Browsing by Author "Ortíz Scarlazetta, María Elena"

Now showing 1 - 9 of 9
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    Concanavalin-A Induces Granulosa Cell Death and Inhibits FSH-Mediated Follicular Growth and Ovarian Maturation in Female Rats
    (2013) Velásquez Opazo, Ethel Virginia; Ríos Raggio, Mariana; Ortíz Scarlazetta, María Elena; Lizama, Carlos; Orge, Felipe; Oliva, Barbara; Orellana Walden, Renán Felipe; Villalón, Manuel J.; Moreno Mauro, Ricardo D.; Owen, Gareth Ivor; Núñez, Elizabeth; Abramovich, Dalhia; Tesone, Marta, Rokka, Anne; Corthals, Garry; Croxatto A., Horacio; Parborell, Fernanda
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    Differential transport of fertilized and unfertilized eggs
    (1991) Carvajal C., Jorge A.; Croxatto A., Horacio; Ortíz Scarlazetta, María Elena
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    Early fitness consequences and hormonal correlates of parental behaviour in the social rodent, Octodon degus
    (2010) Ebensperger Pesce, Luis Alberto; Ramírez Otarola, Natalia Nicole.; León Letelier, Cecilia Alejandra; Ortíz Scarlazetta, María Elena
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    Growth, mortality and recruitment of the yellow clam Mesodesma mactroides on Uruguayan beaches
    (1992) Castilla, Juan Carlos; Ortíz Scarlazetta, María Elena
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    Hormonal control of ovum transport through the rat oviduct
    (1991) Cardenas, Hugo.; Croxatto A., Horacio; Forcelledo Hospital, M. Luisa; Noe Echeverría, Gabriela; Ortíz Scarlazetta, María Elena
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    Importance of uterine expulsion of embryos in the interceptive mechanism of postcoital oestradiol in rats
    (1991) Bastías, Gabriel; Croxatto A., Horacio; Ortíz Scarlazetta, María Elena
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    In vivo postprandial bioavailability of interesterified-lipids in sodium-caseinate or chitosan based O/W emulsions
    (2015) Farfán Martínez, Mariel; Villalón, Manuel J.; Ortíz Scarlazetta, María Elena; Bouchon Aguirre, Pedro Alejandro
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    The effect of interesterification on the bioavailability of fatty acids in structured lipids
    (2013) Farfán Martínez, Mariel; Villalón, Manuel J.; Ortíz Scarlazetta, María Elena; Bouchon Aguirre, Pedro Alejandro
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    Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
    (2003) Hey, Neil A.; Ortíz Scarlazetta, María Elena; Meseguer, Marcos.; Simón, Carlos.; Smorodinsky, Nechama I.; Wreschner, Daniel H.; Aplin, John D.
    Abstract The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.Abstract The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.Abstract The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.Abstract The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.Abstract The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.