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  • 1
    Electronic Resource
    Electronic Resource
    Presence of anti-Müllerian hormone correlates with absence of laminin α5 chain in differentiating rat testis and ovary (1999)
    Springer
    Histochemistry and cell biology 111 (1999), S. 367-373 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The distribution of anti-Müllerian hormone (AMH) and laminin (Ln) α5 chain in differentiating rat testis and ovary were studied by immunohistochemistry. In the incipient embryonic male gonad a weak reaction for Ln α5 chain, but not for AMH, was detected. With further prenatal development, Ln α5 chain rapidly disappeared from the basement membrane (BM) of the incipient testicular cords in parallel with the appearance of AMH in the Sertoli cells. After birth, Ln α5 chain reappeared in the BMs of the cords with the decline and disappearance of AMH from the respective Sertoli cells. In the corresponding stages of the ovary, Ln α5 chain was present in the BM of the prenatal gonadal cords and in postnatal primordial follicles. The cells of those epithelia were negative for AMH. With the growth of the follicles, Ln α5 chain disappeared from the BM when AMH appeared in the epithelial follicular cells. The present results show that male and female gonadal epithelia negative for Ln α5 chain were positive for AMH, and that epithelia positive for Ln α5 chain were negative for AMH. Thus, epithelial Ln α5 chain and AMH as a product of the same cell seemed to exclude each other. The results require an explanation why Ln α5 chain has to be excluded from the BM of the epithelia during the secretion of AMH chain through the basal cell membrane to the surrounding tissues where it executes its important biological functions. These observations suggest a hypothesis that the production of both components is regulated by the same gene and factor system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050369
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  • 2
    Electronic Resource
    Electronic Resource
    Lectin-binding carbohydrates in sexual differentiation of rat male and female gonads (1992)
    Springer
    Histochemistry and cell biology 97 (1992), S. 469-477 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Development and sexual differentiation of the mammalian gonad involve changes in the type and distribution of different proteins and glycoproteins in and around the epithelial gonadal cords, the future seminiferous tubules in the testis, and follicles in the ovary. To study changes in cellular carbohydrate-containing compounds in the sex-specific morphogenesis of rat gonads, sections from embryonic, fetal and early postnatal gonads were labelled with seven different fluorescein isothiocyanate (FITC)-conjugated plant lectins of various carbohydrate-binding specificities. Double labelling of laminin with tetramethylrhodamine isothiocyanate (TRITC)-conjugated antibodies was used to outline the epithelial tissues. From the results we conclude that the abundance and similar distribution of carbohydrates in the early gonads of both sexes supports their sexually indifferent nature. Furthermore, the basement membranes of the differentiating gonadal cords in both sexes have common features, which differ, however, from those of the other developing urogenital organs. Changes in carbohydrate composition appear with the sexual differentiation of the gonads; the similarity of the changes in lectin binding to the gonadal cords of embryonic and fetal male, and to postnatal female, suggests similar mechanisms of cell-cell interactions in both sexes although activated at different developmental stages. These carbohydrate specificites at the tissue level should be taken into account together with cell-type specific changes, e.g. in the formation of the zona pellucida, when the phenomenon of polymorphic expression of different compounds is integrated into theories of epithelial differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316066
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  • 3
    Electronic Resource
    Electronic Resource
    Differentiation-related changes in the distribution of glycoconjugates in rat testis (1990)
    Springer
    Histochemistry and cell biology 94 (1990), S. 387-395 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of glycoconjugates in differentiating rat testis was investigated by fluorescein labeled lectins during embryogenesis and postnatal development. Double immunofluorescence with rhodamine coupled laminin antibodies was used to delineate testicular cords from the interstitium in embryonic testes. Rat testis was found to be rich in various glycoconjugates, with distinct differentiation-related changes in their distribution. All types of germ cells contained carbohydrate rich compounds in their cytoplasm. Glycosylation in the embryonic testis was different from that in the adult rat. At an early stage of testicular differentiation, the labeling of germ cells and other testicular cells was almost identical. The lectin binding patterns of embryonic germ cells and somatic cells were related to the developmental age of the animal, with a graded disappearance of galactose containing glycoconjugates in embryonal spermatogonia. Spermatogenic cell differentiation was characterized by striking changes in lectin binding patterns of germ cells, particularly in the acrosomes of developing spermatids, in relation to their functional activation and the emergence of adult type of glycosylation during the postnatal maturation of the testis. As the knowledge of regular glycosylation throughout tissue differentiation is of significance for the analysis of aberrant glycosylations occurring in pathologic disorders, our findings suggest the usefulness of lectin histochemistry for the studies on germ cell differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266445
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  • 4
    Electronic Resource
    Electronic Resource
    Sox9 protein in rat Sertoli cells is age and stage dependent (2000)
    Springer
    Histochemistry and cell biology 113 (2000), S. 31-36 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  We studied the location of Sox9 protein in the embryonic, juvenile, and adult rat testis by immunohistochemistry and immunoblotting. Sox9 belongs to a family of Sox proteins that are transcription factors and important in several developmental processes. In the incipient embryonic testis, Sox9 was prominently present in the gonadal blastema. With further embryonic differentiation, Sox9-positive cells arranged in the periphery of the testicular cords, showing the location of the Sertoli cells. Thereafter the immunoreaction for Sox9 gradually declined and was only weakly detectable in the 2-day-old postnatal rat testis. This situation remained for some period of time. In the 15-day-old rat testis, Sox9 protein strongly reappeared in the testicular cords. In the adult, the Sertoli cells of most regions of the seminiferous tubules were positive for Sox9. The strongest reaction for Sox9 was found in the dark zone. However, clearly negative or only weakly positive spermatogenic stages for the protein were also found, as seen for example in the pale zone. In fertile 1-year-old rats this basic situation was still detectable. Analyzed rat ovaries were all negative for Sox9, showing the sex-specific nature of Sox9. The results showed that Sox9 protein is distinctly present in the developing and mature Sertoli cells, but that its presence and amount is dependent on the age and the spermatogenetic stage within the seminiferous tubuli. The prominent presence of Sox9 in the incipient testis and at puberty suggests that this protein is needed at important phases of aggregation and reorganization of the Sertoli cells. The age and stage-specific presence of Sox9 in the testicular cords and in the seminiferous tubules of the adult suggests that Sox9 also may have a pivotal role in germ cell differentiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050004
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    Paper (German National Licenses)
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