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  • 1
    ISSN: 1040-452X
    Keywords: Sperm maturation ; Sperm-egg recognition ; Fertilization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the preceding study (Okamura et al., 1992; Biol Reprod 47:1040-1052) we suggested that a 135-kDa protein secreted by porcine epididymis is involved in the sperm maturation. In this work, we have isolated the cDNA clone coding the 135-kDa protein in an effort to investigate its structure and function.The 135-kDa protein was purified from porcine cauda epididymal fluid. Three oligonucleotide probes were synthesized according to the amino acid sequences of N-termini of the native protein and trypsin-digested peptides. A cDNA clone hybridizing with these three probes was isolated from the cDNA library derived from the porcine proximal corpus epididymis. It encodes a novel protein with 1,006 amino acid residues in an open reading frame.Its overall amino acid sequence was significantly homologous (25.7%) to the α-mannosidase precursor of Dictiostelium discoideum (P34098). The 135-kDa protein could digest both p-nitro-phenyl-α-D-mannoside and high mannose oligo saccharide (Man8-GlcNAc2), strongly suggesting that it is an α-mannosidase homologue.The expression of this protein was specific to porcine and was localized to the very narrow parts of epididymis: the border of the caput and corpus epididymis. This protein may serve as a good marker for the functional differentiation in porcine epididymis. A possible role of this protein in the species-specific sperm-egg interaction is discussed. © 1995 wiley-Liss, Inc.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0878
    Keywords: Epididymis ; Immunogold technique ; Ultrastructure ; Protein secretion ; Antagglutinin ; Boar
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Antagglutinin, a specific protein synthesized by the boar epididymis, was localized by an ultrastructural immunogold-labeling procedure in the principal cells of the three regions of the caput epididymidis, most notably at the sites of synthesis and secretion. The intensity of the reaction was variable in the three epididymal zones. Labeling was of low intensity in the proximal and middle caput, except in the granules of the latter. These granular “storage sites” did not correspond to typical secretory granules but appeared to be intracellular sites of degradation of this protein. In the distal caput, which was devoid of these granules, intense secretory activity for antagglutinin was detected. Few gold particles were localized in the RER profiles but labeling was detected in the Golgi zone, in numerous dense vesicles, in structures distributed between the Golgi zone and the apex of the cell, and in the epididymal lumen. This study has enabled us to visualize immunocytochemically antagglutinin along its intracellular secretory pathway, i.e. at the site of its synthesis, during its passage via the Golgi zone, and its intracellular transport to the lumen.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 255 (1989), S. 371-378 
    ISSN: 1432-0878
    Keywords: Epididymis ; Antagglutinin ; Biotin-streptavidin technique ; Castration ; Testosterone ; Boar (Large White)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Antagglutinin, a specific protein synthesized by the boar epididymis, was secreted by the principal cells of the initial segment, the caput and the corpus, but was not detectable in the caudal cells. Castration completely abolished the synthesis and secretion of antagglutinin in all epididymal cells. Androgen replacement suggests that the epithelial cells from different segments have differential regulatory mechanisms. The proximal zone appeared refractory to exogenous testosterone; the median zone was a typical androgen-dependent region; and the caudal cells, where an unusual secretion of antagglutinin was detected, revealed still a different reaction pattern. It is postulated that these latter cells depend not solely on androgen but also or exclusively on other factors. Our results, which demonstrate a primary role of the Golgi complex in the secretory process in the epididymal cells, also suggest that the apical smooth endoplasmic reticulum may be implicated in the intracellular transport of glycoproteins to the cell surface.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 252 (1988), S. 329-337 
    ISSN: 1432-0878
    Keywords: Antagglutinin ; Epididymis ; Biotin-streptavidin technique ; Protein secretion ; Boar (Large White)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Antagglutinin, a specific protein synthesized by the boar epididymis, was localized by the biotin-streptavidin method in all the principal cells of the caput and corpus epididymidis as well as in the lumen of this organ. Intracellular staining, which was first detected in the initial segment, appeared stronger in the distal caput and in the corpus but diminished and disappeared in the caudal epididymal cells. In all the principal cells, a consistent reaction product was localized in the large Golgi complex. Only slight and diffuse immunoreactive material was detected in the cytoplasm, except in the middle caput where the heterogeneous reactive granules appeared to be intracellular sites of degradation of this protein. In the lumen, the intensity of reaction increased from the caput to the cauda. Antagglutinin appeared strongly associated with the luminal surfaces, especially around and between the stereocilia. However, the spermatozoa also exhibited a distinct pattern of immunostaining. The results are discussed in relation to protein secretion in the epididymis and to the role of antagglutinin in the gamete-interaction process.
    Type of Medium: Electronic Resource
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