9–12 days. The secretion of acid phosphatase (ACP), alkaline phosphatase (AKP) and N-acetylglucosaminidase (NAG) into apical and basal compartments of culture chambers was monitored with time in culture for cells from the proximal and distal epididymis of 37-day-old animals. There was independent secretion of the three enzymes: secretion of NAG and AKP was mainly apical, that of ACP basal; daily secretion of ACP and AKP was constant throughout culture, that of NAG declined; there was greater secretion of NAG and AKP by cells from the proximal than the distal region. The initial high apical secretion of NAG is thought to reflect loss of enzyme from unattached cells, whereas the later AKP secretion is truly directional. Secretion was not influenced by the enzymes used in cell preparation. The cytotoxic agent Thimerosal inhibited secretion of all enzymes when placed beneath the cultures, indicating that secretion depended on viable cells, but initially stimulated release of AKP when applied above the cells possibly reflecting release from the cell membrane.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 14 (1986), S. 47-56 
    ISSN: 0148-7280
    Keywords: rat sperm ; osmotic swelling ; sperm maturation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The form that rat spermatozoa assume when swelling in hyposmotic media depends on the position of the cytoplasmic droplet, previous exposure to hypertonic media, and the stiffness of the flagellum. Bending at the end of the midpiece occurs when the swelling droplet is situated at this site; this occurs in midcaput cells, but sperm from more proximal sites do not bend in this fashion. Stiffening of caput sperm stored in vitro reduces the incidence of such midpiece bending but looping at the tip of the tail still occurs, and previous exposure of caput spermatozoa to hypertonic media also prevents hairpin bend formation. Mature sperm from the cauda are too stiff to form hairpin loops when placed in hypotonic media unless first treated with a penetrating disulphydryl-reducing agent, after which swollen spherical vesicles can result from very flexible flagella confined within an intact membrane. Long-chain acylcarnitines are more potent lytic agents than acylcholines, but, for both, chain lengths of 16 carbon atoms is optimal for preventing the swelling of rat caput sperm.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0148-7280
    Keywords: galactosyltransferase ; capacitation ; epididymis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of bovine mammary alpha-lactalbumin on the motility and zona-binding characteristics of mouse sperm were investigated. Two properties of sperm associated with capacitation, hyperactivated motility, and the ability of sperm to bind to the zona pellucida of oocytes were shown to be suppressed by alpha-lactalbumin. These inhibitory effects were not accompanied by changes in the percentage of motile cells or by differences in the velocity parameters of the hyperactivated and non-hyperactivated spermatozoa. Bovine serum albumin prevented and reversed the alpha-lactalbumin-induced suppression of hyperactivation. Sperm-zona pellucida binding was partially restored by lowering the alpha-lactalbumin concentration in the medium in which sperm were allowed to bind to the zona pellucida. The results suggest that mouse sperm are decapacitated by bovine mammary alpha-lactalbumin. The counteracting effect of bovine serum albumin to the suppressive action of alpha-lactalbumin on the flagellum suggests the involvement of a mechanism different from the action of alpha-lactalbumin on the sperm head inhibiting binding to the zona pellucida.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Publication Date: 2005-04-06
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 9
    Publication Date: 1987-06-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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  • 10
    Publication Date: 1985-02-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
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