Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 208 (1984), S. 197-206 
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Mouse and guinea pig epididymal tissues have been investigated by light and electron microscopic autoradiography after long intervals ranging from 24 h to 5 days postinjection (p.i.) of the glycoprotein precursors, L-fucose-6-3H of D-glucosamine-1-3H. Using modified fixations to enhance glcoprotein preservation in situ, we found intense labelling of luminal contents in at least some of the epididymal segments after all the intervals investigated. At 24 h p.i., the label in guinea pig was associated with spermatozoa during remodelling of the acrosome in segment II, and at 3 days p.i., radioactivity was trapped within sperm head associations (“rouleaux”) in segment IV of the epididymis. At this time, similar rouleau labelling extended from segment IV to segment VIII. In mouse, the luminal contents of the cauda epididymis were still intensely labelled at 5 days p.i.; analysis of the electron microscopic autoradiograms showed that relative grain concentration over the spermatozoa was twice that of the epididymal plasma. This concentration was especially elevated in the region of the sperm head. These findings taken together were interpreted as the binding of secreted epididymal glycoproteins to spermatozoa during sperm transit through the epididymis.In contrast to luminal contents, the labelling of the epididymal epithelium was generally lower, except on the clear cells which showed more pronounced labelling than the neighboring principal cells in mouse cauda epididymis at 5 days p.i. This label probably originated from the resorption of luminal glycoproteins.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 41 (1995), S. 274-274 
    ISSN: 1040-452X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 40 (1995), S. 305-310 
    ISSN: 1040-452X
    Keywords: Fibrillarin ; Nucleolin ; Immunocytochemistry ; Cleavage-stage embryo ; Mouse ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The localization of fibrillarin and nucleolin in the nuclei of mouse two-cell, four-cell, and eight-cell embryos has been studied using immunofluorescent staining with specific antibodies. In all of these cleavage stages, both antigens were associated exclusively with the peripheral region of the nucleolus precursor bodies (NPBs). The original speckled fluorescent staining pattern in the early two-cell stage was progressively changed into a continuous fluorescent-positive layer localized in the cortex of the NPBs in the four-cell embryos. The compact central area of NPBs was never stained. Both proteins were colocalized in the same substructures of developing nucleoli. In order to analyze the interaction of chromatin, with NPBs, DNA structures were specifically immunolbelled. At the time of resumption of nucleolar transcription (in the two-cell mouse embryo), DNA was detected at the periphery of, but not penetrating into, NPBs. Our results confirm the view that the cortical region of NPBs could represent a nucleolonemal area involved in the resumption of nucleolar transcription in the early mouse embryo. © 1995 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 1 (1989), S. 79-90 
    ISSN: 1040-452X
    Keywords: Cleaving embryo ; RNA synthesis ; DNA distribution ; Cattle ; Nucleogenesis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Eight-cell cow embryos were isolated and cultured in vitro in a medium enriched with 200 μCi of [5-3H]uridine for 20 min. Epon ultrathin sections of the embryos were investigated for the nucleolar morphology and for the appearance and localization of the sites of [5-3H]uridine incorporation by means of electron microscopic autoradiography. In addition to this, a general pattern of replicated embryonal DNA distribution was revealed by [methyl-3H]thymidine incorporation and light microscopic autoradiography.The essential phases of the transformation of the small nucleous precursor body (NPB) into a vast, functionally fully active nucleolus, characterized by typical nucleolar substructural components, are taking place within the eight-cell stage. This process differed in its morphology from the nucleologenetic process in early embryogenesis of other mammals, especially of that in the mouse.The first sign of NPB, transformation was the appearance of a large central vacuole followed later on by perinucleolar chromatin penetration into NPB, documented by both morphology and [3H]thymidine autoradiography. In some cases, concentration of dense fibrillar material forming clumps or stalks was seen in the central vacuole.The following rapid nucleolar development was characterized by the formation of secondary vacuoles concomitant with the onset of [5-3H]uridine incorporation into the dense fibrillar component and with the appearance of the first granules in the otherwise fibrillar structure of the nucleolus. During the late eight-cell stage, the still-rounded nucleolus developed features of a reticulated nucleolus known from somatic cells intensively synthesizing rRNA: a dense fibrillar component with associated labeling encircling fibrillar centers and a well-developed granular component. The labeled dense fibrillar component was observed mostly in the central area of the nucleolus; early embryonic NPB dense fibrous material not involved in transcription was disappearing rapidly. At the transition to the 16-cell stage the nucleoli lost their rounded shape because of the accumulation of a large amount of granular component, and they occupied a considerable part of the nucleus. In conclusion, the appearance of the nucleolar vacuole in eight-cell cow embryo is the starting point for following morphogenetic events linked with the onset of transcription.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    American Journal of Anatomy 151 (1978), S. 39-53 
    ISSN: 0002-9106
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The ultrastructure of spermatozoa from the cauda epididymidis and vas deferens of Octodon degus  -  a Chilean hystricomorph rodent - is presented. The head of spermatozoa measured 7.7 μm long by 5.9 μm wide and the tail was 41 μm long. The head was flattened dorso-ventrally and ovate in outline. The acrosome was the most distinctive feature of O. degus spermatozoa. In a frontal view of the head, the rim of the acrosome surrounding the nucleus had the shape of an inverted U. The acrosomal region covering the plane of the flattened head exhibited dome-shaped protrusions. Transverse or sagittal sections of acrosomal protrusions showed that the plasma membrane and outer acrosomal membrane were evaginated, while the inner acrosomal membrane followed the contour of the nucleus. The protrusions were not distributed at random and they were absent in the equatorial segment and in the rim of the acrosome.In frontal views, near the boundary between the acrosome and post-acrosomal region, fine rods about 170 nm long ran obliquely on the caudal part of the equatorial segment. Behind the same boundary, the post-acrosomal region showed a serrated border.Phosphotungstic acid treatment at pH 0.3 produced staining at the surface of the sperm as well as within a superficial layer of the marginal thickening of the acrosome and on the acrosomal protuberances.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 9 (1984), S. 425-440 
    ISSN: 0148-7280
    Keywords: acrosin ; acrosome reaction ; enzyme localization ; immunocytochemistry ; proacrosin ; spermatozoa ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Proacrosin and acrosin were localized immunocytochemically at the electron microscope level in ram spermatozoa undergoing an ionophore-induced acrosome reaction. Antigenicity was preserved after fixation with 0.5% w/v ethyl-(dimethylaminopropyl)-carbodimide, and an antibody preparation was used that reacted with all major forms of ram acrosin. All stages of the acrosome reaction could be observed in a single preparation. At the earliest stage, labeling was observed throughout the acrosomal contents, which were just beginning to disperse. As dispersal proceeded, labeling diminished, being associated only with visible remnants of the acrosomal matrix. By the time the acrosome had emptied, almost no labeling could be detected on the inner acrosomal membrane.The relationship between matrix dispersal and proacrosin activation was studied in isolated ram sperm heads. While proacrosin was prevented from activating, the acrosomal matrix remained compact; but as activation proceeded, the matrix decondensed and dispersed in close parallel. By the time proacrosin activation was complete, the acrosomal contents had almost entirely disappeared.We conclude that proacrosin is distributed throughout the acrosomal contents as an intrinsic constituent of the acrosomal matrix. During the acrosome reaction, proacrosin activation occurs, resulting directly in decondensation of the matrix. All the contents of the acrosome including acrosin disperse and, by the time the acrosome is empty and the acrosomal cap is lost, only occasional traces of acrosin remain on the inner acrosomal membrane. Since the acrosomal cap is normally lost during the earliest stages of zona penetration, acrosin's role in fertilization is unclear: it does not appear to be a zona lysin bound to the inner acrosomal membrane.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 3 (1980), S. 141-148 
    ISSN: 0148-7280
    Keywords: cow blastocysts ; zona pellucida ; stability and location of antigenic material ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Labeling of the zona pellucida of cow blastocysts with zona-specific anti-serum shows that antigenicity is unaffected by abnormal cleavage, in vitro culture, or frozen storage. The uniform labeling in thin sections indicates that the zona pellucida is homogeneous antigenically. Heavier labeling of the inner and outer surfaces of the zona pellucida in thick sections appers to be due to greater porosity of these regions, in which the zona material becomes highly dispersed, or even partly solubilized, thereby permitting the formation of an antigen-antibody matrix.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 21 (1988), S. 185-192 
    ISSN: 0148-7280
    Keywords: oocyte ; fusion ; protein synthesis inhibition ; maturation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The method of polyethylene-glycol-induced fusion of mammalian oocytes was applied to study maturation-promoting factor (MPF) activity. After homologous fusions of one maturing-late diakinesis (LD), metaphase I (MI)-pig or mouse oocyte to one, two, or three immature-germinal vesicle (GV)-oocytes, giant cells were cultured in control or cycloheximide supplemented medium for 3 hours. The occurrence of germinal vesicle breakdown (GVBD) and premature chromosome condensation (PCC) served as a control of MPF activity. In giant cells composed of one maturing and one, two, or three immature oocytes, GVBD and PCC were observed in all cases after cultivation in the control medium. In the presence of cycloheximide, the completion of GVBD and PCC remained high when one maturing and one immature oocyte were fused (83.7% and 95.7% of GVBD in pig and mouse, respectively). However, in giant cells composed of one maturing and up to three immature oocytes, all GVs were broken down only occasionally (4.8% and 11.7% in pig and mouse, respectively). These results suggest that in pig and mouse oocytes MPF does not amplify autocatalytically, but requires active protein synthesis for its production.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Gamete Research 17 (1987), S. 35-42 
    ISSN: 0148-7280
    Keywords: zona pellucida ; autoradiography ; sperm binding ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Rabbit spermatozoa were labeled predominantely in their acrosomal glycoproteins by 1-3H-glucosamine during spermiogenesis. Ova fertilized in vivo by spermatozoa labeled 22 days earlier were analyzed by fine-structure autoradiography for the localization of the label. The latter was found associated with 1) the fused membranes of the acrosomal cap remaining on the zona pellucida surface, 2) the material released on the zona surface after the acrosome reaction and possibly detectable after tannic acid fixation, 3) the equatorial segment of the sperm head and the preequatorial swellings, and 4) other sperm components, eg, the sperm tail. No labeling, on the other hand, was detected on the denuded leading edge of spermatozoa found either in the penetration slit or in the perivitelline space. Our observations suggest the involvement of acrosomal glycoproteins in different mechanisms of sperm/zona pellucida interaction but are not in favor of a major role of (enzymatic) glycoproteins bound to the inner acrosomal membrane during the penetration of the zona pellucida.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...