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Potential Mechanisms of Exercise in Gestational Diabetes

DOI: 10.1155/2013/285948

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Abstract:

Gestational diabetes mellitus (GDM) is defined as glucose intolerance first diagnosed during pregnancy. This condition shares same array of underlying abnormalities as occurs in diabetes outside of pregnancy, for example, genetic and environmental causes. However, the role of a sedentary lifestyle and/or excess energy intake is more prominent in GDM. Physically active women are less likely to develop GDM and other pregnancy-related diseases. Weight gain in pregnancy causes increased release of adipokines from adipose tissue; many adipokines increase oxidative stress and insulin resistance. Increased intramyocellular lipids also increase cellular oxidative stress with subsequent generation of reactive oxygen species. A well-planned program of exercise is an important component of a healthy lifestyle and, in spite of old myths, is also recommended during pregnancy. This paper briefly reviews the role of adipokines in gestational diabetes and attempts to shed some light on the mechanisms by which exercise can be beneficial as an adjuvant therapy in GDM. In this regard, we discuss the mechanisms by which exercise increases insulin sensitivity, changes adipokine profile levels, and boosts antioxidant mechanisms. 1. Introduction Gestational diabetes mellitus (GDM) is the most prevalent metabolic disorder during pregnancy and is defined as glucose intolerance of variable severity that is first diagnosed during pregnancy and usually resolves not long after delivery [1, 2]. This definition includes any degree of glucose intolerance from just impaired to frankly diabetic [3]. Resolution of the condition is also important when differentiating between previously undiagnosed type 2 diabetes and GDM [4]. Insulin resistance, due to a series of hormonal changes, contributes to decreased blood glucose uptake by muscles [5]. This phenomenon seems to be important from an evolutionary point of view, as it ensures adequate glucose supply for fetal growth and development. In the third trimester a healthy pregnant woman has to increase her insulin secretion by 2–4 times to maintain glucose levels within normal limits. Pregnant women who develop GDM are unable to augment insulin production to compensate for their increased resistance to insulin [6]. There are several modifiable and unmodifiable risk factors for developing GDM. Obesity is a modifiable risk factor that is strongly associated with the development of gestational diabetes. In a survey of 97000 singleton births, obese women had a 3-fold increased risk of developing GDM than nonobese women [7]. Not only obese (body

References

[1]  “Canadian Diabetes Association Clinical Practice Guidelines Expert Committee: Canadian Diabetes Association clinical practice guidelines for the prevention and management of diabetes in Canada,” Canadian Journal of Diabetes, vol. 27, pp. S99–S105, 2003.
[2]  American Diabetes Association, “Gestational diabetes mellitus,” Diabetes Care, vol. 27, pp. S88–S90, 2004.
[3]  K. G. Alberti and P. Z. Zimmet, “Definition, diagnosis and classification of diabetes mellitus and its complications. Part 1: diagnosis and classification of diabetes mellitus provisional report of a WHO consultation,” Diabetic Medicine, vol. 15, no. 7, pp. 539–553, 1998.
[4]  E. A. Reece, C. Homko, M. Miodovnik, and O. Langer, “A consensus report of the Diabetes in Pregnancy Study Group of North America conference: little Rock, Arkansas, May 2002,” Journal of Maternal-Fetal and Neonatal Medicine, vol. 12, no. 6, pp. 362–364, 2002.
[5]  R. Artal, “Exercise: the alternative therapeutic intervention for gestational diabetes,” Clinical Obstetrics and Gynecology, vol. 46, no. 2, pp. 479–487, 2003.
[6]  C. Kühl, “Etiology and pathogenesis of gestational diabetes,” Diabetes Care, vol. 21, no. 2, pp. B19–B26, 1998.
[7]  A. T. Blanco, S. W. Semilen, Y. Davis, S. Lopez, R. Lapinski, and C. J. Lockwood, “Pregnancy outcome and weight gain recommendations for the morbidly obese women,” Obstetrics and Gynecology, vol. 91, no. 1, pp. 97–102, 1998.
[8]  Y. Linné, “Effects of obesity on women's reproduction and complications during pregnancy,” Obesity Reviews, vol. 5, no. 3, pp. 137–143, 2004.
[9]  HAPO Study Cooperative Research Group, “Hyperglycemia and Adverse Pregnancy Outcome (HAPO) Study: associations with maternal body mass index,” An International Journal of Obstetrics and Gynaecology, vol. 117, no. 5, pp. 575–584, 2010.
[10]  D. Getahun, C. Nath, C. V. Ananth, M. R. Chavez, and J. C. Smulian, “Gestational diabetes in the United States: temporal trends 1989 through 2004,” American Journal of Obstetrics and Gynecology, vol. 198, no. 5, pp. 525.e1–525.e5, 2008.
[11]  American Diabetes Association, “Standards of medical care in diabetes-2009,” Diabetes Care, vol. 32, no. supplement 1, pp. S13–S61, 2009.
[12]  S. Schneider, C. Bock, M. Wetzel, H. Maul, and A. Loerbroks, “The prevalence of gestational diabetes in advanced economies,” Journal of Perinatal Medicine, vol. 40, no. 5, pp. 511–520, 2012.
[13]  M. J. Paglia and D. R. Coustan, “Gestational diabetes: evolving diagnostic criteria,” Current Opinion in Obstetrics and Gynecology, vol. 23, pp. 72–75, 2011.
[14]  “Canadian Diabetes Association Clinical Practice Guidelines Expert Committee,” Canadian Diabetes Association, vol. 32, pp. S1–S201, 2008.
[15]  S. Y. Chu, W. M. Callaghan, S. Y. Kim et al., “Maternal obesity and risk of gestational diabetes mellitus,” Diabetes Care, vol. 30, no. 8, pp. 2070–2076, 2007.
[16]  M. R. Torloni, A. P. Betrán, B. L. Horta et al., “Prepregnancy BMI and the risk of gestational diabetes: a systematic review of the literature with meta-analysis: diagnostic in Obesity and Complications,” Obesity Reviews, vol. 10, no. 2, pp. 194–203, 2009.
[17]  M. M. Schlüssel, E. B. De Souza, M. E. Reichenheim, and G. Kac, “Physical activity during pregnancy and maternal-child health outcomes: a systematic literature review,” Cadernos de Saude Publica, vol. 24, no. 4, pp. S531–S544, 2008.
[18]  J. C. Dempsey, C. L. Butler, and M. A. Williams, “No need for a pregnant pause: physical activity may reduce the occurrence of gestational diabetes mellitus and preeclampsia,” Exercise and Sport Sciences Reviews, vol. 33, no. 3, pp. 141–149, 2005.
[19]  “ACOG Committee opinion. Number 267, January 2002: exercise during pregnancy and the postpartum period,” Obstetrics & Gynecology, vol. 99, no. 1, pp. 171–173, 2002.
[20]  American Diabetes Association, “Gestational diabetes mellitus,” Diabetes Care, vol. 26, pp. S103–S105, 2003.
[21]  B. E. Metzger, T. A. Buchanan, D. R. Coustan, et al., “Summary and recommendations of the Fifth International Workshop-Conference on Gestational Diabetes Mellitus,” Diabetes Care, vol. 30, no. supplement 2, pp. s251–s260, 2007.
[22]  T. A. Buchanan, A. Xiang, S. L. Kjos, and R. Watanabe, “What is gestational diabetes?” Diabetes Care, vol. 30, no. 2, pp. S105–S111, 2007.
[23]  P. M. Catalano, E. D. Tzybir, R. R. Wolfe, et al., “Carbohydrate metabolism during pregnancy in control subjects and women with gestational diabetes,” American Journal of Physiology, vol. 264, pp. E60–E67, 1993.
[24]  T. A. Buchanan and A. H. Xiang, “Gestational diabetes mellitus,” Journal of Clinical Investigation, vol. 115, no. 3, pp. 485–491, 2005.
[25]  K. Y. Lain and P. M. Catalano, “Metabolic changes in pregnancy,” Clinical Obstetrics and Gynecology, vol. 50, no. 4, pp. 938–948, 2007.
[26]  J. P. Kirwan, S. Hauguel-De Mouzon, J. Lepercq et al., “TNF-α is a predictor of insulin resistance in human pregnancy,” Diabetes, vol. 51, no. 7, pp. 2207–2213, 2002.
[27]  I. Falc?o-Pires, P. Castro-Chaves, D. Miranda-Silva, A. P. Louren?o, and A. F. Leite-Moreira, “Physiological, pathological and potential therapeutic roles of adipokines,” Drug Discovery Today, vol. 17, pp. 880–889, 2012.
[28]  T. S. Tsao, H. E. Murrey, C. Hug, D. H. Lee, and H. F. Lodish, “Oligomerization state-dependent activation of NF-κB signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30),” Journal of Biological Chemistry, vol. 277, no. 33, pp. 29359–29362, 2002.
[29]  U. B. Pajvani, X. Du, T. P. Combs et al., “Structure-function studies of the adipocyte-secreted hormone Acrp30/adiponectin: implications for metabolic regulation and bioactivity,” Journal of Biological Chemistry, vol. 278, no. 11, pp. 9073–9085, 2003.
[30]  S. Suzuki, E. M. Wilson-Kubalek, D. Wert, T. S. Tsao, and D. H. Lee, “The oligomeric structure of high molecular weight adiponectin,” FEBS Letters, vol. 581, no. 5, pp. 809–814, 2007.
[31]  U. B. Pajvani, M. Hawkins, T. P. Combs et al., “Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity,” Journal of Biological Chemistry, vol. 279, no. 13, pp. 12152–12162, 2004.
[32]  D. K. Oh, T. Ciaraldi, and R. R. Henry, “Adiponectin in health and disease,” Diabetes, Obesity and Metabolism, vol. 9, no. 3, pp. 282–289, 2007.
[33]  S. Rizza, F. Gigli, A. Galli et al., “Adiponectin isoforms in elderly patients with or without coronary artery disease,” Journal of the American Geriatrics Society, vol. 58, no. 4, pp. 702–706, 2010.
[34]  P. Almeda-Valdes, D. Cuevas-Ramos, R. Mehta et al., “Total and high molecular weight adiponectin have similar utility for the identification of insulin resistance,” Cardiovascular Diabetology, vol. 9, article 26, 2010.
[35]  S. Mazaki-Tovi, H. Kanety, and E. Sivan, “Adiponectin and human pregnancy,” Current Diabetes Reports, vol. 5, no. 4, pp. 278–281, 2005.
[36]  W. S. Yang, W. J. Lee, T. Funahashi et al., “Weight reduction increases plasma levels of an adipose-derived anti-inflammatory protein, adiponectin,” Journal of Clinical Endocrinology and Metabolism, vol. 86, no. 8, pp. 3815–3819, 2001.
[37]  A. Mavri, P. Poredo?, D. ?uran, B. Gaborit, I. Juhan-Vague, and P. Poredo?, “Effect of diet-induced weight loss on endothelial dysfunction: early improvement after the first week of dieting,” Heart and Vessels, vol. 26, no. 1, pp. 31–38, 2011.
[38]  K. Ohashi, N. Ouchi, and Y. Matsuzawa, “Anti-inflammatory and anti-atherogenic properties of adiponectin,” Biochimie, vol. 94, pp. 2137–2142, 2012.
[39]  G. Musso, R. Gambino, G. Biroli et al., “Hypoadiponectinemia predicts the severity of hepatic fibrosis and pancreatic beta-cell dysfunction in nondiabetic nonobese patients with nonalcoholic steatohepatitis,” American Journal of Gastroenterology, vol. 100, no. 11, pp. 2438–2446, 2005.
[40]  R. Retnakaran, A. J. G. Hanley, N. Raif et al., “Adiponectin and beta cell dysfunction in gestational diabetes: pathophysiological implications,” Diabetologia, vol. 48, no. 5, pp. 993–1001, 2005.
[41]  N. Ouchi, S. Kihara, Y. Arita et al., “Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-κB signaling through a cAMP-dependent pathway,” Circulation, vol. 102, no. 11, pp. 1296–1301, 2000.
[42]  T. Yokota, K. Oritani, I. Takahashi et al., “Adiponectin, a new member of the family of soluble defense collagens, negatively regulates the growth of myelomonocytic progenitors and the functions of macrophages,” Blood, vol. 96, no. 5, pp. 1723–1732, 2000.
[43]  D. Cortelazzi, S. Corbetta, S. Ronzoni et al., “Maternal and foetal resistin and adiponectin concentrations in normal and complicated pregnancies,” Clinical Endocrinology, vol. 66, no. 3, pp. 447–453, 2007.
[44]  S. Mazaki-Tovi, H. Kanety, C. Pariente et al., “Maternal serum adiponectin levels during human pregnancy,” Journal of Perinatology, vol. 27, no. 2, pp. 77–81, 2007.
[45]  A. J. O'Sullivan, A. D. Kriketos, A. Martin, and M. A. Brown, “Serum adiponectin levels in normal and hypertensive pregnancy,” Hypertension in Pregnancy, vol. 25, no. 3, pp. 193–203, 2006.
[46]  T. F. Chan, S. S. F. Yuan, H. S. Chen et al., “Correlations between umbilical and maternal serum adiponectin levels and neonatal birthweights,” Acta Obstetricia et Gynecologica Scandinavica, vol. 83, no. 2, pp. 165–169, 2004.
[47]  J. Chen, B. Tan, E. Karteris et al., “Secretion of adiponectin by human placenta: differential modulation of adiponectin and its receptors by cytokines,” Diabetologia, vol. 49, no. 6, pp. 1292–1302, 2006.
[48]  F. Haugen, T. Ranheim, N. K. Harsem, E. Lips, A. C. Staff, and C. A. Drevon, “Increased plasma levels of adipokines in preeclampsia: relationship to placenta and adipose tissue gene expression,” American Journal of Physiology, vol. 290, no. 2, pp. E326–E333, 2006.
[49]  C. Worda, H. Leipold, C. Gruber, A. Kautzky-Willer, M. Kn?fler, and D. Bancher-Todesca, “Decreased plasma adiponectin concentrations in women with gestational diabetes mellitus,” American Journal of Obstetrics and Gynecology, vol. 191, no. 6, pp. 2120–2124, 2004.
[50]  K. Cseh, E. Baranyi, Z. Melczer, E. Kaszás, E. Palik, and G. Winkler, “Plasma adiponectin and pregnancy-induced insulin resistance,” Diabetes Care, vol. 27, no. 1, pp. 274–275, 2004.
[51]  M. A. Williams, C. Qiu, M. Muy-Rivera, S. Vadachkoria, T. Song, and D. A. Luthy, “Plasma adiponectin concentrations in early pregnancy and subsequent risk of gestational diabetes mellitus,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 5, pp. 2306–2311, 2004.
[52]  C. Winzer, O. Wagner, A. Festa et al., “Plasma adiponectin, insulin sensitivity, and subclinical inflammation in women with prior gestational diabetes mellitus,” Diabetes Care, vol. 27, no. 7, pp. 1721–1727, 2004.
[53]  S. M. Heitritter, C. G. Solomon, G. F. Mitchell, N. Skali-Ounis, and E. W. Seely, “Subclinical inflammation and vascular dysfunction in women with previous gestational diabetes mellitus,” Journal of Clinical Endocrinology and Metabolism, vol. 90, no. 7, pp. 3983–3988, 2005.
[54]  H. C. Sung, H. K. Soo, B. S. Youn et al., “High plasma retinol binding protein-4 and low plasma adiponectin concentrations are associated with severity of glucose intolerance in women with previous gestational diabetes mellitus,” Journal of Clinical Endocrinology and Metabolism, vol. 93, no. 8, pp. 3142–3148, 2008.
[55]  J. Be?towski, “Adiponectin and resistin—new hormones of white adipose tissue,” Medical Science Monitor, vol. 9, no. 2, pp. RA55–RA61, 2003.
[56]  T. Yamauchi, J. Kamon, Y. Minokoshi, et al., “Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase,” Nature Medicine, vol. 8, pp. 1288–1295, 2002.
[57]  T. Yamauchi, J. Kamon, H. Waki et al., “Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis,” Journal of Biological Chemistry, vol. 278, no. 4, pp. 2461–2468, 2003.
[58]  A. E. Civitarese, B. Ukropcova, S. Carling et al., “Role of adiponectin in human skeletal muscle bioenergetics,” Cell Metabolism, vol. 4, no. 1, pp. 75–87, 2006.
[59]  R. B. Ceddia, R. Somwar, A. Maida, X. Fang, G. Bikopoulos, and G. Sweeney, “Globular adiponectin increases GLUT4 translocation and glucose uptake but reduces glycogen synthesis in rat skeletal muscle cells,” Diabetologia, vol. 48, no. 1, pp. 132–139, 2005.
[60]  R. A. Miller, Q. Chu, J. Le Lay et al., “Adiponectin suppresses gluconeogenic gene expression in mouse hepatocytes independent of LKB1-AMPK signaling,” Journal of Clinical Investigation, vol. 121, no. 6, pp. 2518–2528, 2011.
[61]  M. Okamoto, M. Ohara-Imaizumi, N. Kubota et al., “Adiponectin induces insulin secretion in vitro and in vivo at a low glucose concentration,” Diabetologia, vol. 51, no. 5, pp. 827–835, 2008.
[62]  K. Staiger, N. Stefan, H. Staiger et al., “Adiponectin is functionally active in human islets but does not affect insulin secretory function or β-cell lipoapoptosis,” Journal of Clinical Endocrinology and Metabolism, vol. 90, no. 12, pp. 6707–6713, 2005.
[63]  M. S. Winzell, R. Nogueiras, C. Dieguez, and B. Ahrén, “Dual action of adiponectin on insulin secretion in insulin-resistant mice,” Biochemical and Biophysical Research Communications, vol. 321, no. 1, pp. 154–160, 2004.
[64]  N. Wijesekara, M. Krishnamurthy, A. Bhattacharjee, A. Suhail, G. Sweeney, and M. B. Wheeler, “Adiponectin-induced ERK and Akt phosphorylation protects against pancreatic beta cell apoptosis and increases insulin gene expression and secretion,” Journal of Biological Chemistry, vol. 285, no. 44, pp. 33623–33631, 2010.
[65]  A. T. Turer and P. E. Scherer, “Adiponectin: mechanistic insights and clinical implications,” Diabetologia, vol. 55, no. 9, pp. 2319–2326, 2012.
[66]  A. M. Brennan and C. S. Mantzoros, “Drug Insight: the role of leptin in human physiology and pathophysiology—emerging clinical applications,” Nature Clinical Practice Endocrinology and Metabolism, vol. 2, no. 6, pp. 318–327, 2006.
[67]  H. Ge, L. Huang, T. Pourbahrami, and C. Li, “Generation of soluble leptin receptor by ectodomain shedding of membrane-spanning receptors in vitro and in vivo,” Journal of Biological Chemistry, vol. 277, no. 48, pp. 45898–45903, 2002.
[68]  R. Yang and L. A. Barouch, “Leptin signaling and obesity: cardiovascular consequences,” Circulation Research, vol. 101, no. 6, pp. 545–559, 2007.
[69]  S. H. Bates and M. G. Myers, “The role of leptin—STAT3 signaling in neuroendocrine function: an integrative perspective,” Journal of Molecular Medicine, vol. 82, no. 1, pp. 12–20, 2004.
[70]  C. Kloek, A. K. Haq, S. L. Dunn, H. J. Lavery, A. S. Banks, and M. G. Myers Jr., “Regulation of Jak kinases by intracellular leptin receptor sequences,” Journal of Biological Chemistry, vol. 277, no. 44, pp. 41547–41555, 2002.
[71]  K. D. Niswender, B. Gallis, J. E. Blevins, M. A. Corson, M. W. Schwartz, and D. G. Baskin, “Immunocytochemical detection of phosphatidylinositol 3-kinase activation by insulin and leptin,” Journal of Histochemistry and Cytochemistry, vol. 51, no. 3, pp. 275–283, 2003.
[72]  H. Masuzaki, Y. Ogawa, N. Sagawa et al., “Nonadipose tissue production of leptin: leptin as a novel placenta- derived hormone in humans,” Nature Medicine, vol. 3, no. 9, pp. 1029–1033, 1997.
[73]  S. Hauguel-de Mouzon, J. Lepercq, and P. Catalano, “The known and unknown of leptin in pregnancy,” American Journal of Obstetrics and Gynecology, vol. 194, no. 6, pp. 1537–1545, 2006.
[74]  M. Wauters, R. V. Considine, and L. F. Van Gaal, “Human leptin: from an adipocyte hormone to an endocrine mediator,” European Journal of Endocrinology, vol. 143, no. 3, pp. 293–311, 2000.
[75]  C. Grunfeld, C. Zhao, J. Fuller et al., “Endotoxin and cytokines induce expression of leptin, the ob gene product, in hamsters: a role for leptin in the anorexia of infection,” Journal of Clinical Investigation, vol. 97, no. 9, pp. 2152–2157, 1996.
[76]  P. J. Havel, S. Kasim-Karakas, W. Mueller, P. R. Johnson, R. L. Gingerich, and J. S. Stern, “Relationship of plasma leptin to plasma insulin and adiposity in normal weight and overweight women: effects of dietary fat content and sustained weight loss,” Journal of Clinical Endocrinology and Metabolism, vol. 81, no. 12, pp. 4406–4413, 1996.
[77]  E. Jequier, “Leptin signaling, adiposity and energy balance,” Annals of the New York Academy of Sciences, vol. 967, pp. 379–388, 2002.
[78]  C. Schubring, P. Englaro, T. Siebler et al., “Longitudinal analysis of maternal serum leptin levels during pregnancy, at birth and up to six weeks after birth: relation to body mass index, skinfolds, sex steroids and umbilical cord blood leptin levels,” Hormone Research, vol. 50, no. 5, pp. 276–283, 1998.
[79]  H. Laivuori, R. Kaaja, H. Koistinen et al., “Leptin during and after preeclamptic or normal pregnancy: its relation to serum insulin and insulin sensitivity,” Metabolism, vol. 49, no. 2, pp. 259–263, 2000.
[80]  D. D. Briana and A. Malamitsi-Puchner, “Reviews: adipocytokines in normal and complicated pregnancies,” Reproductive Sciences, vol. 16, no. 10, pp. 921–937, 2009.
[81]  E. Oteng-Ntim, R. Varma, H. Croker, L. Poston, and P. Doyle, “Lifestyle interventions for overweight and obese pregnant women to improve pregnancy outcome: systematic review and meta-analysis,” BMC Medicine, vol. 10, article 47, 2012.
[82]  S. L. Nascimento, F. G. Surita, and J. G. Cecatti, “Physical exercise during pregnancy: a systematic review,” Current Opinion in Obstetrics and Gynecology, vol. 24, no. 6, pp. 387–394, 2012.
[83]  J. M. Atègbo, O. Grissa, A. Yessoufou et al., “Modulation of adipokines and cytokines in gestational diabetes and macrosomia,” Journal of Clinical Endocrinology and Metabolism, vol. 91, no. 10, pp. 4137–4143, 2006.
[84]  T. J. Highman, J. E. Friedman, L. P. Huston, W. W. Wong, and P. M. Catalano, “Longitudinal changes in maternal serum leptin concentrations, body composition, and resting metabolic rate in pregnancy,” American Journal of Obstetrics and Gynecology, vol. 178, no. 5, pp. 1010–1015, 1998.
[85]  M. C. Henson, K. F. Swan, and J. S. O'Neil, “Expression of placental leptin and leptin receptor transcripts in early pregnancy and at term,” Obstetrics and Gynecology, vol. 92, no. 6, pp. 1020–1028, 1998.
[86]  D. Chen, G. Xia, P. Xu, and M. Dong, “Peripartum serum leptin and soluble leptin receptor levels in women with gestational diabetes,” Acta Obstetricia et Gynecologica Scandinavica, vol. 89, no. 12, pp. 1595–1599, 2010.
[87]  C. Qiu, M. A. Williams, S. Vadachkoria, I. O. Frederick, and D. A. Luthy, “Increased maternal plasma leptin in early pregnancy and risk of gestational diabetes mellitus,” Obstetrics and Gynecology, vol. 103, no. 3, pp. 519–525, 2004.
[88]  X. L. Gao, H. X. Yang, and Y. Zhao, “Variations of tumor necrosis factor-α, leptin and adiponectin in mid-trimester of gestational diabetes mellitus,” Chinese Medical Journal, vol. 121, no. 8, pp. 701–705, 2008.
[89]  R. D'Anna, G. Baviera, M. L. Cannata, A. De Vivo, A. Di Benedetto, and F. Corrado, “Midtrimester amniotic fluid leptin and insulin levels and subsequent gestational diabetes,” Gynecologic and Obstetric Investigation, vol. 64, no. 2, pp. 65–68, 2007.
[90]  R. G. Lea, D. Howe, L. T. Hannah, O. Bonneau, L. Hunter, and N. Hoggard, “Placental leptin in normal, diabetic and fetal growth-retarded pregnancies,” Molecular Human Reproduction, vol. 6, no. 8, pp. 763–769, 2000.
[91]  M. A. Nuamah, S. Yura, N. Sagawa et al., “Significant increase in maternal plasma leptin concentration in induced delivery: a possible contribution of pro-inflammatory cytokines to placental leptin secretion,” Endocrine Journal, vol. 51, no. 2, pp. 177–187, 2004.
[92]  L. A. Barbour, C. E. McCurdy, T. L. Hernandez, J. P. Kirwan, P. M. Catalano, and J. E. Friedman, “Cellular mechanisms for insulin resistance in normal pregnancy and gestational diabetes,” Diabetes Care, vol. 30, no. 2, pp. S112–S119, 2007.
[93]  J. A. Gavard and R. Artal, “Effect of exercise on pregnancy outcome,” Clinical Obstetrics and Gynecology, vol. 51, pp. 467–480, 2008.
[94]  R. R. Banerjee and M. A. Lazar, “Dimerization of resistin and resistin-like molecules is determined by a single cysteine,” Journal of Biological Chemistry, vol. 276, no. 28, pp. 25970–25973, 2001.
[95]  C. M. Steppan, S. T. Bailey, S. Bhat et al., “The hormone resistin links obesity to diabetes,” Nature, vol. 409, no. 6818, pp. 307–312, 2001.
[96]  P. G. McTernan, C. M. Kusminski, and S. Kumar, “Resistin,” Current Opinion in Lipidology, vol. 17, no. 2, pp. 170–175, 2006.
[97]  E. Adeghate, “An update on the biology and physiology of resistin,” Cellular and Molecular Life Sciences, vol. 61, pp. 2485–2496, 2004.
[98]  C. M. Steppan and M. A. Lazar, “The current biology of resistin,” Journal of Internal Medicine, vol. 255, no. 4, pp. 439–447, 2004.
[99]  K. Azuma, F. Katsukawa, S. Oguchi et al., “Correlation between serum resistin level and adiposity in obese individuals,” Obesity Research, vol. 11, no. 8, pp. 997–1001, 2003.
[100]  J. V. Silha, M. Krsek, J. V. Skrha, P. Sucharda, B. L. G. Nyomba, and L. J. Murphy, “Plasma resistin, adiponectin and leptin levels in lean and obese subjects: correlations with insulin resistence,” European Journal of Endocrinology, vol. 149, no. 4, pp. 331–335, 2003.
[101]  K. M. Utzschneider, D. B. Carr, J. Tong et al., “Resistin is not associated with insulin sensitivity or the metabolic syndrome in humans,” Diabetologia, vol. 48, no. 11, pp. 2330–2333, 2005.
[102]  G. M. Dick, P. S. Katz, M. Farias III et al., “Resistin impairs endothelium-dependent dilation to bradykinin, but not acetylcholine, in the coronary circulation,” American Journal of Physiology, vol. 291, no. 6, pp. H2997–H3002, 2006.
[103]  D. B. Savage, C. P. Sewter, E. S. Klenk et al., “Resistin / Fizz3 expression in relation to obesity and peroxisome proliferator—activated receptor-γ action in humans,” Diabetes, vol. 50, no. 10, pp. 2199–2202, 2001.
[104]  L. Patel, A. C. Buckels, I. J. Kinghorn et al., “Resistin is expressed in human macrophages and directly regulated by PPARγ activators,” Biochemical and Biophysical Research Communications, vol. 300, no. 2, pp. 472–476, 2003.
[105]  D. Chen, M. Dong, Q. Fang, J. He, Z. Wang, and X. Yang, “Alterations of serum resistin in normal pregnancy and pre-eclampsia,” Clinical Science, vol. 108, no. 1, pp. 81–84, 2005.
[106]  S. Yura, N. Sagawa, H. Itoh et al., “Resistin is expressed in the human placenta,” Journal of Clinical Endocrinology and Metabolism, vol. 88, no. 3, pp. 1394–1397, 2003.
[107]  N. Di Simone, F. Di Nicuolo, D. Marzioni et al., “Resistin modulates glucose uptake and glucose transporter-1 (GLUT-1) expression in trophoblast cells,” Journal of Cellular and Molecular Medicine, vol. 13, no. 2, pp. 388–397, 2009.
[108]  E. Palik, E. Baranyi, Z. Melczer et al., “Elevated serum acylated (biologically active) ghrelin and resistin levels associate with pregnancy-induced weight gain and insulin resistance,” Diabetes Research and Clinical Practice, vol. 76, no. 3, pp. 351–357, 2007.
[109]  S. Mazaki-Tovi, R. Romero, J. P. Kusanovic et al., “Maternal visfatin concentration in normal pregnancy,” Journal of Perinatal Medicine, vol. 37, no. 3, pp. 206–217, 2009.
[110]  A. Megia, J. Vendrell, C. Gutierrez et al., “Insulin sensitivity and resistin levels in gestational diabetes mellitus and after parturition,” European Journal of Endocrinology, vol. 158, no. 2, pp. 173–178, 2008.
[111]  M. Lappas, K. Yee, M. Permezel, and G. E. Rice, “Release and regulation of leptin, resistin and adiponectin from human placenta, fetal membranes, and maternal adipose tissue and skeletal muscle from normal and gestational diabetes mellitus-complicated pregnancies,” Journal of Endocrinology, vol. 186, no. 3, pp. 457–465, 2005.
[112]  G. Winkler, K. Cseh, é. Baranyi et al., “Tumor necrosis factor system in insulin resistance in gestational diabetes,” Diabetes Research and Clinical Practice, vol. 56, no. 2, pp. 93–99, 2002.
[113]  G. S. Hotamisligil, D. L. Murray, L. N. Choy, and B. M. Spiegelman, “Tumor necrosis factor alpha inhibits signaling from the insulin receptor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, pp. 4854–4858, 1994.
[114]  R. Feinstein, H. Kanety, M. Z. Papa, B. Lunenfeld, and A. Karasik, “Tumor necrosis factor-α suppresses insulin-induced tyrosine phosphorylation of insulin receptor and its substrates,” Journal of Biological Chemistry, vol. 268, no. 35, pp. 26055–26058, 1993.
[115]  L. F. del Aguila, K. P. Claffey, and J. P. Kirwan, “TNF-α impairs insulin signaling and insulin stimulation of glucose uptake in C2C12 muscle cells,” American Journal of Physiology, vol. 276, no. 5, pp. E849–E855, 1999.
[116]  G. S. Hotamisligil, P. Peraldi, A. Budavari, R. Ellis, M. F. White, and B. M. Spiegelman, “IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance,” Science, vol. 271, no. 5249, pp. 665–668, 1996.
[117]  J. P. Kirwan, R. K. Krishnan, J. A. Weaver, L. F. del Aguila, and W. J. Evans, “Human aging is associated with altered TNF-α production during hyperglycemia and hyperinsulinemia,” American Journal of Physiology, vol. 281, no. 6, pp. E1137–E1143, 2001.
[118]  P. R. Ling, B. R. Bistrian, B. Mendez, and N. W. Istfan, “Effects of systemic infusions of endotoxin, tumor necrosis factor, and interleukin-1 on glucose metabolism in the rat: relationship to endogenous glucose production and peripheral tissue glucose uptake,” Metabolism, vol. 43, no. 3, pp. 279–284, 1994.
[119]  L. F. del Aguila, R. K. Krishnan, J. S. Ulbrecht et al., “Muscle damage impairs insulin stimulation of IRS-1, PI 3-kinase, and Akt-kinase in human skeletal muscle,” American Journal of Physiology, vol. 279, no. 1, pp. E206–E212, 2000.
[120]  M. T. Coughlan, K. Oliva, H. M. Georgiou, J. M. H. Permezel, and G. E. Rice, “Glucose-induced release of tumour necrosis factor-alpha from human placental and adipose tissues in gestational diabetes mellitus,” Diabetic Medicine, vol. 18, no. 11, pp. 921–927, 2001.
[121]  K. A. McLachlan, D. O'Neal, A. Jenkins, and F. P. Alford, “Do adiponectin, TNFα, leptin and CRP relate to insulin resistance in pregnancy? Studies in women with or without gestational diabetes, during and after pregnancy,” Diabetes/Metabolism Research and Reviews, vol. 22, no. 2, pp. 131–138, 2006.
[122]  A. Fukuhara, M. Matsuda, M. Nishizawa et al., “Visfatin: a protein secreted by visceral fat that Mimics the effects of insulin,” Science, vol. 307, no. 5708, pp. 426–430, 2005.
[123]  T. D. Filippatos, C. S. Derdemezis, I. F. Gazi et al., “Increased plasma visfatin levels in subjects with the metabolic syndrome,” European Journal of Clinical Investigation, vol. 38, no. 1, pp. 71–72, 2008.
[124]  M. P. Chen, F. M. Chung, D. M. Chang et al., “Elevated plasma level of visfatin/pre-B cell colony-enhancing factor in patients with type 2 diabetes mellitus,” Journal of Clinical Endocrinology and Metabolism, vol. 91, no. 1, pp. 295–299, 2006.
[125]  J. Berndt, N. Kl?ting, S. Kralisch et al., “Plasma visfatin concentrations and fat depot-specific mRNA expression in humans,” Diabetes, vol. 54, no. 10, pp. 2911–2916, 2005.
[126]  S. A. Morgan, J. B. Bringolf, and E. R. Seidel, “Visfatin expression is elevated in normal human pregnancy,” Peptides, vol. 29, no. 8, pp. 1382–1389, 2008.
[127]  B. Telejko, M. Kuzmicki, A. Zonenberg et al., “Visfatin in gestational diabetes: serum level and mRNA expression in fat and placental tissue,” Diabetes Research and Clinical Practice, vol. 84, no. 1, pp. 68–75, 2009.
[128]  S. Ognjanovic, T. L. Ku, and G. D. Bryant-Greenwood, “Pre-B-cell colony-enhancing factor is a secreted cytokine-like protein from the human amniotic epithelium,” American Journal of Obstetrics and Gynecology, vol. 193, no. 1, pp. 273–282, 2005.
[129]  T. Josephs, H. Waugh, I. Kokay, D. Grattan, and M. Thompson, “Fasting-induced adipose factor identified as a key adipokine that is up-regulated in white adipose tissue during pregnancy and lactation in the rat,” Journal of Endocrinology, vol. 194, no. 2, pp. 305–312, 2007.
[130]  D. D. Briana, M. Boutsikou, D. Gourgiotis et al., “Role of visfatin, insulin-like growth factor-I and insulin in fetal growth,” Journal of Perinatal Medicine, vol. 35, no. 4, pp. 326–329, 2007.
[131]  K. C. Lewandowski, N. Stojanovic, M. Press et al., “Elevated serum levels of visfatin in gestational diabetes: a comparative study across various degrees of glucose tolerance,” Diabetologia, vol. 50, no. 5, pp. 1033–1037, 2007.
[132]  K. Krzyzanowska, W. Krugluger, F. Mittermayer et al., “Increased visfatin concentrations in women with gestational diabetes mellitus,” Clinical Science, vol. 110, no. 5, pp. 605–609, 2006.
[133]  S. Mazaki-Tovi, R. Romero, J. P. Kusanovic et al., “Visfatin in human pregnancy: maternal gestational diabetes vis-à-vis neonatal birthweight,” Journal of Perinatal Medicine, vol. 37, no. 3, pp. 218–231, 2009.
[134]  T. F. Chan, Y. L. Chen, C. H. Lee et al., “Decreased plasma visfatin concentrations in women with gestational diabetes mellitus,” Journal of the Society for Gynecologic Investigation, vol. 13, no. 5, pp. 364–367, 2006.
[135]  D. G. Haider, A. Handisurya, A. Storka et al., “Visfatin response to glucose is reduced in women with gestational diabetes mellitus,” Diabetes Care, vol. 30, no. 7, pp. 1889–1891, 2007.
[136]  M. Akturk, A. E. Altinova, I. Mert et al., “Visfatin concentration is decreased in women with gestational diabetes mellitus in the third trimester,” Journal of Endocrinological Investigation, vol. 31, no. 7, pp. 610–613, 2008.
[137]  G. Mastorakos, G. Valsamakis, D. C. Papatheodorou et al., “The role of adipocytokines in insulin resistance in normal pregnancy: visfatin concentrations in early pregnancy predict insulin sensitivity,” Clinical Chemistry, vol. 53, no. 8, pp. 1477–1483, 2007.
[138]  S. Ognjanovic, L. S. Tashima, and G. D. Bryant-Greenwood, “The effects of pre-B-cell colony-enhancing factor on the human fetal membranes by microarray analysis,” American Journal of Obstetrics and Gynecology, vol. 189, no. 4, pp. 1187–1195, 2003.
[139]  B. Masri, N. Morin, L. Pedebernade, B. Knibiehler, and Y. Audigier, “The apelin receptor is coupled to Gi1 or Gi2 protein and is differentially desensitized by apelin fragments,” Journal of Biological Chemistry, vol. 281, no. 27, pp. 18317–18326, 2006.
[140]  M. De Falco, L. De, N. Onori et al., “Apelin expression in normal human tissues,” In Vivo, vol. 16, no. 5, pp. 333–336, 2002.
[141]  S. Rayalam, M. A. Della-Fera, P. A. Krieg, C. M. Cox, A. Robins, and C. A. Baile, “A putative role for apelin in the etiology of obesity,” Biochemical and Biophysical Research Communications, vol. 368, no. 3, pp. 815–819, 2008.
[142]  O. Kunduzova, N. Alet, N. Delesque-Touchard et al., “Apelin/APJ signaling system: a potential link between adipose tissue and endothelial angiogenic processes,” The FASEB Journal, vol. 22, no. 12, pp. 4146–4153, 2008.
[143]  J. Be?towski, “Apelin and visfatin: unique “beneficial” adipokines up regulated in obesity?” Medical Science Monitor, vol. 12, pp. RA112–RA119, 2006.
[144]  K. Tatemoto, K. Takayama, M. X. Zou et al., “The novel peptide apelin lowers blood pressure via a nitric oxide-dependent mechanism,” Regulatory Peptides, vol. 99, no. 2-3, pp. 87–92, 2001.
[145]  L. Cobellis, M. De Falco, A. Mastrogiacomo et al., “Modulation of apelin and APJ receptor in normal and preeclampsia-complicated placentas,” Histology and Histopathology, vol. 22, no. 1–3, pp. 1–8, 2007.
[146]  C. M. Cox, S. L. D'Agostino, M. K. Miller, R. L. Heimark, and P. A. Krieg, “Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo,” Developmental Biology, vol. 296, no. 1, pp. 177–189, 2006.
[147]  M. Aslan, O. Celik, N. Celik, et al., “Cord blood nesfatin-1 and apelin-36 levels in gestational diabetes mellitus,” Endocrine, vol. 41, pp. 424–429, 2012.
[148]  B. A. Zabel, A. M. Silverio, and E. C. Butcher, “Chemokine-like receptor 1 expression and chemerin-directed chemotaxis distinguish plasmacytoid from myeloid dendritic cells in human blood,” Journal of Immunology, vol. 174, no. 1, pp. 244–251, 2005.
[149]  V. Wittamer, J. D. Franssen, M. Vulcano et al., “Specific recruitment of antigen-presenting cells by chemerin, a novel processed ligand from human inflammatory fluids,” Journal of Experimental Medicine, vol. 198, no. 7, pp. 977–985, 2003.
[150]  S. Kralisch, S. Weise, G. Sommer et al., “Interleukin-1? induces the novel adipokine chemerin in adipocytes in vitro,” Regulatory Peptides, vol. 154, no. 1–3, pp. 102–106, 2009.
[151]  K. Bozaoglu, K. Bolton, J. McMillan et al., “Chemerin is a novel adipokine associated with obesity and metabolic syndrome,” Endocrinology, vol. 148, no. 10, pp. 4687–4694, 2007.
[152]  J. F. Clapp III and W. Kiess, “Effects of pregnancy and exercise on concentrations of the metabolic markers tumor necrosis factor α and leptin,” American Journal of Obstetrics and Gynecology, vol. 182, no. 2, pp. 300–306, 2000.
[153]  D. Pfau, H. Stepan, J. Kratzsch et al., “Circulating levels of the adipokine chemerin in gestational diabetes mellitus,” Hormone Research in Paediatrics, vol. 74, no. 1, pp. 56–61, 2010.
[154]  G. Barker, R. Lim, G. E. Rice, and M. Lappas, “Increased chemerin concentrations in fetuses of obese mothers and correlation with maternal insulin sensitivity,” Journal of Maternal-Fetal and Neonatal Medicine, vol. 25, pp. 2274–2280, 2012.
[155]  G. Ceysens, D. Rouiller, and M. Boulvain, “Exercise for diabetic pregnant women,” Cochrane Database of Systematic Reviews, vol. 3, p. CD004225, 2006.
[156]  S. Han, P. Middleton, and C. A. Crowther, “Exercise for pregnant women for preventing gestational diabetes mellitus,” Cochrane Database of Systematic Reviews, vol. 11, no. 7, Article ID CD009021, 2012.
[157]  D. K. Tobias, C. Zhang, R. M. van Dam, K. Bowers, and F. B. Hu, “Physical activity before and during pregnancy and risk of gestational diabetes mellitus: a meta-analysis,” Diabetes Care, vol. 34, no. 1, pp. 223–229, 2011.
[158]  J. C. Dempsey, C. L. Butler, T. K. Sorensen et al., “A case-control study of maternal recreational physical activity and risk of gestational diabetes mellitus,” Diabetes Research and Clinical Practice, vol. 66, no. 2, pp. 203–215, 2004.
[159]  C. Zhang, C. G. Solomon, J. E. Manson, and F. B. Hu, “A prospective study of pregravid physical activity and sedentary behaviors in relation to the risk for gestational diabetes mellitus,” Archives of Internal Medicine, vol. 166, no. 5, pp. 543–548, 2006.
[160]  E. Oken, Y. Ning, S. L. Rifas-Shiman, J. S. Radesky, J. W. Rich-Edwards, and M. W. Gillman, “Associations of physical activity and inactivity before and during pregnancy with glucose tolerance,” Obstetrics and Gynecology, vol. 108, no. 5, pp. 1200–1207, 2006.
[161]  L. A. H. Haakstad, N. Voldner, T. Henriksen, and K. B?, “Physical activity level and weight gain in a cohort of pregnant Norwegian women,” Acta Obstetricia et Gynecologica Scandinavica, vol. 86, no. 5, pp. 559–564, 2007.
[162]  L. A. H. Haakstad, N. Voldner, T. Henriksen, and K. B?, “Why do pregnant women stop exercising in the third trimester?” Acta Obstetricia et Gynecologica Scandinavica, vol. 88, no. 11, pp. 1267–1275, 2009.
[163]  G. S. Zavorsky and L. D. Longo, “Exercise guidelines in pregnancy: new perspectives,” Sports Medicine, vol. 41, no. 5, pp. 345–360, 2011.
[164]  Royal College of Obstetricians and Gynecologists. Exercise in Pregnancy. RCOG, Statement. No4. 2006, http://www.rcog.org.uk/womens-health/clinical-guidance/exercise-pregnancy.
[165]  T. Hayashi, J. F. P. Wojtaszewski, and L. J. Goodyear, “Exercise regulation of glucose transport in skeletal muscle,” American Journal of Physiology, vol. 273, no. 6, pp. E1039–E1051, 1997.
[166]  S. Lund, G. D. Holman, O. Schmitz, and O. Pedersen, “Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 13, pp. 5817–5821, 1995.
[167]  J. R. Zierath, T. S. Tsao, A. E. Stenbit, J. W. Ryder, D. Galuska, and M. J. Charron, “Restoration of hypoxia-stimulated glucose uptake in GLUT4-deficient muscles by muscle-specific GLUT4 transgenic complementation,” Journal of Biological Chemistry, vol. 273, no. 33, pp. 20910–20915, 1998.
[168]  B. Cheatham, C. J. Vlahos, L. Cheatham, L. Wang, J. Blenis, and C. R. Kahn, “Phosphatidylinositol 3-kinase activation is required for insulin stimulation of pp70 S6 kinase, DNA synthesis, and glucose transporter translocation,” Molecular and Cellular Biology, vol. 14, no. 7, pp. 4902–4911, 1994.
[169]  L. J. Goodyear, “AMP-activated protein kinase: a critical signaling intermediary for exercise-stimulated glucose transport?” Exercise and Sport Sciences Reviews, vol. 28, no. 3, pp. 113–116, 2000.
[170]  A. Krook, M. Bj?rnholm, D. Galuska et al., “Characterization of signal transduction and glucose transport in skeletal muscle from type 2 diabetic patients,” Diabetes, vol. 49, no. 2, pp. 284–292, 2000.
[171]  J. A. Houmard, C. D. Shaw, M. S. Hickey, and C. J. Tanner, “Effect of short-term exercise training on insulin-stimulated PI 3-kinase activity in human skeletal muscle,” American Journal of Physiology, vol. 277, no. 6, pp. E1055–E1060, 1999.
[172]  D. S. King, G. P. Dalsky, M. A. Staten, W. E. Clutter, D. R. Van Houten, and J. O. Holloszy, “Insulin action and secretion in endurance-trained and untrained humans,” Journal of Applied Physiology, vol. 63, no. 6, pp. 2247–2252, 1987.
[173]  B. H. Goodpaster, A. Katsiaras, and D. E. Kelley, “Enhanced fat oxidation through physical activity is associated with improvements in insulin sensitivity in obesity,” Diabetes, vol. 52, no. 9, pp. 2191–2197, 2003.
[174]  V. A. Hughes, M. A. Fiatarone, R. A. Fielding et al., “Exercise increases muscle GLUT-4 levels and insulin action in subjects with impaired glucose tolerance,” American Journal of Physiology, vol. 264, no. 6, pp. E855–E862, 1993.
[175]  C. R. Bruce, A. D. Kriketos, G. J. Cooney, and J. A. Hawley, “Disassociation of muscle triglyceride content and insulin sensitivity after exercise training in patients with Type 2 diabetes,” Diabetologia, vol. 47, no. 1, pp. 23–30, 2004.
[176]  P. Poirier, A. Tremblay, T. Broderick, C. Catellier, G. Tancrède, and A. Nadeau, “Impact of moderate aerobic exercise training on insulin sensitivity in type 2 diabetic men treated with oral hypoglycemic agents: is insulin sensitivity enhanced only in nonobese subjects?” Medical Science Monitor, vol. 8, no. 2, pp. CR59–CR65, 2002.
[177]  G. L. Dohm, “Invited review: regulation of skeletal muscle GLUT-4 expression by exercise,” Journal of Applied Physiology, vol. 93, no. 2, pp. 782–787, 2002.
[178]  J. R. Zierath, “Invited review: exercise training-induced changes in insulin signaling in skeletal muscle,” Journal of Applied Physiology, vol. 93, no. 2, pp. 773–781, 2002.
[179]  P. S. MacLean, D. Zheng, and G. L. Dohm, “Muscle glucose transporter (GLUT 4) gene expression during exercise,” Exercise and Sport Sciences Reviews, vol. 28, no. 4, pp. 148–152, 2000.
[180]  I. Irrcher, P. J. Adhihetty, A. M. Joseph, V. Ljubicic, and D. A. Hood, “Regulation of mitochondrial biogenesis in muscle by endurance exercise,” Sports Medicine, vol. 33, no. 11, pp. 783–793, 2003.
[181]  M. F. Mottola, “The role of exercise in the prevention and treatment of gestational diabetes mellitus,” Current Diabetes Reports, vol. 8, no. 4, pp. 299–304, 2008.
[182]  J. J. Lehman, P. M. Barger, A. Kovacs, J. E. Saffitz, D. M. Medeiros, and D. P. Kelly, “Peroxisome proliferator-activated receptor γ coactivator-1 promotes cardiac mitochondrial biogenesis,” Journal of Clinical Investigation, vol. 106, no. 7, pp. 847–856, 2000.
[183]  H. Liang and W. F. Ward, “PGC-1α: a key regulator of energy metabolism,” American Journal of Physiology, vol. 30, no. 4, pp. 145–151, 2006.
[184]  W. T. Garvey, L. Maianu, J. A. Hancock, A. M. Golichowski, and A. Baron, “Gene expression of GLUT4 in skeletal muscle from insulin-resistant patients with obesity, IGT, GDM, and NIDDM,” Diabetes, vol. 41, no. 4, pp. 465–475, 1992.
[185]  O. Pedersen, J. F. Bak, P. H. Andersen et al., “Evidence against altered expression of GLUT1 or GLUT4 in skeletal muscle of patients with obesity for NIDDM,” Diabetes, vol. 39, no. 7, pp. 865–870, 1990.
[186]  F. Dela, T. Ploug, A. Handberg et al., “Physical training increases muscle GLUT4 protein and mRNA in patients with NIDDM,” Diabetes, vol. 43, no. 7, pp. 862–865, 1994.
[187]  J. R. Zierath and H. Wallberg-Henriksson, “From receptor to effector: insulin signal transduction in skeletal muscle from type II diabetic patients,” Annals of the New York Academy of Sciences, vol. 967, pp. 120–134, 2002.
[188]  J. P. Kirwan and M. Jing, “Modulation of insulin signaling in human skeletal muscle in response to exercise,” Exercise and Sport Sciences Reviews, vol. 30, no. 2, pp. 85–90, 2002.
[189]  M. Ishiki and A. Klip, “Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners,” Endocrinology, vol. 146, no. 12, pp. 5071–5078, 2005.
[190]  R. V. Farese, M. P. Sajan, and M. L. Standaert, “Atypical protein kinase C in insulin action and insulin resistance,” Biochemical Society Transactions, vol. 33, no. 2, pp. 350–353, 2005.
[191]  C. Fr?sig and E. A. Richter, “Improved insulin sensitivity after exercise: focus on insulin signaling,” Obesity, vol. 17, no. 3, pp. S15–S20, 2009.
[192]  C. B. Dugani and A. Klip, “Glucose transporter 4: cycling, compartments and controversies,” EMBO Reports, vol. 6, no. 12, pp. 1137–1142, 2005.
[193]  L. Jovanovic-Peterson, E. P. Durak, and C. M. Peterson, “Randomized trial of diet versus diet plus cardiovascular conditioning on glucose levels in gestational diabetes,” American Journal of Obstetrics and Gynecology, vol. 161, no. 2, pp. 415–419, 1989.
[194]  G. N. Brankston, B. F. Mitchell, E. A. Ryan, and N. B. Okun, “Resistance exercise decreases the need for insulin in overweight women with gestational diabetes mellitus,” American Journal of Obstetrics and Gynecology, vol. 190, no. 1, pp. 188–193, 2004.
[195]  P. Bung, R. Artal, N. Khodiguian, and S. Kjos, “Exercise in gestational diabetes: an optional therapeutic approach?” Diabetes, vol. 40, no. 2, pp. 182–185, 1991.
[196]  American Diabetes Association, “Standards of medical care in diabetes—2008,” Diabetes Care, supplement 1, pp. s12-–s54, 2008.
[197]  ACOG Committee Obstetric Practice, “ACOG Committee opinion. Number 267, January 2002: exercise during pregnancy and the postpartum period,” Obstetrics & Gynecology, vol. 99, pp. 171–13, 2002.
[198]  M. D. Avery, A. S. Leon, and R. A. Kopher, “Effects of a partially home-based exercise program for women with gestational diabetes,” Obstetrics and Gynecology, vol. 89, no. 1, pp. 10–15, 1997.
[199]  A. García-Patterson, E. Martín, J. Ubeda, M. A. María, A. de Leiva, and R. Corcoy, “Evaluation of light exercise in the treatment of gestational diabetes,” Diabetes Care, vol. 24, no. 11, pp. 2006–2007, 2001.
[200]  B. L. Marks, A. Ward, D. H. Morris, J. Castellani, and J. M. Rippe, “Fat-free mass is maintained in women following a moderate diet and exercise program,” Medicine and Science in Sports and Exercise, vol. 27, no. 9, pp. 1243–1251, 1995.
[201]  D. C. Nieman, J. M. Davis, D. A. Henson et al., “Carbohydrate ingestion influences skeletal muscle cytokine mRNA and plasma cytokine levels after a 3-h run,” Journal of Applied Physiology, vol. 94, no. 5, pp. 1917–1925, 2003.
[202]  N. Erdei, Z. Bagi, I. édes, G. Kaley, and A. Koller, “H2O2 increases production of constrictor prostaglandins in smooth muscle leading to enhanced arteriolar tone in Type 2 diabetic mice,” American Journal of Physiology, vol. 292, no. 1, pp. H649–H656, 2007.
[203]  C. Keller, A. Steensberg, H. Pilegaard et al., “Transcriptional activation of the IL-6 gene in human contracting skeletal muscle: influence of muscle glycogen content,” The FASEB Journal, vol. 15, no. 14, pp. 2748–2750, 2001.
[204]  M. A. Febbraio and B. K. Pedersen, “Contraction-induced myokine production and release: is skeletal muscle an endocrine organ?” Exercise and Sport Sciences Reviews, vol. 33, no. 3, pp. 114–119, 2005.
[205]  B. K. Pedersen and M. A. Febbraio, “Point: interleukin-6 does have a beneficial role in insulin sensitivity and glucose homeostasis,” Journal of Applied Physiology, vol. 102, no. 2, pp. 814–819, 2007.
[206]  A. Festa, R. D'Agostino, G. Howard, L. Mykk?nen, R. P. Tracy, and S. M. Haffner, “Chronic subclinical inflammation as part of the insulin resistance syndrome: the insulin resistance atherosclerosis study (IRAS),” Circulation, vol. 102, no. 1, pp. 42–47, 2000.
[207]  E. W. Petersen, A. L. Carey, M. Sacchetti et al., “Acute IL-6 treatment increases fatty acid turnover in elderly humans in vivo and in tissue culture in vitro,” American Journal of Physiology, vol. 288, no. 1, pp. E155–E162, 2005.
[208]  G. van Hall, A. Steensberg, M. Sacchetti et al., “Interleukin-6 stimulates lipolysis and fat oxidation in humans,” Journal of Clinical Endocrinology and Metabolism, vol. 88, no. 7, pp. 3005–3010, 2003.
[209]  E. Hopps, B. Canino, and G. Caimi, “Effects of exercise on inflammation markers in type 2 diabetic subjects,” Acta Diabetologica, vol. 48, pp. 183–189, 2011.
[210]  L. Volpe, G. Di Cianni, C. Lencioni, I. Cuccuru, L. Benzi, and S. Del Prato, “Gestational diabetes, inflammation, and late vascular disease,” Journal of Endocrinological Investigation, vol. 30, no. 10, pp. 873–879, 2007.
[211]  H. Zhang and C. Zhang, “Vasoprotection by dietary supplements and exercise: role of TNFα signaling,” Experimental Diabetes Research, vol. 2012, Article ID 972679, 6 pages, 2012.
[212]  S. A. Hopkins, J. C. Baldi, W. S. Cutfield, L. McCowan, and P. L. Hofman, “Effects of exercise training on maternal hormonal changes in pregnancy,” Clinical Endocrinology, vol. 74, no. 4, pp. 495–500, 2011.
[213]  J. B. Ruige, J. M. Dekker, W. F. Blum et al., “Leptin and variables of body adiposity, energy balance, and insulin resistance in a population-based study: the Hoorn study,” Diabetes Care, vol. 22, no. 7, pp. 1097–1104, 1999.
[214]  P. W. Franks, I. S. Farooqi, J. Luan et al., “Does physical activity energy expenditure explain the between-individual variation in plasma leptin concentrations after adjusting for differences in body composition?” Journal of Clinical Endocrinology and Metabolism, vol. 88, no. 7, pp. 3258–3263, 2003.
[215]  J. A. Houmard, J. H. Cox, P. S. MacLean, and H. A. Barakat, “Effect of short-term exercise training on leptin and insulin action,” Metabolism, vol. 49, no. 7, pp. 858–861, 2000.
[216]  E. Herrera and H. Ortega-Senovilla, “Disturbances in lipid metabolism in diabetic pregnancy—are these the cause of the problem?” Best Practice & Research, vol. 24, no. 4, pp. 515–525, 2010.
[217]  E. Sivan and G. Boden, “Free fatty acids, insulin resistance, and pregnancy,” Current Diabetes Reports, vol. 3, no. 4, pp. 319–322, 2003.
[218]  S. Furukawa, T. Fujita, M. Shimabukuro et al., “Increased oxidative stress in obesity and its impact on metabolic syndrome,” Journal of Clinical Investigation, vol. 114, no. 12, pp. 1752–1761, 2004.
[219]  L. P. Turcotte, E. A. Richter, and B. Kiens, “Increased plasma FFA uptake and oxidation during prolonged exercise in trained vs. Untrained humans,” American Journal of Physiology, vol. 262, no. 6, pp. E791–E799, 1992.
[220]  R. J. Tunstall, K. A. Mehan, G. D. Wadley et al., “Exercise training increases lipid metabolism gene expression in human skeletal muscle,” American Journal of Physiology, vol. 283, no. 1, pp. E66–E72, 2002.
[221]  H. A. Keizer, G. Schaart, N. N. Tandon, J. F. C. Glatz, and J. J. F. P. Luiken, “Subcellular immunolocalisation of fatty acid translocase (FAT)/CD36 in human type-1 and type-2 skeletal muscle fibres,” Histochemistry and Cell Biology, vol. 121, no. 2, pp. 101–107, 2004.
[222]  S. Golbidi, S. A. Ebadi, and I. Laher, “Antioxidants in the treatment of diabetes,” Current Diabetes Reviews, vol. 7, pp. 106–125, 2011.
[223]  S. Golbidi and I. Laher, “Antioxidant therapy in human endocrine disorders,” Medical Science Monitor, vol. 16, no. 1, pp. RA9–RA24, 2010.
[224]  M. T. Coughlan, P. P. Vervaart, M. Permezel, H. M. Georgiou, and G. E. Rice, “Altered placental oxidative stress status in gestational diabetes mellitus,” Placenta, vol. 25, no. 1, pp. 78–84, 2004.
[225]  M. T. Coughlan, M. Permezel, H. M. Georgiou, and G. E. Rice, “Repression of oxidant-induced nuclear factor-κB activity mediates placental cytokine responses in gestational diabetes,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 7, pp. 3585–3594, 2004.
[226]  M. Lappas, M. Permezel, and G. E. Rice, “Release of proinflammatory cytokines and 8-isoprostane from placenta, adipose tissue, and skeletal muscle from normal pregnant women and women with gestational diabetes mellitus,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 11, pp. 5627–5633, 2004.
[227]  E. Peuchant, J. L. Brun, V. Rigalleau et al., “Oxidative and antioxidative status in pregnant women with either gestational or type 1 diabetes,” Clinical Biochemistry, vol. 37, no. 4, pp. 293–298, 2004.
[228]  U. Kamath, G. Rao, C. Raghothama, L. Rai, and P. Rao, “Erythrocyte indicators of oxidative stress in gestational diabetes,” Acta Paediatrica, vol. 87, no. 6, pp. 676–679, 1998.
[229]  V. Toescu, S. L. Nuttall, U. Martin et al., “Changes in plasma lipids and markers of oxidative stress in normal pregnancy and pregnancies complicated by diabetes,” Clinical Science, vol. 106, no. 1, pp. 93–98, 2004.
[230]  N. Inoue, S. Ramasamy, T. Fukai, R. M. Nerem, and D. G. Harrison, “Shear stress modulates expression of Cu/Zn superoxide dismutase in human aortic endothelial cells,” Circulation Research, vol. 79, no. 1, pp. 32–37, 1996.
[231]  J. Hollander, R. Fiebig, M. Gore et al., “Superoxide dismutase gene expression in skeletal muscle: fiber-specific adaptation to endurance training,” American Journal of Physiology, vol. 277, no. 3, pp. R856–R862, 1999.
[232]  F. Moien-Afshari, S. Ghosh, M. Khazaei, T. J. Kieffer, R. W. Brownsey, and I. Laher, “Exercise restores endothelial function independently of weight loss or hyperglycaemic status in db/db mice,” Diabetologia, vol. 51, no. 7, pp. 1327–1337, 2008.
[233]  S. Sankaralingam, Y. Jiang, S. T. Davidge, and S. Yeo, “Effect of exercise on vascular superoxide dismutase expression in high-risk pregnancy,” American Journal of Perinatology, vol. 28, no. 10, pp. 803–810, 2011.
[234]  F. W. Wagey, “Pregnancy exercise increase enzymatic antioxidant in pregnant women,” Bali Medical Journal, vol. 1, pp. 36–39, 2012.

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