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  • 1
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Monatsschrift Kinderheilkunde 146 (1998), S. 590-593 
    ISSN: 1433-0474
    Keywords: Schlüsselwörter Ektodermale Dysplasie ; Hypohidrotisch ; Key words Ectodermal dysplasia ; Hypohidrotic
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary We present a case report of a 15 year old girl suffering from a hypohidrotic ectodermal dysplasia with the symptoms of oligodontia and teeth anomalies. Her hair growth pattern was generally reduced and the Minor-sweat-test showed pathological results. On histological examination there were no sweatglands and only rudimentary adnexal structures. In the mother and sister of the patient only a hypodontia could be diagnosed. Discussion Recurring bouts of otherwise unexpliceble fever in combination with anomalies of hair and teeth suggest the possibility of hypohidrotic ectodermal dysplasia.
    Notes: Zusammenfassung Es wird ein 15jähriges Mädchen mit einer hypohidrotischen ektodermalen Dysplasie vorgestellt. Die Patientin wies eine Oligodontie und Zahnformanomalien auf. Das Behaarungsmuster war generell stark reduziert, der Minor-Schweißtest pathologisch. Das histologische Bild der Haut ließ keine Schweißdrüsen und nur rudimentäre Adnexstrukturen erkennen. Die Mutter und die Schwester der Patientin wiesen hingegen lediglich eine Hypodontie auf. Diskussion: Bei rezidivierendem Fieber unklarer Ursache mit gleichzeitig vorhandenen Zahn- und Haaranomalien sollte auch an die hypohidrotische ektodermale Dysplasie gedacht werden.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Reproduktionsmedizin 15 (1999), S. 231-239 
    ISSN: 1434-808X
    Keywords: Schlüsselwörter Humanspermien ; Adhäsionsmoleküle ; Fertilisierung ; Polymerasekettenreaktion ; Hamster Oozyten Penetrations-Test ; In-vitro-Fertilisierung ; Key words Human spermatozoa ; Adhesion molecules ; Fertilization ; Polymerase chain reaction ; Hamster oocyte penetration test (HOP-test) ; In vitro fertilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Ejaculated spermatozoa and spermatogenic cells express α- and β-chains of β1-, β3- and β4-integrins as well as their ligands laminin and fibronectin. These adhesion molecules (AM) showed an extended intra- and interindividual variation and different patterns of location. The mRNA transcripts of the AM were detectable by nested polymerase chain reaction in the spermatozoa. The conclusion of a functional competence of the AM was supported by the correlation of the AM-expression on the spermatozoal surface after the acrosome reaction with three function tests: (i) the zona-free hamster oocyte penetration (HOP) test, (ii) the in vitro fertilization of human oocytes and (iii) the cell attachment assays. AM labelling was modified by progesterone, human follicular fluid, disintegration of the sperm plasma membrane in seminal plasma, and micro organisms. In contrast, the sperm cryopreservation did barely influence the labelling of spermatozoal AM.
    Notes: Zusammenfassung Ejakulierte Spermien und Spermatogenesezellen exprimieren α- und β-Ketten der β1-, β3- und β4-Integrine sowie deren Liganden Fibronektin und Laminin. Die Adhäsionsmoleküle (AM) zeigen auf der Spermienoberfläche eine ausgeprägte intra- und interindividuelle Variation sowie unterschiedliche Lokalisationen. Die „nested“ Polymerasekettenreaktion war in der Lage, mRNA Transkripte dieser Moleküle in ejakulierten Humanspermien nachzuweisen. Bis zum heutigen Tag ist unklar, ob die AM funktionelle Relevanz für die Interaktionen zwischen Spermien und Oozyten oder anderen Spermienkontaktzellen aufweisen oder nur „biologische Redundanz“ darstellen bzw. nur die allerletzte Bindungsabsicherung (final insurance). Die Vermutung einer funktionellen Kompetenz der AM wird durch drei Funktionstests unterstützt, (a) die Korrelation der AM-Expression auf der Spermienoberfläche nach der artifiziellen Akrosomenreaktion mit der Spermien-Oozyten-Bindung im zonafreien Hamster-Oozyten-Penetrationstest (HOP-Test), (b) mit der In-vitro-Fertilisierung humaner Oozyten und (c) mit der Bindung im Festphasen Bindungsassay. Die Markierung der Spermien-AM wurde durch Progesteron, humane Follikelflüssigkeit, Disintegration der Spermienplasmamembran im Seminalplasma und Mikroorganismen modifiziert. Die Spermakryokonservierung führte nur zu geringgradigen Änderungen.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell and tissue banking 1 (2000), S. 133-142 
    ISSN: 1573-6814
    Keywords: human spermatozoa ; cryopreservation ; plasma membrane ; fluorogenic enzyme substrates ; Annexin V-binding ; apoptosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effects of cryopreservation on two characteristics of human spermatozoa were investigated: the early phases of disturbed plasma membrane function and the activity of enzymes in intact spermatozoa. The membrane function was detected by means of the calcium-dependent binding of fluorescein isothiocyanate (FITC)-conjugated Annexin V to sperm plasma membranes. Annexin V monitors the translocation of phosphatidylserine from the inner to the outer leaflet of the plasma membrane, which is one of the earliest features of membrane disintegration. For the second aim synthetic fluorogenic substrates for peptidases, proteinases, esterases, elastases and collagenases were applied. These substrates, CellProbe™ reagents consist of different peptide sequences, specific for the enzymes, and a fluorescein- or rhodamine 110-dye moiety. They enter the cells without previous membrane permeabilisation and exhibit fluorescence after cleavage depending on enzyme activity. The number of positive cells and the intensity of the fluorescence were determined by flow cytometric analysis comparing fresh spermatozoa with cryopreserved ones. Thirty-five semen samples collected from 35 donors were cryopreserved using the freezing medium TEST yolk buffer. All specimens showed normal spermiogram parameters. Twenty-five of the samples were used for detection of Annexin V-FITC binding and 10 semen samples for investigations of the intracellular enzymes. The Annexin V-assay applied two fluorescent dyes (Annexin V, AN and propidium iodide, PI) which led to three groups of spermatozoa (a) viable spermatozoa (AN V-negative and PI-negative), (b) dead spermatozoa (AN V-positive and PI-positive) and (c) cells with impaired but integer plasma membrane (AN V-positive and PI-negative). The percentage of vital Annexin V-negative spermatozoa (x ± SEM) decreased significantly (p 〈 0.001) from fresh spermatozoa (51.6 ± 3.1) to cryopreserved spermatozoa (26.6 ± 2.2%) and was associated with their motility (57.9 ± 1.9% motile fresh spermatozoa vs. 22.6 ± 3.9% motile sperm after cryopreservation). Of the spermatozoa 28.2% were Annexin V-positive before and 44.4% after cryostorage even though they did not bind to PI. Thus, vital spermatozoa showed a disturbed membrane function indicating viability before as well as after cryostorage. Moreover, after cryopreservation the spermatozoal fluorescence increased applying substrates for butyryl esterase (p 〈 0.05), prolyl-aminopeptidase (p 〈 0.001) and val-lys-(VK)-cathepsin (p 〈 0.001). In contrast, the activities of fluorescein diacetate (FDA)- and FDA/sodium fluoride (NAF)-esterase (p 〈 0.05), ala-ala-pro-val-(AAPV)-elastase (p 〈 0.001), gly-pro-leu-gly-pro-(GPLGP)-collagenase (p 〈 0.05) and gly-gly-leu-(GGL)-subtilisin (p 〈 0.001) decreased after cryopreservation. The substrates for arg-gly-glut-ser-(RGES)-elastase, gly-phenyl-gly-ala-(GFGA)-collagenase and threo-pro-(TP)-cathepsin were not cleaved before as well as after cryostorage. In addition to the known effects of sperm cryopreservation our results showed two further alterations of human ejaculated spermatozoa: (a) disturbed plasma membrane function, which is not detectable by supravital staining and (b) a changed pattern of intracellular enzyme activities.
    Type of Medium: Electronic Resource
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