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Expression and localization of urokinase-type plasminogen activator receptor in bovine cumulus–oocyte complexes

Published online by Cambridge University Press:  05 May 2015

Daniela C. García
Affiliation:
Instituto Superior de Investigaciones Biológicas (INSIBIO), CONICET-UNT, San Miguel de Tucumán, Argentina.
Dora C. Miceli
Affiliation:
Instituto Superior de Investigaciones Biológicas (INSIBIO), CONICET-UNT, San Miguel de Tucumán, Argentina. Instituto de Biología ‘Dr. Francisco D. Barbieri’, Facultad de Bioquímica, Química y Farmacia, UNT, Chacabuco 461, T4000ILI – San Miguel de Tucumán, Argentina.
Gabriela Rizo
Affiliation:
Instituto Superior de Investigaciones Biológicas (INSIBIO), CONICET-UNT, San Miguel de Tucumán, Argentina. Instituto de Biología ‘Dr. Francisco D. Barbieri’, Facultad de Bioquímica, Química y Farmacia, UNT, Chacabuco 461, T4000ILI – San Miguel de Tucumán, Argentina.
Elina V. García
Affiliation:
Instituto Superior de Investigaciones Biológicas (INSIBIO), CONICET-UNT, San Miguel de Tucumán, Argentina. Instituto de Biología ‘Dr. Francisco D. Barbieri’, Facultad de Bioquímica, Química y Farmacia, UNT, Chacabuco 461, T4000ILI – San Miguel de Tucumán, Argentina.
Pablo A. Valdecantos
Affiliation:
Instituto de Biología ‘Dr. Francisco D. Barbieri’, Facultad de Bioquímica, Química y Farmacia, UNT, Chacabuco 461, T4000ILI – San Miguel de Tucumán, Argentina.
Mariela Roldán-Olarte
Affiliation:
Instituto de Biología ‘Dr. Francisco D. Barbieri’, Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, T4000ILI – San Miguel de Tucumán, Argentina. Instituto Superior de Investigaciones Biológicas (INSIBIO), CONICET-UNT, San Miguel de Tucumán, Argentina.
Corresponding

Summary

Urokinase-type plasminogen activator (uPA) is a serine protease involved in extracellular matrix remodeling through plasmin generation. uPA usually binds to its receptor, uPAR, which is anchored to the plasma membrane through a glycosylphosphatidylinositol anchor. uPA/uPAR binding increases proteolytic activity in the neighborhood of the cells containing uPAR and activates intracellular signaling pathways involved in extracellular matrix remodeling, cell migration and proliferation. The aim of this work was to study the expression of uPA, uPAR and plasminogen activator inhibitor-1 (PAI-1) in immature and in vitro matured bovine cumulus–oocyte complexes (COCs). uPA is only expressed in the cumulus cells of immature and in vitro matured COCs, while uPAR and PAI-1 are expressed in both the cumulus cells and the immature and in vitro matured oocytes. In addition, uPAR protein was localized by confocal microscopy in the plasma membrane of oocytes and cumulus cells of immature COCs. Results from this research led us to hypothesize that the uPA/uPAR interaction could cause the local production of uPA-mediated plasmin over oocyte and cumulus cell surface; plasmin formation could also be regulated by PAI-1.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2015 

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References

Bieser, B., Stojkovic, M., Wolf, E., Meyer, H. & Einspanier, R. (1998). Growth factors and components for extracellular proteolysis are differentially expressed during in vitro maturation of bovine cumulus-oocyte complexes. Biol. Reprod. 59, 801–6.CrossRefGoogle ScholarPubMed
Blasi, F. & Sidenius, N. (2010). The urokinase receptor: focused cell surface proteolysis, cell adhesion and signaling. FEBS Lett. 584, 1923–30.CrossRefGoogle ScholarPubMed
Coy, P., Jiménez-Movilla, M., García-Vázquez, F. A., Mondéjar, I., Grullón, L. & Romar, R. (2012). Oocytes use the plasminogen-plasmin system to remove supernumerary spermatozoa. Hum. Reprod. 27, 1985–93.CrossRefGoogle ScholarPubMed
D’Alessandris, C., Canipari, R., Di Giacomo, M., Epifano, O., Camaioni, A., Siracusa, G. & Salustri, A. (2001). Control of mouse cumulus cell-oocyte complex integrity before and after ovulation: plasminogen activator synthesis and matrix degradation. Endocrinology 142, 3033–40.CrossRefGoogle ScholarPubMed
Dass, K., Ahmad, A., Azmi, A.S., Sarkar, S.H. & Sarkar, F.H. (2008). Evolving role of uPA/uPAR system in human cancers. Cancer Treat. Rev. 34, 122–36.CrossRefGoogle ScholarPubMed
Funahashi, H., Ekwall, H., Kikuchi, K. & Rodriguez-Martinez, H. (2001). Transmission electron microscopy studies of the zona reaction in pig oocytes fertilized in vivo and in vitro . Reproduction 122, 443–52.CrossRefGoogle ScholarPubMed
Huarte, J., Vassalli, J. D., Belin, D. & Sakkas, D. (1993). Involvement of the plasminogen activator/plasmin proteolytic cascade in fertilization. Dev. Biol. 157, 539–46.CrossRefGoogle ScholarPubMed
Jiménez-Díaz, M., Roldán, M. & Miceli, D.C. (2002). Localization of plasminogen in the extracellular matrix of hamster eggs: exogenous activation by streptokinase. Mol. Reprod. Dev. 61, 528–35.CrossRefGoogle ScholarPubMed
Kouba, A.J., Alvarez, I.M. & Buhi, W.C. (2000). Identification and localization of plasminogen activator inhibitor-1 within the porcine oviduct. Biol. Reprod. 62, 501–10.CrossRefGoogle ScholarPubMed
Liu, Y.X., Liu, X.M., Nin, L.F., Shi, L. & Chen, S.R. (2013). Serine protease and ovarian paracrine factors in regulation of ovulation. Front. Biosci. (Landmark Ed.) 18, 650–64.CrossRefGoogle ScholarPubMed
Lu, C.H., Lee, R.K., Hwu, Y.M., Lin, M.H., Yeh, L.Y., Chen, Y.J., Lin, S.P. & Li, S.H. (2013). Involvement of the serine protease inhibitor, SERPINE2, and the urokinase plasminogen activator in cumulus expansion and oocyte maturation. PLoS One 8, e74602.CrossRefGoogle ScholarPubMed
Martínez-Hernández, M.G., Baiza-Gutman, L.A., Castillo-Trápala, A. & Armant, D.R. (2011). Regulation of proteinases during mouse peri-implantation development: urokinase-type plasminogen activator expression and cross talk with matrix metalloproteinase 9. Reproduction 141, 227–39.CrossRefGoogle ScholarPubMed
Mondéjar, I., Acuña, O.S., Izquierdo-Rico, M.J., Coy, P. & Avilés, M. (2012a). The oviduct: functional genomic and proteomic approach. Reprod. Domest. Anim. 47 (Suppl. 3), 22–9.CrossRefGoogle Scholar
Mondéjar, I., Grullón, L.A., García-Vázquez, F.A., Romar, R. & Coy, P. (2012b). Fertilization outcome could be regulated by binding of oviductal plasminogen to oocytes and by releasing of plasminogen activators during interplay between gametes. Fertil. Steril. 97, 453–61.CrossRefGoogle ScholarPubMed
Ny, T., Wahlberg, P. & Brandstrom, I.J. (2002). Matrix remodeling in the ovary: regulation and functional role of the plasminogen activator and matrix metalloproteinase systems. Mol. Cell. Endocrinol. 187, 2938.CrossRefGoogle ScholarPubMed
Papanikolaou, T., Amiridis, G.S., Dimitriadis, I., Vainas, E. & Rekkas, C.A. (2008). Effect of plasmin, plasminogen activators and a plasmin inhibitor on bovine in vitro embryo production. Reprod. Fertil. Dev. 20, 320–7.CrossRefGoogle Scholar
Park, K.W., Choi, S.H., Song, X.X., Funahashi, H. & Niwa, K. (1999). Production of plasminogen activators (PAs) in bovine cumulus-oocyte complexes during maturation in vitro: effects of epidermal growth factor on production of PAs in oocytes and cumulus cells. Biol. Reprod. 61, 298304.CrossRefGoogle ScholarPubMed
Rekkas, C.A., Besenfelder, U., Havlicek, V., Vainas, E. & Brem, G. (2002). Plasminogen activator activity in cortical granules of bovine oocytes during in vitro maturation. Theriogenology 57, 1897–905.CrossRefGoogle ScholarPubMed
Roldán-Olarte, M., García, D.C., Jiménez-Díaz, M., Valdecantos, P.A. & Miceli, D.C. (2012). In vivo and in vitro expression of the plasminogen activators and urokinase type plasminogen activator receptor (uPAR) in the pig oviduct. Anim. Reprod. Sci. 136, 90–9.CrossRefGoogle Scholar
Roldán-Olarte, M., Jiménez-Díaz, M. & Miceli, D.C. (2005). Plasminogen detection in oocytes and plasminogen activator activities in the porcine oviduct during the estrous cycle. Zygote 13, 115–23.CrossRefGoogle ScholarPubMed
Smith, H.W. & Marshall, C.J. (2010). Regulation of cell signalling by u-PAR. Nat. Rev. Mol. Cell. Biol. 11, 2336.CrossRefGoogle Scholar
Zhang, X., Kidder, G.M., Zhang, C., Khamsi, F. & Armstrong, D.T. (1994). Expression of plasminogen activator genes and enzymatic activities in rat preimplantation embryos. J. Reprod. Fertil. 101, 235–40.CrossRefGoogle Scholar
Zhang, X., Rutledge, J., Khamsi, F. & Armstrong, D.T. (1992). Release of tissue-type plasminogen activator by activated rat eggs and its possible role in the zona reaction. Mol. Reprod. Dev. 32, 2832.CrossRefGoogle Scholar
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