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  • 1
    ISSN: 1432-0568
    Keywords: Ultrastructure ; Human knee joint capsule ; Free nerve endings ; Ruffini corpuscles ; Pacini corpuscles
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ultrastructure of sensory nerve endings in the human knee joint capsule was studied. Three types of nerve endings were found: free nerve endings (FNE), Ruffini corpuscles and Pacini corpuscles. In the joint capsule, FNE are located below the synovial layer and within the fibrous layer near blood vessels. These nerve terminals derive from myelinated Aδ-fibres or from unmyelinated C-fibres. Their structure is almost identical to FNE in human hairy and non-hairy skin. Ruffini corpuscles are present within the fibrous layer and the ligaments of the capsule in three variations: small Ruffini corpuscles without a capsule, small with a connective tissue capsule, and large Ruffini corpuscles with an incomplete perineural capsule. Their afferent axons are myelinated and measure 3–5 μm in diameter. Inside the corpuscle, nerve terminals are anchored in the connective tissue belonging to the fibrous layer or to the ligaments respectively. The presence of an incomplete perineural capsule depends on the structure of the surrounding connective tissue. In ligaments with collagenous fibrils oriented in a parallel fashion, the perineural capsule is well-developed and the Ruffini corpuscle resembles a Golgi tendon organ; in areas where the fibrils show no predominant orientation, Ruffini corpuscles lack a capsule. Small Pacini corpuscles are situated within the fibrous layer near the capsular insertion at the meniscus articularis or at the periost. They consist of one or several inner cores and a perineural capsule of 1–2 layers. Larger Pacini corpuscles with one or several inner cores and a perineural capsule consisting of 20–30 layers are found on the outer surface of the fibrous layer. The ultrastructure of these nerve endings is compared with the ultrastructure of articular receptors of various animals and with the ultrastructure of sensory nerve endings in the skin of several mammalian species including man.
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  • 2
    ISSN: 1612-4766
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Description / Table of Contents: Summary Studies on controlling the nun moth, Lymantria monacha L., by help of Disparlure, a synthetic pheromone In a pine forest near Schwabach/Franconia trials were run to control the nun moth, Lymantria monacha, by trapping males with “Disparlure”, cis-7,8-epoxy-2-methyl-octadecane. Satisfactory results were achieved using sticky plates hanging vertically and double cone traps of adequate size with dichlorvos as a killing agent. Reaction was most intense at the beginning of the flight period. Catch size of neighbouring traps often differed constantly. Thus the range of attractancy that may be of practical value for control purposes is assumed to be about 50 metres.
    Notes: Zusammenfassung In einem Kiefernforst im Kreis Schwabach/Franken wurden Versuche zur Bekämpfung der Nonne, Lymantria monacha durch Anlockung der Männchen mit „Disparlure”, cis-7,8-Epoxy-2-methyl-octadecan, angelegt. Befriedigende Wirkungen erreichten vertikale Leimtafeln und — nur bei hinreichender Größe — horizontale Doppeltrichterfallen mit Dichlorvos als Abtötungsmittel. Der stärkste Anflug erfolgte zu Beginn der Flugperiode. Konstante große Unterschiede im Fangergebnis benachbarter Fallen machen es wahrscheinlich, daß die für Bekämpfungszwecke verwertbare Reichweite etwa im Bereich um 50 m liegt.
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  • 3
    ISSN: 1573-4919
    Keywords: membrane ATPases ; cytochemistry ; myocardium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract ATPases of cardiac cells are known to be among the most important enzymes to maintain the fluxes of vital cations by hydrolysis of the terminal high-energy phosphate of ATP. Biochemically the activities of Ca2+-pump ATPase, Ca2+/Mg2+-ecto ATPase, Na+,K+-ATPase and Mg2+-ATPase are determined in homogenates and isolated membranes as well as in myofibrillar and mitochondrial fractions of various purities. Such techniques permit estimation of enzyme activitiesin vitro under optimal conditions without precise enzyme topography. On the other hand, cytochemical methods demonstrate enzyme activityin situ, but not under optimal conditions. Until recently several cytochemical methods have been employed for each enzyme in order to protect its specific activity and precise localization but the results are difficult to interpret. To obtain more consistent data from biochemical and cytochemical point of view, we modified cytochemical methods in which unified conditions for each ATPase were used. The fixative solution (1% paraformaldehyde −0.2% glutaraldehyde in 0.1 M Tris Base buffer, pH 7.4), the same cationic concentrations of basic components in the incubation medium (0.1 M Tris Base, 2mM Pb(NO2)3, 5 mM MgSO4, 5 mM ATP) and selective stimulators or inhibitors were employed. The results reveal improved localization of Ca2+-pump ATPase, Na+−K+ ATPase and Ca2+/Mg2+-ecto ATPase in the cardiac membrane.
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  • 4
    ISSN: 1573-4919
    Keywords: adenylyl cyclase ; muscarinic receptors ; G-proteins ; immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The localization of three key signal transduction components was indicated in rat heart tissue by immunocytochemical and histochemical experiment. It was shown that: 1. The M2 muscarinic receptors are localized along outer cell membranes and T-tubule membranes of cardiomyocytes but additionally at membranes of endothelial cells and fibroblasts. 2. Giα was found along outer cell membranes of cardiomyocytes and other cells of the heart and also inside the cells of the perinuclear space in close contact to the nuclei envelope and the endoplasmic reticulum membranes. Goα were found to be associated mainly in atrial tissue, especially at the nerval (neuronal) endings located among the cardiac muscle cells. This was shown in parallel incubation with specific neuronal antibody as a marker for these structures. 3. Adenylyl cyclase was localized along the sarcolemma and the T-tubule membranes in normal cardiomyocytes of rat and guinea pig hearts. Under ischemic conditions, the adenylyl cyclase was also seen in junctional sarcoplasmic reticulum membranes. The reasons for this changed localization need further elucidation. Binding of the adenylyl cyclase within the molecular structure of the membrane or variation of the marker penetration remain to be clarified.
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  • 5
    ISSN: 1573-4919
    Keywords: Na,K-ATPase ; localization ; immunofluorescence ; immunoelectron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract By indirect immunofluorescence and preembedding peroxidase-diaminobenzidine technique the localization of polyclonal and monoclonal antibodies against α1, α2 and α3 isoforms of the Na,K-ATPase were studied in rat myocardium. The α1-subunit was identified predominantly on sarcolemma of cultured myocytes, neonatal, as well as adult cardiocytes. The α2 signal was localized around nuclei of cultured cardiocytes, very weak signals were seen in neonatal and more intense signal, were dispersed throughout the adult myocytes. The α3-subunit immunoreactivity was weak and localized in cell processes connecting individual cultured cells, on sarcolemma and intercalated discs of neonatal cells and very weak in adult working myocytes. Cytochemically demonstrated ouabain resistant Na,K-ATPase localized in junctional sarcoplasmic reticulum may represent α1 isoenzyme which is directly involved in modulation of action potential fluxes.
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  • 6
    ISSN: 1573-4919
    Keywords: immunogold staining ; adult myocytes ; subsarcolemmal ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract In order to understand the functional significance of Na,K-ATPase subunits as well as their isoenzymes, a precise subcellular localization of these in the myocyte is a crucial prerequisite. Cytochemical, immunofluorescence, preembedding immunogold and horse radish peroxidasediaminobenzidine methods, demonstrated α1 isoenzyme immunoreactivity on the sarcolemma, T-tubules and the subsarcolemmal cisterns of the adult cardiac myocytes. Cytochemically, ouabain resistant Na,K-ATPase precipitate was localized only in the subsarcolemmal cisterns and junctional sarcoplasmic reticulum. For α2 isoenzyme, immunoreactivity was demonstrated on the sarcolemma as well as in all areas of the myocytes in particularly a close proximation to the sarcoplasmic reticulum and microsomes. For α3 isoenzyme, only a weak insignificant signal was noted on the sarcolemma, intercalated disc and sarcoplasm. It is suggested that cytochemical ouabain resistant precipitate present in subsarcolemmal cisterns and junctional sarcoplasmic reticulum represent α1 isoenzyme of Na,K-ATPase. A differential as well as unique localization of α subunit isoenzymes of Na,K-ATPase in specific structures of cardiac myocytes may suggest importance in physiological function at these sites.
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  • 7
    ISSN: 1573-4919
    Keywords: immunocytochemistry ; antipeptide antibodies ; α1-adrenoceptors ; heart cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The localization of the ai adrenoceptors (α1-AR) in the heart tissues from rat and human and in the cultured heart cells from neonatal rats was studied by indirect immunofluorescence and postembedding electronmicroscopical immuno-gold technique. With antipeptide antibodies directed against the second extracellular loop of the human α1-AR (AS sequence 192–218), this receptor was found to be localized along the sarcolemma in both human and rat hearts. Similar localization sites were detected in cultivated rat neonatal cardiomyocytes. Beside the localization in cardiomyocytes, α1-AR were identified in endothelial cells of capillaries and smooth muscle cells of coronary vessels, in neuronal endings, in mast cells of cultivated heart cells but not, or in less amount in fibroblasts. Interestingly, in the right atrium of rat heart the localization of α1-AR was found to be near or on atrial natriuretic factor (ANF) granules, providing the basis for the α-adrenergic influence on ANF release. The immunocytochemical studies further confirm and complete the findings known by using autoradiographic binding studies with specific ligands.
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  • 8
    ISSN: 1573-4919
    Keywords: neonatal rat cardiomyocyte culture ; sarcoplasmic reticulum ; phospholamban ; calcium ATPase ; calcium transport ; thyroid hormone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract This study investigates sarcoplasmic reticulum (SR) calcium-(Ca2+) transport ATPase (SERCA2a) and phospholamban (PLB) in cultured spontaneously contracting neonatal rat cardiomyocytes (CM) to ascertain the function of both SR proteins under various culture conditions. The two major SR proteins were readily detectable in cultured CM by immunofluorescent microscopy using specific anti-SERCA2 and anti-PLB antibodies. Double labeling technique revealed that PLB-positive CM also labeled with anti-SERCA2. Coexpression of SERCA2 and PLB in CM was supported by measurement of cell homogenate oxalate-supported Ca2+ uptake which was completely inhibited by thapsigargin and stimulated by protein kinase A-catalyzed phosphorylation. Under serum-free conditions, incubation of CM with the SERCA2a expression modulator 3,3′,5-triiodo-L-thyronine (100 nM, 72 h) resulted in elevated Ca2+ uptake of +33%. Specific Ca2+ uptake activity was not altered if insulin was omitted from the serum-free culture medium but total SR Ca2+ transport activity was reduced under this culture condition. The results indicate that primary culture of spontaneously contracting neonatal rat CM can be employed as a useful model system for investigating both short- and long-term mechanisms determining the Ca2+ re-uptake function of the SR under defined culture conditions.
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  • 9
    ISSN: 0570-0833
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 237 (1984), S. 395-407 
    ISSN: 1432-0878
    Keywords: Spermatogenesis ; Seminiferous epithelium ; Morphogenesis ; Testis ; Man
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The various types of human primary spermatocytes were classified by means of morphological and morphometrical studies. Based on this classification, the topographic arrangement of the spermatocyte populations in the longitudinal course of seminiferous tubules was determined. This analysis revealed human spermatogenesis be to subjected to a complex local plan of organization, which is based upon the geometry of spirals. The centers of gravity of spermatocyte populations of subsequent degrees of differentiation are arranged on he lices that are contracted conically to the lumen of the seminiferous tubule. On these helices the centers of gravity of the populations diverge continuously 173.8°+/-32.4°. Populations of the same degrees of development are arranged on helices with constant diameters. On these helices the centers of gravity of the populations diverge continuously 142.6°+/-14.2°. The present results lead to new aspects of the kinetics and morphogenesis of the seminiferous epithelium, which can be integrated into a comprehensive biological concept.
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