Activated translation signaling in placenta from pregnant women with gestational diabetes mellitus: Possible role of leptin

Placentas from gestational diabetes (GDM) suffer from structural and functional changes including overgrowth. That is why we aimed to study [ 3H]-leucine incorporation into protein in addition to translation signaling in placenta from GDM. Thus, we investigated the expression of leptin and leptin re...

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Autor principal: Pérez-Pérez, A.
Otros Autores: Maymó, J.L, Gambino, Y.P, Guadix, P., Dueñas, J.L, Varone, C.L, Sánchez-Margalet, V.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2013
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Acceso en línea:Registro en Scopus
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024 7 |2 cas  |a leucine, 61-90-5, 7005-03-0; Leptin; Receptors, Leptin 
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100 1 |a Pérez-Pérez, A. 
245 1 0 |a Activated translation signaling in placenta from pregnant women with gestational diabetes mellitus: Possible role of leptin 
260 |c 2013 
270 1 0 |m Sánchez-Margalet, V.; Department Medical Biochemistry and Molecular Biology, School of Medicine, Virgen Macarena University Hospital, Av. Dr. Fedriani 3, Sevilla 41071, Spain; email: margalet@us.es 
506 |2 openaire  |e Política editorial 
504 |a Gabbe, S.G., Gestational diabetes mellitus (1986) N Engl J Med, 315, pp. 1025-1026 
504 |a Barnes-Powell, L.L., Infants of diabetic mothers: The effects of hyperglycemia on the fetus and neonate (2007) Neonatal Netw, 26, pp. 283-290 
504 |a Jahan, S., Ahmed, C.M., Zinnat, R., Hasan, Z., Habib, S.H., Saha, S., Ali, L., Influence of maternal diabetes on serum leptinemic and insulinemic status of the offspring: A case study of selected patients in a tertiary care hospital in Bangladesh (2011) Diabetes Metab Syndr, 5, pp. 33-37 
504 |a Hagbard, L., Svanborg, A., Prognosis of diabetes mellitus with onset during pregnancy. A clinical study of seventy-one cases (1960) Diabetes, 9, pp. 296-302 
504 |a Kjos, S.L., Peters, R.K., Xiang, A., Henry, O.A., Montoro, M., Buchanan, T.A., Predicting future diabetes in Latino women with gestational diabetes. Utility of early postpartum glucose tolerance testing (1995) Diabetes, 44, pp. 586-591 
504 |a O'Sullivan, J.B., Body weight and subsequent diabetes mellitus (1982) JAMA, 248, pp. 949-952 
504 |a Guibourdenche, J., Porquet, D., Evain-Brion, D., Placental hormones and fetal growth (2001) Gynecol Obstet Fertil, 29, pp. 532-533 
504 |a Perez-Perez, A., Maymo, J., Duenas, J.L., Goberna, R., Calvo, J.C., Varone, C., Sanchez-Margalet, V., Leptin prevents apoptosis of trophoblastic cells by activation of MAPK pathway (2008) Arch Biochem Biophys, 477, pp. 390-395 
504 |a Perez-Perez, A., Gambino, Y., Maymo, J., Goberna, R., Fabiani, F., Varone, C., Sanchez-Margalet, V., MAPK and PI3K activities are required for leptin stimulation of protein synthesis in human trophoblastic cells (2010) Biochem Biophys Res Commun, 396, pp. 956-960 
504 |a Gambino, Y.P., Maymo, J.L., Perez-Perez, A., Duenas, J.L., Sanchez-Margalet, V., Calvo, J.C., Varone, C.L., 17Beta-Estradiol Enhances Leptin Expression in Human Placental Cells Through Genomic and Nongenomic Actions (2010) Biol Reprod, 83, pp. 42-51 
504 |a Maymo, J.L., Perez, P.A., Sanchez-Margalet, V., Duenas, J.L., Calvo, J.C., Varone, C.L., Upregulation of placental leptin by human chorionic gonadotropin (2009) Endocrinology, 150, pp. 304-313 
504 |a Maymo, J.L., Perez, P.A., Duenas, J.L., Calvo, J.C., Sanchez-Margalet, V., Varone, C.L., Regulation of placental leptin expression by cyclic adenosine 5′-monophosphate involves cross talk between protein kinase A and mitogen-activated protein kinase signaling pathways (2010) Endocrinology, 151, pp. 3738-3751 
504 |a Magarinos, M.P., Sanchez-Margalet, V., Kotler, M., Calvo, J.C., Varone, C.L., Leptin promotes cell proliferation and survival of trophoblastic cells (2007) Biol Reprod, 76, pp. 203-210 
504 |a Ericsson, A., Saljo, K., Sjostrand, E., Jansson, N., Prasad, P.D., Powell, T.L., Jansson, T., Brief hyperglycaemia in the early pregnant rat increases fetal weight at term by stimulating placental growth and affecting placental nutrient transport (2007) J Physiol, 581, pp. 1323-1332 
504 |a Taricco, E., Radaelli, T., Nobile De Santis, M.S., Cetin, I., Foetal and placental weights in relation to maternal characteristics in gestational diabetes (2003) Placenta, 24, pp. 343-347 
504 |a Briana, D.D., Malamitsi-Puchner, A., Reviews: Adipocytokines in normal and complicated pregnancies (2009) Reprod Sci, 16, pp. 921-937 
504 |a Proud, C.G., Denton, R.M., Molecular mechanisms for the control of translation by insulin (1997) Biochem J, 328, pp. 329-341 
504 |a Perez-Perez, A., Maymo, J., Gambino, Y., Duenas, J.L., Goberna, R., Varone, C., Sanchez-Margalet, V., Leptin stimulates protein synthesis-activating translation machinery in human trophoblastic cells (2009) Biol Reprod, 81, pp. 826-832 
504 |a Lin, T.A., Kong, X., Haystead, T.A., Pause, A., Belsham, G., Sonenberg, N., Lawrence, Jr.J.C., PHAS-I as a link between mitogen-activated protein kinase and translation initiation (1994) Science, 266, pp. 653-656 
504 |a Kleijn, M., Scheper, G.C., Voorma, H.O., Thomas, A.A., Regulation of translation initiation factors by signal transduction (1998) Eur J Biochem, 253, pp. 531-544 
504 |a Minich, W.B., Balasta, M.L., Goss, D.J., Rhoads, R.E., Chromatographic resolution of in vivo phosphorylated and nonphosphorylated eukaryotic translation initiation factor eIF-4E: Increased cap affinity of the phosphorylated form (1994) Proc Natl Acad Sci USA, 91, pp. 7668-7672 
504 |a Chung, J., Grammer, T.C., Lemon, K.P., Kazlauskas, A., Blenis, J., PDGF- and insulin-dependent pp70S6k activation mediated by phosphatidylinositol-3-OH kinase (1994) Nature, 370, pp. 71-75 
504 |a Pullen, N., Dennis, P.B., Andjelkovic, M., Dufner, A., Kozma, S.C., Hemmings, B.A., Thomas, G., Phosphorylation and activation of p70s6k by PDK1 (1998) Science, 279, pp. 707-710 
504 |a Carlberg, U., Nilsson, A., Nygard, O., Functional properties of phosphorylated elongation factor 2 (1990) Eur J Biochem, 191, pp. 639-645 
504 |a Ryazanov, A.G., Shestakova, E.A., Natapov, P.G., Phosphorylation of elongation factor 2 by EF-2 kinase affects rate of translation (1988) Nature, 334, pp. 170-173 
504 |a Schmittgen, T.D., Livak, K.J., Analyzing real-time PCR data by the comparative C(T) method (2008) Nat Protoc, 3, pp. 1101-1108 
504 |a Lepercq, J., Cauzac, M., Lahlou, N., Timsit, J., Girard, J., Auwerx, J., Hauguel-De, M.S., Overexpression of placental leptin in diabetic pregnancy: A critical role for insulin (1998) Diabetes, 47, pp. 847-850 
504 |a Uzelac, P.S., Li, X., Lin, J., Neese, L.D., Lin, L., Nakajima, S.T., Bohler, H., Lei, Z., Dysregulation of leptin and testosterone production and their receptor expression in the human placenta with gestational diabetes mellitus (2010) Placenta, 31, pp. 581-588 
504 |a Martin-Romero, C., Sanchez-Margalet, V., Human leptin activates PI3K and MAPK pathways in human peripheral blood mononuclear cells: Possible role of Sam68 (2001) Cell Immunol, 212, pp. 83-91 
504 |a Sanchez-Margalet, V., Goldfine, I.D., Vlahos, C.J., Sung, C.K., Role of phosphatidylinositol-3-kinase in insulin receptor signaling: Studies with inhibitor, LY294002 (1994) Biochem Biophys Res Commun, 204, pp. 446-452 
504 |a Boileau, P., Cauzac, M., Pereira, M.A., Girard, J., Hauguel-De, M.S., Dissociation between insulin-mediated signaling pathways and biological effects in placental cells: Role of protein kinase B and MAPK phosphorylation (2001) Endocrinology, 142, pp. 3974-3979 
504 |a Pullen, N., Thomas, G., The modular phosphorylation and activation of p70s6k (1997) FEBS Lett, 410, pp. 78-82 
504 |a Jansson, N., Greenwood, S.L., Johansson, B.R., Powell, T.L., Jansson, T., Leptin stimulates the activity of the system A amino acid transporter in human placental villous fragments (2003) J Clin Endocrinol Metab, 88, pp. 1205-1211 
504 |a Masuzaki, H., Ogawa, Y., Sagawa, N., Hosoda, K., Matsumoto, T., Mise, H., Nishimura, H., Nakao, K., Nonadipose tissue production of leptin: Leptin as a novel placenta-derived hormone in humans (1997) Nat Med, 3, pp. 1029-1033 
504 |a Bajoria, R., Sooranna, S.R., Ward, B.S., Chatterjee, R., Prospective function of placental leptin at maternal-fetal interface (2002) Placenta, 23, pp. 103-115 
504 |a Ambrosini, G., Nath, A.K., Sierra-Honigmann, M.R., Flores-Riveros, J., Transcriptional activation of the human leptin gene in response to hypoxia. Involvement of hypoxia-inducible factor 1 (2002) J Biol Chem, 277, pp. 34601-34609 
504 |a Meissner, U., Ostreicher, I., Allabauer, I., Rascher, W., Dotsch, J., Synergistic effects of hypoxia and insulin are regulated by different transcriptional elements of the human leptin promoter (2003) Biochem Biophys Res Commun, 303, pp. 707-712 
504 |a Najib, S., Sanchez-Margalet, V., Human leptin promotes survival of human circulating blood monocytes prone to apoptosis by activation of p42/44 MAPK pathway (2002) Cell Immunol, 220, pp. 143-149 
504 |a Santos-Alvarez, J., Goberna, R., Sanchez-Margalet, V., Human leptin stimulates proliferation and activation of human circulating monocytes (1999) Cell Immunol, 194, pp. 6-11 
504 |a Meissner, U., Spranger, R., Lehner, M., Allabauer, I., Rascher, W., Dotsch, J., Hypoxia-induced leptin production in human trophoblasts does not protect from apoptosis (2005) Eur J Endocrinol, 153, pp. 455-461 
504 |a Sanchez-Margalet, V., Martin-Romero, C., Human leptin signaling in human peripheral blood mononuclear cells: Activation of the JAK-STAT pathway (2001) Cell Immunol, 211, pp. 30-36 
504 |a Desoye, G., Hauguel-De, M.S., The human placenta in gestational diabetes mellitus. The insulin and cytokine network (2007) Diabetes Care, 30, pp. S120-S126. , 02 
504 |a Yung, H.W., Calabrese, S., Hynx, D., Hemmings, B.A., Cetin, I., Charnock-Jones, D.S., Burton, G.J., Evidence of placental translation inhibition and endoplasmic reticulum stress in the etiology of human intrauterine growth restriction (2008) Am J Pathol, 173, pp. 451-462 
520 3 |a Placentas from gestational diabetes (GDM) suffer from structural and functional changes including overgrowth. That is why we aimed to study [ 3H]-leucine incorporation into protein in addition to translation signaling in placenta from GDM. Thus, we investigated the expression of leptin and leptin receptor (LEPR), as well as the activation state of signaling proteins regulating protein synthesis, such as mTOR, S6 Kinase, EIF4E-BP1, EIF4E, and eEF2 by measuring protein phosphorylation by immunoblot. [ 3H]-Leucine incorporation into protein also was determined in trophoblastic placenta explants from GDM and control pregnancy. We found that leptin and LEPR expression are increased in placentas from GDM and the translation machinery activity as well as [3H]-leucine incorporation into protein were higher in placentas from GDM compared with placentas from control pregnancy. In conclusion, protein synthesis rate is increased in placenta from GDM patients, and this may be due, at least in part, by the activation of translation signaling. The increased expression of leptin and LEPR may contribute to these effects. These results may provide a possible mechanism for the previously observed increase in placenta growth in GDM.  |l eng 
593 |a Departamento de Bioquímica Médica y Biología Molecular, Hospital Universitario Virgen Macarena, Universidad de Sevilla, Spain 
593 |a Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina 
593 |a Servicio de Ginecología y Obstetricia, Hospital Universitario Virgen Macarena, Universidad de Sevilla, Spain 
690 1 0 |a EIF4EBP1 
690 1 0 |a GESTATIONAL DIABETES 
690 1 0 |a LEPR 
690 1 0 |a LEPTIN 
690 1 0 |a MTOR 
690 1 0 |a TRANSLATION 
690 1 0 |a TROPHOBLASTIC CELLS 
690 1 0 |a INITIATION FACTOR 4E 
690 1 0 |a LEPTIN 
690 1 0 |a LEPTIN RECEPTOR 
690 1 0 |a LEUCINE 
690 1 0 |a MAMMALIAN TARGET OF RAPAMYCIN 
690 1 0 |a S6 KINASE 
690 1 0 |a TRANSCRIPTION FACTOR E2F1 
690 1 0 |a ADULT 
690 1 0 |a ARTICLE 
690 1 0 |a CLINICAL ARTICLE 
690 1 0 |a CONTROLLED STUDY 
690 1 0 |a EXPLANT 
690 1 0 |a FEMALE 
690 1 0 |a HUMAN 
690 1 0 |a IMMUNOBLOTTING 
690 1 0 |a PREGNANCY DIABETES MELLITUS 
690 1 0 |a PREGNANT WOMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN EXPRESSION 
690 1 0 |a PROTEIN PHOSPHORYLATION 
690 1 0 |a PROTEIN SYNTHESIS 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a ADULT 
690 1 0 |a CASE-CONTROL STUDIES 
690 1 0 |a DIABETES, GESTATIONAL 
690 1 0 |a FEMALE 
690 1 0 |a HUMANS 
690 1 0 |a LEPTIN 
690 1 0 |a PREGNANCY 
690 1 0 |a RECEPTORS, LEPTIN 
690 1 0 |a SIGNAL TRANSDUCTION 
690 1 0 |a YOUNG ADULT 
650 1 7 |2 spines  |a PLACENTA 
650 1 7 |2 spines  |a PLACENTA 
700 1 |a Maymó, J.L. 
700 1 |a Gambino, Y.P. 
700 1 |a Guadix, P. 
700 1 |a Dueñas, J.L. 
700 1 |a Varone, C.L. 
700 1 |a Sánchez-Margalet, V. 
773 0 |d 2013  |g v. 45  |h pp. 436-442  |k n. 6  |p Horm. Metab. Res.  |x 00185043  |t Hormone and Metabolic Research 
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856 4 0 |u https://doi.org/10.1055/s-0032-1333276  |y DOI 
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