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Adam Gesing Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA
Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA

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Andrzej Bartke Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA

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Michal M Masternak Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA
Department of Internal Medicine, Department of Oncological Endocrinology, Burnett School of Biomedical Sciences, Institute of Human Genetics, Geriatrics Research, Southern Illinois University School of Medicine, 801 North Rutledge Street, Room 4389, Springfield, Illinois 62794-9628, USA

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Type 2 diabetes and obesity are very serious health problems in both developed and developing countries. An increased level of GH is known to promote insulin resistance. Transgenic (Tg) mice over-expressing bovine GH are short-living and characterized, among other traits, by hyperinsulinemia and increased insulin resistance in comparison with normal (N) mice. Pioglitazone (PIO) is a member of the thiazolidinediones – a group of insulin-sensitizing drugs that are selective agonists of peroxisome proliferator-activated receptor gamma (PPARγ). The aim of the study was to analyze the effects of PIO on the insulin-signaling pathway in Tg and N mice. Plasma levels of insulin and glucose as well as hepatic levels of proteins involved in insulin signaling were analyzed by ELISA or western blot methods. Treatment with PIO decreased plasma level of glucose in N mice only. Similarly, PIO increased insulin sensitivity (expressed as the relative insulin sensitivity index; RISI) only in N mice. In the liver, PIO decreased the phosphorylation of insulin receptor substrate-1 (IRS1) at a serine residue (Ser307-pS-IRS1), which inhibits insulin action, and had a tendency to increase tyrosine phosphorylation of IRS2 (Tyr-pY-IRS2) only in N mice but did not affect either of these parameters in Tg mice. Levels of total and phosphorylated mammalian target of rapamycin were increased in Tg mice. Moreover, the level of AKT2 was decreased by PIO in N mice only. In conclusion, the lack of improvement of insulin sensitivity in insulin-resistant Tg mice during PIO treatment indicates that chronically elevated GH levels can inhibit the beneficial effects of PIO on insulin signaling.

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Johanna G Miquet
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Lorena González
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Marina N Matos
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Christina E Hansen Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Geriatrics Research, Facultad de Farmacia y Bioquímica, Junín 956, C1113AAD Buenos Aires, Argentina

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Audreen Louis Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Geriatrics Research, Facultad de Farmacia y Bioquímica, Junín 956, C1113AAD Buenos Aires, Argentina

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Andrzej Bartke Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Geriatrics Research, Facultad de Farmacia y Bioquímica, Junín 956, C1113AAD Buenos Aires, Argentina

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Daniel Turyn
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Ana I Sotelo
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Chronically elevated levels of GH in GH-transgenic mice result in accelerated growth and increased adult body weight. We have previously described that the GH-induced JAK2/STAT5-signaling pathway is desensitized in the liver of transgenic mice overexpressing GH. However, these animals present increased circulating IGF-I levels, increased hepatic GHR expression, and liver organomegaly due to hypertrophy and hyperplasia, which frequently progress to hepatomas as the animals age, indicating that action of GH on the liver is not prevented. In the present study, we have evaluated other GH-signaling pathways that could be activated in the liver of GH-transgenic mice. Upon GH administration, normal mice showed an important increment in STAT3 phosphorylation level, but transgenic mice did not respond to acute GH stimulation. However, STAT3 was constitutively phosphorylated in transgenic mice, whereas its protein content was not increased. GH-transgenic mice showed overexpression of c-Src, accompanied by an elevation of its activity. Other signaling mediators including focal adhesion kinase, epidermal growth factor receptor, Erk, Akt, and mammalian target of rapamycin displayed elevated protein and basal phosphorylation levels in these animals. Thus, GH-overexpressing transgenic mice exhibit hepatic upregulation of signaling mediators related to cell proliferation, survival, and migration. The upregulation of these proteins may represent GH-signaling pathways that are constitutively activated in the presence of dramatically elevated GH levels throughout life. These molecular alterations could be implicated in the pathological alterations observed in the liver of GH-transgenic mice.

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Lorena González
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Ma. Eugenia Díaz
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Johanna G Miquet
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Ana I Sotelo
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Diego Fernández Departamento de Química Biológica, Cátedra de Bioquímica Humana, Geriatrics Research, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina

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Fernando P Dominici
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Andrzej Bartke Departamento de Química Biológica, Cátedra de Bioquímica Humana, Geriatrics Research, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956, 1113 Buenos Aires, Argentina

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Daniel Turyn
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Epidermal growth factor (EGF) is a key regulator of cell survival and proliferation involved in the pathogenesis and progression of different types of cancer. The EGF receptor (EGFR) is activated by binding of the specific ligand but also by transactivation triggered by different growth factors including GH. Chronically, elevated GH levels have been associated with the progression of hepatocellular carcinoma. Considering EGF and GH involvement in cell proliferation and their signaling crosstalk, the objective of the present study was to analyze GH modulatory effects on EGF signaling in liver. For this purpose, GH receptor-knockout (GHR-KO) and GH-overexpressing transgenic mice were used. EGFR content was significantly decreased in GHR-KO mice. Consequently, EGF-induced phosphorylation of EGFR, AKT, ERK1/2, STAT3, and STAT5 was significantly decreased in these mice. In contrast, EGFR content as well as its basal tyrosine phosphorylation was increased in transgenic mice overexpressing GH. However, EGF stimulation caused similar levels of EGFR, AKT, and ERK1/2 phosphorylation in normal and transgenic mice, while EGF induction of STAT3 and STAT5 phosphorylation was inhibited in the transgenic mice. Desensitization of the STATs was related to decreased association of these proteins to the EGFR and increased association between STAT5 and the tyrosine phosphatase SH2-containing phosphatase-2. While GHR knockout is associated with diminished expression of the EGFR and a concomitant decrease in EGF signaling, GH overexpression results in EGFR overexpression with different effects depending on the signaling pathway analyzed: AKT and ERK1/2 pathways are induced by EGF, while STAT3 and STAT5 activation is heterologously desensitized.

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Lorena González Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Ma Eugenia Díaz Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Johanna G Miquet Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Ana I Sotelo Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Diego Fernández Cátedra de Bioquímica Humana, Facultad de Medicina (UBA), Buenos Aires, Argentina

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Fernando P Dominici Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Andrzej Bartke Geriatrics Research, Departments of Internal Medicine and Physiology, School of Medicine, Southern Illinois University, Springfield, Illinois, USA

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Daniel Turyn Departamento de Química Biológica, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina

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Lorena González Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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Johanna G Miquet Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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Pablo E Irene Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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M Eugenia Díaz Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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Soledad P Rossi Instituto de Biología y Medicina Experimental, CONICET, Ciudad de Buenos Aires, Argentina

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Ana I Sotelo Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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Mónica B Frungieri Instituto de Biología y Medicina Experimental, CONICET, Ciudad de Buenos Aires, Argentina

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Cristal M Hill Departments of Internal Medicine and Physiology, Geriatrics Research, School of Medicine, Southern Illinois University, Springfield, Illinois, USA

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Andrzej Bartke Departments of Internal Medicine and Physiology, Geriatrics Research, School of Medicine, Southern Illinois University, Springfield, Illinois, USA

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Daniel Turyn Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Facultad de Farmacia y Bioquímica, Buenos Aires, Argentina

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Transgenic mice overexpressing growth hormone (GH) show increased hepatic protein content of the epidermal growth factor receptor (EGFR), which is broadly associated with cell proliferation and oncogenesis. However, chronically elevated levels of GH result in desensitization of STAT-mediated EGF signal and similar response of ERK1/2 and AKT signaling to EGF compared to normal mice. To ascertain the mechanisms involved in GH attenuation of EGF signaling and the consequences on cell cycle promotion, phosphorylation of signaling mediators was studied at different time points after EGF stimulation, and induction of proteins involved in cell cycle progression was assessed in normal and GH-overexpressing transgenic mice. Results from kinetic studies confirmed the absence of STAT3 and 5 activation and comparable levels of ERK1/2 phosphorylation upon EGF stimulation, which was associated with diminished or similar induction of c-MYC, c-FOS, c-JUN, CYCLIN D1 and CYCLIN E in transgenic compared to normal mice. Accordingly, kinetics of EGF-induced c-SRC and EGFR phosphorylation at activating residues demonstrated that activation of these proteins was lower in the transgenic mice with respect to normal animals. In turn, EGFR phosphorylation at serine 1046/1047, which is implicated in the negative regulation of the receptor, was increased in the liver of GH-overexpressing transgenic mice both in basal conditions and upon EGF stimulus. Increased basal phosphorylation and activation of the p38-mitogen-activated protein kinase might account for increased Ser 1046/1047 EGFR. Hyperphosphorylation of EGFR at serine residues would represent a compensatory mechanism triggered by chronically elevated levels of GH to mitigate the proliferative response induced by EGF.

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Marina C Muñoz
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Valeria Burghi
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Johanna G Miquet
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Jorge F Giani Departamento de Química Biológica, Departments of Biomedical Sciences and Pathology and Laboratory Medicine, Laboratorio de Medicina Experimental, Department of Internal Medicine, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956 (1113) Buenos Aires, Argentina

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Ricardo D Banegas
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Jorge E Toblli Departamento de Química Biológica, Departments of Biomedical Sciences and Pathology and Laboratory Medicine, Laboratorio de Medicina Experimental, Department of Internal Medicine, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956 (1113) Buenos Aires, Argentina

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Yimin Fang Departamento de Química Biológica, Departments of Biomedical Sciences and Pathology and Laboratory Medicine, Laboratorio de Medicina Experimental, Department of Internal Medicine, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956 (1113) Buenos Aires, Argentina

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Feiya Wang Departamento de Química Biológica, Departments of Biomedical Sciences and Pathology and Laboratory Medicine, Laboratorio de Medicina Experimental, Department of Internal Medicine, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956 (1113) Buenos Aires, Argentina

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Andrzej Bartke Departamento de Química Biológica, Departments of Biomedical Sciences and Pathology and Laboratory Medicine, Laboratorio de Medicina Experimental, Department of Internal Medicine, Facultad de Farmacia y Bioquímica, Instituto de Química y Fisicoquímica Biológicas (UBA-CONICET), Universidad de Buenos Aires, Junín 956 (1113) Buenos Aires, Argentina

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Fernando P Dominici
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The renin–angiotensin system (RAS) plays a crucial role in the regulation of physiological homeostasis and diseases such as hypertension, coronary artery disease, and chronic renal failure. In this cascade, the angiotensin-converting enzyme (ACE)/angiotensin II (Ang II)/AT1 receptor axis induces pathological effects, such as vasoconstriction, cell proliferation, and fibrosis, while the ACE2/Ang-(1–7)/Mas receptor axis is protective for end-organ damage. The altered function of the RAS could be a contributing factor to the cardiac and renal alterations induced by GH excess. To further explore this issue, we evaluated the consequences of chronic GH exposure on the in vivo levels of Ang II, Ang-(1–7), ACE, ACE2, and Mas receptor in the heart and the kidney of GH-transgenic mice (bovine GH (bGH) mice). At the age of 7–8 months, female bGH mice displayed increased systolic blood pressure (SBP), a high degree of both cardiac and renal fibrosis, as well as increased levels of markers of tubular and glomerular damage. Angiotensinogen abundance was increased in the liver and the heart of bGH mice, along with a concomitant increase in cardiac Ang II levels. Importantly, the levels of ACE2, Ang-(1–7), and Mas receptor were markedly decreased in both tissues. In addition, Ang-(1–7) administration reduced SBP to control values in GH-transgenic mice, indicating that the ACE2/Ang-(1–7)/Mas axis is involved in GH-mediated hypertension. The data indicate that the altered expression profile of the ACE2/Ang-(1–7)/Mas axis in the heart and the kidney of bGH mice could contribute to the increased incidence of hypertension, cardiovascular, and renal alterations observed in these animals.

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Ellen R Lubbers Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Edward O List Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Adam Jara Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine
Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Lucila Sackman-Sala Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Jose Cordoba-Chacon Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Manuel D Gahete Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Rhonda D Kineman Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Ravneet Boparai Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Andrzej Bartke Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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John J Kopchick Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine
Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Darlene E Berryman Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine
Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine
Edison Biotechnology Institute, Department of Biomedical Sciences, School of Applied Health Sciences and Wellness, Jesse Brown VA Medical Center, Southern Illinois University School of Medicine

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Adiponectin is positively correlated with longevity and negatively correlated with many obesity-related diseases. While there are several circulating forms of adiponectin, the high-molecular-weight (HMW) version has been suggested to have the predominant bioactivity. Adiponectin gene expression and cognate serum protein levels are of particular interest in mice with altered GH signaling as these mice exhibit extremes in obesity that are positively associated with insulin sensitivity and lifespan as opposed to the typical negative association of these factors. While a few studies have reported total adiponectin levels in young adult mice with altered GH signaling, much remains unresolved, including changes in adiponectin levels with advancing age, proportion of total adiponectin in the HMW form, adipose depot of origin, and differential effects of GH vs IGF1. Therefore, the purpose of this study was to address these issues using assorted mouse lines with altered GH signaling. Our results show that adiponectin is generally negatively associated with GH activity, regardless of age. Further, the amount of HMW adiponectin is consistently linked with the level of total adiponectin and not necessarily with previously reported lifespan or insulin sensitivity of these mice. Interestingly, circulating adiponectin levels correlated strongly with inguinal fat mass, implying that the effects of GH on adiponectin are depot specific. Interestingly, rbGH, but not IGF1, decreased circulating total and HMW adiponectin levels. Taken together, these results fill important gaps in the literature related to GH and adiponectin and question the frequently reported associations of total and HMW adiponectin with insulin sensitivity and longevity.

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