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  • 1
    Electronic Resource
    Electronic Resource
    Cell growth and monoclonal antibody production in the presence of antigen and serum (1995)
    s.l. : American Chemical Society
    Biotechnology progress 11 (1995), S. 518-524 
    Details
    ISSN: 1520-6033
    Source: ACS Legacy Archives
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bp00035a004
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  • 2
    Electronic Resource
    Electronic Resource
    Evidence for a unique N-linked glycan associated with human infertility on sperm CD52: a candidate contraceptive vaccinogen (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Immunological reviews 171 (1999), S. 0 
    Details
    ISSN: 1600-065X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: A major objective in developing a sperm antigen-based contraceptive vaccine for humans is the discovery of sperm surface immunogens that are functionally relevant and sperm specific. The latter criterion is deemed essential to avoid the possibility of inducing autoimmune disease upon vaccination. This review presents evidence that a unique carbohydrate epitope is synthesized in the human epididymis, is attached to the core peptide of CD52, a lymphocyte differentiation marker, and is subsequently inserted into the sperm membrane via a glycosylphosphatidylinositol anchor. This unique CDS2 glycoform is localized to the entire sperm surface, functions as a potent target for agglutitiating and cytotoxic antibodies, and is one of the few well-defined sperm surface glycoproteins indicated in human antibody-mediated infertility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-065X.1999.tb01350.x
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  • 3
    Electronic Resource
    Electronic Resource
    The baboon expresses the calbindin-D9k gene in intestine but not in uterus and placenta: Implication for conservation of the gene in primates (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 40 (1995), S. 400-407 
    Details
    ISSN: 1040-452X
    Keywords: Calbindin ; Uterus ; Placenta ; Duodenum ; Estrogen ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Expression of the Calbindin-D9k (CaBP-9k) gene was studied in the baboon. Northern blot analysis using a human CaBP-9k cDNA probe detected expression in duodenum but not in uterus and placenta. Reverse transcription/polymerase chain reaction (RT/PCR) confirmed this expression pattern and indicated a high degree of identity between the baboon and human CaBP-9k mRNAs. PCR was employed to amplify the intron A region of the baboon CaBP-9k gene using human-derived primers and baboon genomic DNA. The baboon intron was closely related to the human CaBP-9k intron A, including the presence a complete Alu-repetitive element. Most significantly, a 13 nucleotide long element at the 5′ end of the baboon intron matched exactly the human sequence. This element represents a nonfunctional variation of an estrogen response element found at the same location in the rat CaBP-9k gene. The rat element functions as an enhancer and mediates uterine and possibly placental CaBP-9k expression in the rat and probably most other mammals. The finding of a modified ERE in baboon as in human suggests that during primate evolution the expression of this mammalian-specific gene has been eliminated in uterus and placenta. This scenario raises the question of the role of CaBP-9k in these reproductive tissues. © 1995 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080400403
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of alternatively spliced human SP-10 mRNAs (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 41 (1995), S. 100-108 
    Details
    ISSN: 1040-452X
    Keywords: Sperm ; SP-10 ; Intra-acrosomal Quantitative competitive PCR ; Cryptic splicing ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Alternatively spliced mRNAs encoding the human intraacrosomal protein SP-10 were sought by the reverse transcriptase polymerase chain reaction (RTPCR). Eleven RTPCR products were identified, characterized, and found to represent authentic alternatively spliced SP-10 mRNAs. The 11 alternatively spliced SP-10 mRNAs encoded proteins ranging from 81 to 265 amino acids. The 10 smaller variants all resulted from one or two in-frame deletions in exons 2 and/or 3 of the SP-10 genomic sequence. Quantitative competitive RTPCR showed that the four largest SP-10 mRNAs represented the majority (〉99%) of the SP-10 message in testes from each of four men. The relative abundance of each of the four SP-10 mRNAs varied between individuals, but the longest SP-10 mRNA, SP10-1, which encoded a 265 amino acid protein, was consistently the most abundant, comprising 53-72% of the total SP-10 message. This was followed by the second largest SP-10 mRNA, SP10-2, which encoded a protein of 246 amino acids and comprised 15-32%. The third and fourth largest SP-10 mRNAs, SP10-3 and SP10-4, encoded proteins of 210 and 195 amino acids and accounted for 3.4-8.3% and 8.7-12.5% of the total SP-10 messages, respectively. The remaining 7 SP-10 mRNAs combined accounted for〈1% of the total SP-10 message. Within the low abundance group of mRNAs were two that deleted the entire third exon of SP-10. The present study suggests that phenomena of cryptic splicing and exon skipping occur within the SP-10 mRNA. Along with proteolysis, alternative splicing also helps to explain the heterogeneous forms of SP-10 that have been observed on Western blots of human sperm extracts. © 1995 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080410115
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of baboon and cynomolgus monkey intraacrosomal protein SP-10: Homology with human SP-10 and a mouse sperm antigen (MSA-63) (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Molecular Reproduction and Development 34 (1993), S. 140-148 
    Details
    ISSN: 1040-452X
    Keywords: Alternative splicing ; Polymerase chain reaction ; Sperm-specific protein ; Contraceptive vaccine ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this study, cDNAs encoding the intraacrosomal protein SP-10 were cloned and sequenced from baboon (Papio papio) and macaque (Macaca fasicularis) testis libraries and the sequence compared to that of human SP-10. Two alternatively spliced SP-10 cDNAs were obtained from both baboon and macaque testis libraries. The two cDNAs in each species contained open reading frames encoding proteins of exactly 285 and 251 amino acids. A 98% homology between baboon and macaque SP-10 was found at the protein and DNA levels. An 85% and 89% homology between baboon and macaque SP-10 and human SP-10 was present at the protein and DNA level, respectively. A mouse intraacrosomal protein, MSA-63, considered to be an SP-10 homologue, exhibited an overall 53% homology to nonhuman primate SP-10 and a 60% homology to human SP-10 at the protein level. Polymerase chain reaction analysis of testis mRNA confirmed the existence of two alternately spliced SP-10 mRNAs in both nonhuman primates. Primer extension analysis indicated a common major transcriptional start site in baboon, macaque, and human SP-10 67 nucleotides 5′ to the ATG codon. The amino acid sequence data for nonhuman primate SP-10s suggest that antibodies generated by vaccinating baboons and macaques with human SP-10 will likely recognize nonhuman primate SP-10, supporting the testing of an SP-10 contraceptive vaccine based on human SP-10 in these nonhuman primate models. © 1993 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/mrd.1080340205
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  • 6
    Electronic Resource
    Electronic Resource
    Physiological responses of hybridoma cells in a protein-free medium to soluble and immobilized antigen (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1155-1159 
    Details
    ISSN: 0006-3592
    Keywords: hybridoma cells ; monoclonal antibody production ; antigens ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: This study examined the effect of antigen in a protein free medium on cell growth and monoclonal antibody production by a hybridoma line. Antigen immobilized on a Sepharose gel matrix via a bovine γ-globulin carrier protein was used to stimulate the cell cultures in T-flasks. In comparison to antigen-free culture, total antibody production during was increased up to 40%, while slower cell growth rates were observed. The specific antibody production during the stationary culture phase was 40% to 80% higher in the presence of immobilized antigen. The surface density of antigen on the Sepharose beads had a strong influence on the physiological response of the hybridomas. © 1994 John Wiley & Sons, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260440917
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of vasectomy on the epididymis (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 30 (1995), S. 82-100 
    Details
    ISSN: 1059-910X
    Keywords: Vasectomy ; Epididymis ; Vas deferens ; Hydrostatic pressure ; Antisperm antibodies ; Spermatic granulomas ; Inflammation ; Lysosmes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Common principles can be discerned in the response of the epididymis to vasectomy, despite species differences. Increases in the size and number of lysosomes are the most frequent changes in the epididymal epithelium. The presence or absence of additional alterations such as changes in the height of the epithelium may be related to variations in distensibility of the vas deferens and epididymis. Direct measurements by micropuncture of epididymal and seminiferous tubule hydrostatic pressure indicate that, contrary to dogma, increased pressure in the distal epididymis after vasectomy is not generally transmitted to the seminiferous tubules. The epididymal interstitium shows microscopic changes indicative of chronic inflammation, with infiltration of macrophages, lymphocytes, and plasma cells, and rats with these lesions have higher antisperm antibody levels than animals lacking epididymal changes. Macrophages and neutrophils may enter the duct through the epididymal epithelium, at sites of rupture of the duct, and in the efferent ductules. Cyst-like spermatic granulomas occur in virtually all species where the epididymis or vas deferens ruptures with escape of spermatozoa. The sites and timing of granuloma formation may depend on the mechanical properties of the tract in different species, and they are probably important in the immune response to vasectomy. Postvasectomy sera in Lewis rats recognize a consensus repertoire of dominant autoantigens that closely resembles the antigens bound by sera from rats immunized with isologous spermatozoa. There are multiple routes for disposal of the sperm that continue to be produced after vasectomy. © 1995 Wiley-Liss, Inc.
    Additional Material: 19 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070300107
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  • 8
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of the major glycoprotein of epididymal fluid from the cauda in the epithelium of the mouse epididymis (1988)
    Springer
    Cell & tissue research 251 (1988), S. 603-610 
    Details
    ISSN: 1432-0878
    Keywords: Epididymis ; Protein secretion ; Immunocyto chemistry ; Mouse
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The most abundant protein in fluid from the mouse cauda epididymidis, designated CP 27, is a glycoprotein that migrates at approximately 27000 daltons on SDS-polyacrylamide gels. Samples of CP 27 were isolated by preparative gel electrophoresis and were used to raise a guinea-pig polyclonal antiserum, which reacted with a single band on western blots of caudal epididymal fluid. This antiserum was used for immunocytochemical localization of CP 27 in histological sections of mouse epididymis using the peroxidase-antiperoxidase and protein A-gold methods. The most proximal staining with anti-CP 27 was in segment 6 of the distal caput epididymidis, where the lumen and a portion of the supranuclear cytoplasm of principal cells were stained. In contrast, in the distal corpus and cauda epididymidis (segments 8–11), there was pronounced staining of the luminal contents, stereocilia, and scattered cells identified as the “light” cells of the epididymal epithelium. Although CP 27 was found in the epididymal lumen of all segments distal to segment 6, the intensity of staining appeared to decline distally in the cauda epididymidis. Control sections exposed to pre-immune serum instead of anti-CP 27 showed no reaction. The results suggest that CP 27, the major glycoprotein of cauda epididymal fluid, is synthesized by principal cells of segment 6 of the distal caput epididymidis. CP 27 may be among the substances absorbed from the lumen by the light cells of the distal epididymis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00214009
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  • 9
    Electronic Resource
    Electronic Resource
    Stage-specific detection of mRNA for the sperm antigen SP-10 in human testes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 236 (1993), S. 619-625 
    Details
    ISSN: 0003-276X
    Keywords: SP-10 antigen ; Acrosome ; In situ hybridization ; Seminiferous epithelium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: SP-10 is a sperm-specific, intra-acrosomal protein that is considered to be a vaccine candidate for immunocontraception. In the present study, in situ hybridization with biotin and 35S labeled riboprobes was used to determine the pattern of SP-10 mRNA expression in human testes. Both methods demonstrated SP-10 mRNA primarily in round spermatids found in stages I, II, and III of the seminiferous cycle. Morphometric analysis of silver grains with the 35S-labeled probe showed less SP-10 mRNA in spermatids at stages IV, V, and VI than in previous stages, and rarely was label found in spermatogonia or spermatocytes. The expression of SP-10 mRNA first appeared at stage I coincident with the appearance of the protein, which was shown previously to persist in the acrosomal matrix throughout spermiogenesis. The decrease in SP-10 mRNA occurred when spermatids underwent polarization, nuclear condensation, and elongation. The appearance of SP-10 mRNA in round spermatids suggest that increases in SP-10 transcription or SP-10 mRNA stability or both occur as spermatids develop from the Golgi phase to the cap phase. The subsequent decline of SP-10 mRNA, despite the persistence of the SP-10 protein in all spermatids, suggests that a decrease in SP-10 transcription or an increase in mRNA degradation occurs when spermatids elongate. © 1993 Wiley-Liss, Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092360405
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  • 10
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of the 9-kilodalton vitamin d-dependent calcium-binding protein in the murine intraplacental yolk sac (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    The @Anatomical Record 222 (1988), S. 252-259 
    Details
    ISSN: 0003-276X
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: The calcium-binding protein (CaBP) calbindin has been implicated in the molecular mechanism of placental calcium transfer. Previous light microscopic studies have identified CaBP in visceral (but not parietal) endodermal cells of the yolk sac with the most intense immunocytochemical signal observed in the intraplacental yolk sac. In the present studies, electron microscopy was used to study the localization of CaBP in placenta.Placentas of 17-day pregnant mice were fixed by perfusion in 0.5% gluteraldehyde, embedded in low-temperature Lowicryl K4M, and examined in thin section for specific labeling with a polyclonal antiserum. Antibody to CaBP was localized by using protein A-gold particles which were quantified for subcellular compartmentation by using a Videoplan computer system. A high signal for CaBP was found in the visceral endodermal cells of the intraplacental yolk sac. In these cells, gold particles indicating the location of CaBP were observed over (1) the cytoplasmic matrix where the average number of gold particles per μm2 was 33; (2) the microvilli (17/μm2); (3) the mitochondria (17/μm2); and (4) the nucleus (43/μm2). Sections from antigen-absorbed controls, by contrast, showed few gold particles: cytosol, 2/μm2; microvilli, 5/μm2; mitochondria, 5/μm2; and nucleus, 4/μm2. Electron-lucent profiles of the Golgi and endoplasmic reticulum contained no particles in the controls and a low particle count (4/μm2) in the stained sections. Parietal endodermal cells of the intraplacental yolk sac showed a relatively low signal for CaBP compared with the visceral endodermal cells (5 particles/μm2 vs. 39). Only low numbers of gold particles were observed in trophoblasts (6/μm2), lymphocytes (5/μm2), and erythrocytes (5/μm2). These findings indicate that 9 kd CaBP is located predominantly in cytoplasmic matrix, nucleus, and mitochondria within the visceral endodermal cells of the intraplacental yolk sac.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ar.1092220306
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