2019, Number 1
General aspects of cholesterol transport in the steroidogenesis of the human placenta
Language: Spanish
References: 73
Page: 1-9
PDF size: 399.65 Kb.
ABSTRACT
The human placenta requires cholesterol to synthesize the progesterone that maintains the relationship between the fetus and the mother, which allows it to successfully conclude pregnancy. The placenta incorporates cholesterol through the LDL obtained from the maternal blood stream by a mechanism of endocytosis. Endosomes formed by this process degrade the LDL, bind several proteins forming the late endosomes and releasing the cholesterol to syncytiotrophoblast mitochondria to transform it into pregnenolone and then, into progesterone. The soluble attachment proteins denominated SNARE participates in the transport of cholesterol in specific contact sites where the mitochondrial proteins responsible for steroidogenesis are located.REFERENCES
Alpy, F., Rousseau, A., Schwab, Y., Legueux, F., Stoll, I., Wendling, C., Spiegelhalter, C., Kessler, P., Mathelin, C., Rio, M.C., Levine, T.P. & Tomasetto, C. (2013). STARD3 or STARD3NL and VAP form a novel molecular tether between late endosomes and the ER. J. Cell Sci., 126, 5500–5512. DOI: 10.1242/jcs.139295.
Bhattacharjee, J., Ietta, F., Romagnoli, R., Bechi, N., Caniggia, I. & Paulesu, L. (2012). ABC transporters in human placenta and their role in maternal-fetal cholesterol transfer: ABCA1 candidate target. En Jing Zheng (Ed.). Recent Advances in Research on the Human Placenta (pp. 336-354).London: IntechOpen. ISBN 978-953-51- 0194-9 DOI: 10.5772/1211.
Bianco-Miotto, T., Blundell, C., Buckberry, S., Chamley, L., Chong, S., Cottrell, E., Dawson, P., Hanna, C., Holland, O., Lewis, R.M., Moritz, K., Myatt, L., Perkins, A.V., Powell, T., Saffery, R., Sferruzzi-Perri, A., Sibley, C., Simmons, D. & O’Tierney-Ginn, P.F. (2016). IFPA meeting 2015 workshop report I: Placental mitochondrial function, transport systems and epigenetics. Placenta, 48, Suppl. 1, Trophoblast Res., 30, S3-S6. DOI: 10.1016/j. placenta.2015.11.014. 10. Bose, M., Whittal, R.M., Miller, W.L. & Bose, H.S. (2008). Steroidogenic activity of StAR requires contact with mitochondrial VDAC1 and phosphate carrier protein. J. Biol. Chem., 283, 8837–8845. DOI: 10.1074/jbc. M709221200.
Esparza-Perusquía, M., Olvera-Sánchez, S., Flores-Herrera, O., Flores-Herrera, H., Guevara-Flores, A., Pardo, J.P., Espinosa-García, M.T. & Martínez, F. (2015). Mitochondrial proteases act on STARD3 to activate progesterone synthesis in human syncytiotrophoblast. Biochim. Biophys. Acta, 1850(1), 107-117. DOI: 10.1016/j.bbagen.2014.10.009.
Pagler, T.A., Golsabahi, S., Doringer, M., Rhode, S., Schutz, G.J., Pavelka, M., Wadsack, C., Gauster, M., Lohninger, A., Laggner, H., Strobl, W. & Stangl, H. (2006). A Chinese hamster ovarian cell line imports cholesterol by high density lipoprotein degradation. J. Biol. Chem., 281, 38159-38171. DOI: 10.1074/jbc.M603334200
Poderoso, C., Duarte, A., Cooke, M., Orlando, U., Gottifredi, V., Solano, A.R. Lemos, J.R. & Podestá, E.J. (2013). The spatial and temporal regulation of the hormonal signal. Role of mitochondria in the formation of a protein complex required for the activation of cholesterol transport and steroids synthesis. Mol. Cell. Endocrinol., 371, 26–33. DOI: 10.1016/j.mce.2012.12.024.
Rajapaksha, M., Kaur, J., Prasad, M., Pawlak, K.J., Marshall, B., Perry, E.W., Whittal, R.M. & Bose, H.S. (2016). An outer mitochondrial translocase, Tom22, is crucial for inner mitochondrial steroidogenic regulation in adrenal and gonadal tissues. Mol. Cell Biol., 36(6), 1032-1047. DOI: 10.1128/MCB.01107-15;
Tu, L.N., Morohaku, K., Manna, P.R., Pelton, S.H., Butler, W.R., Stocco, D.M. & Selvaraj, V. (2014). Peripheral benzodiazepine receptor/translocator protein global knock-out mice are viable with no effects on steroid hormone biosynthesis. J. Biol. Chem., 289, 40, 27444– 27454. DOI: 10.1074/jbc.M114.578286.
Watari, H., Arakane, F., Moog-Lutz, C., Kallen, C.B., Tomasetto, C., Gerton, G.L., Rio, M.C., Baker, M.E. & Strauss, J.F. 3rd. (1997). MLN64 contains a domain with homology to the steroidogenic acute regulatory protein (StAR) that stimulates steroidogenesis. Proc. Natl. Acad. Sci. USA, 94(16), 8462-8467doi.org/10.1073/ pnas.94.16.8462