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Baozhen Hua - One of the best experts on this subject based on the ideXlab platform.

  • Ultrastructure and function of the seminal vesicle of Bittacidae (Insecta: Mecoptera).
    Arthropod structure & development, 2018
    Co-Authors: Qi-hui Lyu, Bei-bei Zhang, Baozhen Hua
    Abstract:

    The fine structure of the seminal vesicle and reproductive accessory glands was investigated in Bittacidae of Mecoptera using light and transmission electron microscopy. The male reproductive system of Bittacidae mainly consists of a pair of testes, a pair of vasa deferentia, and an ejaculatory sac. The vas deferens is greatly expanded for its middle and medio-posterior parts to form a well-developed seminal vesicle. The seminal vesicle is composed of layers of developed muscles and a mono-layered epithelium surrounding the small central lumen. The epithelium is rich in rough endoplasmic reticulum and mitochondria, and secretes vesicles and granules into the central lumen by Merocrine mechanisms. A pair of elongate mesodermal accessory glands opens into the lateral side of the seminal vesicles. The accessory glands are similar to the seminal vesicle in structure, also consisting of layers of muscle fibres and a mono-layered elongated epithelium, the cells of which contain numerous cisterns of rough endoplasmic reticulum and mitochondria, and a few Golgi complexes. The epithelial cells of accessory glands extrude secretions via apocrine and Merocrine processes. The seminal vesicles mainly serve the function of secretion rather than temporarily storing spermatozoa. The sperm instead are temporarily stored in the epididymis, the greatly coiled distal portion of the vas deferens.

  • Ultrastructure of the seminal vesicle and sperm storage in Panorpidae (Insecta: Mecoptera)
    Micron (Oxford England : 1993), 2010
    Co-Authors: Sha Xie, Baozhen Hua
    Abstract:

    The histology and ultrastructure of the seminal vesicle, male accessory gland and the epididymis in Panorpa and Sinopanorpa were observed using light microscopy and scanning and transmission electron microscopy. The seminal vesicle consists of a mono-layered elongated columnar epithelium, which contains abundant electron-dense granules and secretory vesicles, and a small central lumen. In the apical region of the epithelium of the seminal vesicle, the intense secretory activity seems to be effected by means of Merocrine mechanisms. The epithelium of the accessory gland is rich in rough endoplasmic reticulum and Golgi complex, and secretes seminal fluid into the lumen via both apocrine and Merocrine mechanisms. The seminal vesicle is similar to the accessory gland in the epithelium structure and their secretory activity, mainly serving a secretory function rather than storing sperms. Instead, the sperms are stored in the epididymis, whose epithelium secretes nutrients into the large lumen by Merocrine mechanisms. The secretory activity and function of the seminal vesicle are briefly discussed.

Osamu Yamamoto - One of the best experts on this subject based on the ideXlab platform.

  • Three-dimensional structure of a parameatal urethral cyst by scanning electron microscopy.
    Urology, 2013
    Co-Authors: Nanako Yamada, Yuichi Yoshida, Ayako Ito, Shinichi Morino, Osamu Yamamoto
    Abstract:

    We report scanning electron microscopy (SEM) for a case of parameatal urethral cyst. A 6-year-old Japanese boy presented with a cyst on the right lateral side of the urethral meatus. Histological examination revealed a cyst lined with columnar epithelium. An immunohistochemical study showed positive staining for CK7, CK13, and CEA, and negative for CK20 in luminal cells. On SEM examination, the inner surface of the cyst showed ridges arranged in a gyrus-like manner at lower magnification. Higher magnification revealed luminal cells with short microvillus projections. Some cells showed apocrine, Merocrine, and possibly holocrine-type secretions.

Beate Wilhelm - One of the best experts on this subject based on the ideXlab platform.

  • establishing of two in vitro models of epithelial cells from the apocrine secreting rat coagulating gland
    Andrologia, 2003
    Co-Authors: R Wiche, J Seitz, Beate Wilhelm
    Abstract:

    Summary. Apocrine secretion is an alternative export pathway for proteins and was described especially for accessory sex glands of rodents and men. This mechanism is not as well characterized as the classical Merocrine (eccrine) export. In the rat coagulating gland both secretion modes were observed, and several proteins were identified to be released by these two pathways. To obtain more data on the apocrine secretion mode, we established two culture models of the rat coagulating gland: primary epithelial cells and an organ culture system. The in vitro models were characterized with immunocytochemistry, electron microscopy and RT-PCR. The polarity of primary and passaged epithelial cells (passage 8) was proven by the detection of occludin, E-cadherin and β-actin. The gland tissue pieces showed good maintenance after 1-week culture. Finally we demonstrated that the epithelial cells of both culture models are still expressing and producing apocrine and Merocrine proteins. Using these two culture models for the rat coagulating gland, it is now possible to initiate studies on the apocrine secretion mechanism in vitro.

  • Identification and characterization of an IgG binding protein in the secretion of the rat coagulating gland.
    Biological chemistry, 2002
    Co-Authors: Beate Wilhelm, Gerhard Aumuller, Claudia Keppler, Dietmar Linder, Anne Henkeler, Margret Schilli-westermann, Jürgen Seitz
    Abstract:

    A Merocrine released protein (named 115k protein) was highly enriched from the secretion of the rat coagulating gland. The protein has a molecular mass of 115 kDa as calculated by SDS-PAGE under reducing conditions. Furthermore, the 115 kDa protein is glycosylated, and carries Man, GlcNAc, Gal, Fuc and sialic acid residues. For identification, N-terminal amino acid and nucleotide sequence analyses were performed. The sequences obtained showed 86 to 100% identity with human and mouse IgGFc binding proteins. The functional capacity of IgG binding of the 115 kDa protein was shown by overlay experiments, indicating its membership in the IgG binding protein family.

  • simultaneous apocrine and Merocrine secretion in the rat coagulating gland
    Cell and Tissue Research, 1999
    Co-Authors: Stephanie Groos, J Seitz, Beate Wilhelm, Heiner Renneberg, A Riva, Rudolf Reichelt, Gerhard Aumuller
    Abstract:

    The coagulating gland of the rat synthesizes two prevalent secretory proteins (transglutaminase and 115 K) that are discharched in a different manner, one being secreted in an apocrine fashion (transglutaminase) and the other one in a Merocrine way (115 K). Differences in the intra- cellular pathway and the release of either protein were studied using immunofluorescence on semithin sections, immunoelectron microscopy of preembedding-processed chopper sections and postembedding-processed ultrathin sections of rat coagulating gland. Immunohistochemical staining using an anti-transglutaminase antibody resulted in dense labeling of the cytoplasm of secretory cells and their apical blebs, whereas the cisternae of the rough endoplasmic reticulum and the Golgi apparatus were completely unlabeled. When, on the contrary, the anti-115 K antiserum was used, dense labeling of the cisternae of the rough endoplasmic reticulum, the Golgi apparatus, and the secretory granules was seen. Intraluminal secretion was also labeled, but the secretory blebs remained unlabeled. Our findings show that, in the coagulating gland of the male rat, the two secretory proteins studied are processed in parallel, but at completely different intracellular pathways. They are released via different extrusion mechanisms. Transglutaminase is synthesized outside the endoplasmic reticulum, reaches the apical cell pole by free flow in the cytoplasm, and is released via apocrine blebs, the membranes of which appear to be derived from the apical plasma membrane. The protein 115 K, on the other hand, follows the classic route, being synthesized within the cisternae of rough endoplasmic reticulum, subsequently glycosylated in the Golgi apparatus, and released in a Merocrine fashion. The mutual exclusion of the two secretory pathways and the regulation of the alternative release mechanism are still unresolved issues.

  • cytoplasmic carbonic anhydrase ii of rat coagulating gland is secreted via the apocrine export mode
    Journal of Histochemistry and Cytochemistry, 1998
    Co-Authors: Beate Wilhelm, Gerhard Aumuller, Claudia Keppler, Gudrun Hoffbauer, Friedrich Lottspeich, Dietmar Linder, Andreas Meinhardt, J Seitz
    Abstract:

    SUMMARY Two different pathways for protein secretion are described for epithelial cells of rat coagulating gland and dorsal prostate: the classical Merocrine and the alternative apocrine release mode. Apocrine-secreted proteins are synthesized on cytoplasmic polyribosomes and are subsequently exported in protrusions on the apical cell surface (aposomes). In this article we report the identification and purification to homogeneity of a 29kD protein from the secretion of rat coagulating gland. N-terminal amino acid sequence analyses revealed 100% identity to rat brain carbonic anhydrase II (CAH II). In addition, the 29-kD protein showed CAH enzyme activity. On Western blot analysis, a polyclonal antiCAH II antibody raised in rabbit reacted specifically with the rat and human but not bovine CAH II isoforms. Immunohistochemical studies on rat coagulating gland showed strong labeling for CAH II protein in aposomes. Immunoelectron microscopy confined CAH II protein to the cytoplasm and aposomes, whereas no staining was visible in the compartments of the classical Merocrine route, the endoplasmic reticulum and Golgi apparatus. The resident cytoplasmic protein lactate dehydrogenase, however, was not found in the secretion. Taken together, the morphological and biochemical data clearly indicate that cytoplasmic CAH II from rat coagulating gland is specifically selected and then secreted via the apocrine pathway. (J Histochem Cytochem 46:505‐511, 1998)

Gerhard Aumuller - One of the best experts on this subject based on the ideXlab platform.

  • Identification and characterization of an IgG binding protein in the secretion of the rat coagulating gland.
    Biological chemistry, 2002
    Co-Authors: Beate Wilhelm, Gerhard Aumuller, Claudia Keppler, Dietmar Linder, Anne Henkeler, Margret Schilli-westermann, Jürgen Seitz
    Abstract:

    A Merocrine released protein (named 115k protein) was highly enriched from the secretion of the rat coagulating gland. The protein has a molecular mass of 115 kDa as calculated by SDS-PAGE under reducing conditions. Furthermore, the 115 kDa protein is glycosylated, and carries Man, GlcNAc, Gal, Fuc and sialic acid residues. For identification, N-terminal amino acid and nucleotide sequence analyses were performed. The sequences obtained showed 86 to 100% identity with human and mouse IgGFc binding proteins. The functional capacity of IgG binding of the 115 kDa protein was shown by overlay experiments, indicating its membership in the IgG binding protein family.

  • simultaneous apocrine and Merocrine secretion in the rat coagulating gland
    Cell and Tissue Research, 1999
    Co-Authors: Stephanie Groos, J Seitz, Beate Wilhelm, Heiner Renneberg, A Riva, Rudolf Reichelt, Gerhard Aumuller
    Abstract:

    The coagulating gland of the rat synthesizes two prevalent secretory proteins (transglutaminase and 115 K) that are discharched in a different manner, one being secreted in an apocrine fashion (transglutaminase) and the other one in a Merocrine way (115 K). Differences in the intra- cellular pathway and the release of either protein were studied using immunofluorescence on semithin sections, immunoelectron microscopy of preembedding-processed chopper sections and postembedding-processed ultrathin sections of rat coagulating gland. Immunohistochemical staining using an anti-transglutaminase antibody resulted in dense labeling of the cytoplasm of secretory cells and their apical blebs, whereas the cisternae of the rough endoplasmic reticulum and the Golgi apparatus were completely unlabeled. When, on the contrary, the anti-115 K antiserum was used, dense labeling of the cisternae of the rough endoplasmic reticulum, the Golgi apparatus, and the secretory granules was seen. Intraluminal secretion was also labeled, but the secretory blebs remained unlabeled. Our findings show that, in the coagulating gland of the male rat, the two secretory proteins studied are processed in parallel, but at completely different intracellular pathways. They are released via different extrusion mechanisms. Transglutaminase is synthesized outside the endoplasmic reticulum, reaches the apical cell pole by free flow in the cytoplasm, and is released via apocrine blebs, the membranes of which appear to be derived from the apical plasma membrane. The protein 115 K, on the other hand, follows the classic route, being synthesized within the cisternae of rough endoplasmic reticulum, subsequently glycosylated in the Golgi apparatus, and released in a Merocrine fashion. The mutual exclusion of the two secretory pathways and the regulation of the alternative release mechanism are still unresolved issues.

  • cytoplasmic carbonic anhydrase ii of rat coagulating gland is secreted via the apocrine export mode
    Journal of Histochemistry and Cytochemistry, 1998
    Co-Authors: Beate Wilhelm, Gerhard Aumuller, Claudia Keppler, Gudrun Hoffbauer, Friedrich Lottspeich, Dietmar Linder, Andreas Meinhardt, J Seitz
    Abstract:

    SUMMARY Two different pathways for protein secretion are described for epithelial cells of rat coagulating gland and dorsal prostate: the classical Merocrine and the alternative apocrine release mode. Apocrine-secreted proteins are synthesized on cytoplasmic polyribosomes and are subsequently exported in protrusions on the apical cell surface (aposomes). In this article we report the identification and purification to homogeneity of a 29kD protein from the secretion of rat coagulating gland. N-terminal amino acid sequence analyses revealed 100% identity to rat brain carbonic anhydrase II (CAH II). In addition, the 29-kD protein showed CAH enzyme activity. On Western blot analysis, a polyclonal antiCAH II antibody raised in rabbit reacted specifically with the rat and human but not bovine CAH II isoforms. Immunohistochemical studies on rat coagulating gland showed strong labeling for CAH II protein in aposomes. Immunoelectron microscopy confined CAH II protein to the cytoplasm and aposomes, whereas no staining was visible in the compartments of the classical Merocrine route, the endoplasmic reticulum and Golgi apparatus. The resident cytoplasmic protein lactate dehydrogenase, however, was not found in the secretion. Taken together, the morphological and biochemical data clearly indicate that cytoplasmic CAH II from rat coagulating gland is specifically selected and then secreted via the apocrine pathway. (J Histochem Cytochem 46:505‐511, 1998)

Sha Xie - One of the best experts on this subject based on the ideXlab platform.

  • Ultrastructure of the seminal vesicle and sperm storage in Panorpidae (Insecta: Mecoptera)
    Micron (Oxford England : 1993), 2010
    Co-Authors: Sha Xie, Baozhen Hua
    Abstract:

    The histology and ultrastructure of the seminal vesicle, male accessory gland and the epididymis in Panorpa and Sinopanorpa were observed using light microscopy and scanning and transmission electron microscopy. The seminal vesicle consists of a mono-layered elongated columnar epithelium, which contains abundant electron-dense granules and secretory vesicles, and a small central lumen. In the apical region of the epithelium of the seminal vesicle, the intense secretory activity seems to be effected by means of Merocrine mechanisms. The epithelium of the accessory gland is rich in rough endoplasmic reticulum and Golgi complex, and secretes seminal fluid into the lumen via both apocrine and Merocrine mechanisms. The seminal vesicle is similar to the accessory gland in the epithelium structure and their secretory activity, mainly serving a secretory function rather than storing sperms. Instead, the sperms are stored in the epididymis, whose epithelium secretes nutrients into the large lumen by Merocrine mechanisms. The secretory activity and function of the seminal vesicle are briefly discussed.