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- Author: Antonio Andrés x
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Unidade de Suprarrenal, Instituto do Câncer de São Paulo ICESP, Département de Médecine, Disciplina de Endocrinologia e Metabologia, Hospital das Clínicas, Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
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Unidade de Suprarrenal, Instituto do Câncer de São Paulo ICESP, Département de Médecine, Disciplina de Endocrinologia e Metabologia, Hospital das Clínicas, Faculdade de Medicina da Universidade de São Paulo, São Paulo, Brazil
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ACTH-independent macronodular adrenal hyperplasia is a rare cause of Cushing's syndrome (CS), accounting for <2% of all endogenous CS cases; however it is more frequently identified incidentally with sub-clinical cortisol secretion. Recently, cortisol secretion has been shown to be regulated by ectopic corticotropin, which is in turn produced by clusters of steroidogenic cells of the hyperplastic adrenal nodules. Hence, the term ‘ACTH-independent’ is not entirely appropriate for this disorder. Accordingly, the disease is designated primary macronodular adrenal hyperplasia (PMAH) in this review article. The means by which cortisol production is regulated in PMAH despite the suppressed levels of ACTH of pituitary origin is exceedingly complex. Several molecular events have been proposed to explain the enhanced cortisol secretion, increased cell proliferation, and nodule formation in PMAH. Nonetheless, the precise sequence of events and the molecular mechanisms underlying this condition remain unclear. The purpose of this review is therefore to present new insights on the molecular and genetic profile of PMAH pathophysiology, and to discuss the implications for disease progression.
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The role of central leptin in regulating the heart from lipid accumulation in lean leptin-sensitive animals has not been fully elucidated. Herein, we investigated the effects of central leptin infusion on the expression of genes involved in cardiac metabolism and its role in the control of myocardial triacylglyceride (TAG) accumulation in adult Wistar rats. Intracerebroventricular (icv) leptin infusion (0.2 µg/day) for 7 days markedly decreased TAG levels in cardiac tissue. Remarkably, the cardiac anti-steatotic effects of central leptin were associated with the selective upregulation of gene and protein expression of peroxisome proliferator-activated receptor β/δ (PPARβ/δ, encoded by Pparb/d) and their target genes, adipose triglyceride lipase (encoded by Pnpla2, herefater referred to as Atgl), hormone sensitive lipase (encoded by Lipe, herefater referred to as Hsl), pyruvate dehydrogenase kinase 4 (Pdk4) and acyl CoA oxidase 1 (Acox1), involved in myocardial intracellular lipolysis and mitochondrial/peroxisomal fatty acid utilization. Besides, central leptin decreased the expression of stearoyl-CoA deaturase 1 (Scd1) and diacylglycerol acyltransferase 1 (Dgat1) involved in TAG synthesis and increased the CPT-1 independent palmitate oxidation, as an index of peroxisomal β-oxidation. Finally, the pharmacological inhibition of PPARβ/δ decreased the effects on gene expression and cardiac TAG content induced by leptin. These results indicate that leptin, acting at central level, regulates selectively the cardiac expression of PPARβ/δ, contributing in this way to regulate the cardiac TAG accumulation in rats, independently of its effects on body weight.
Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Centro de Biología Molecular ‘Severo Ochoa’, Facultad de Ciencias, Universidad Autónoma, Campus de Cantoblanco, 28049 Madrid, Spain
Area de Bioquímica, Facultad de Químicas, Centro Regional de Investigaciones Biomédicas (CRIB), Universidad de Castilla La Mancha, 13071 Ciudad Real, Spain
Facultad de Ciencias de la Salud, Universidad Rey Juan Carlos, 28922 Alcorcón, Madrid, Spain
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Insulin resistance develops with ageing in humans and rodents. Here, we have studied the evolution of insulin sensitivity with ageing trying to discriminate the role of adiposity from that of ageing in this process. We performed oral glucose tolerance tests and determined overall and tissue-specific glucose utilization under euglycemic-hyper-insulinemic conditions in 3-, 8-, and 24-month-old rats fed ad libitum, and in 8- and 24-month-old rats after 3 months of calorie restriction. Body composition and adipocyte-derived cytokines such as leptin, resistin, and adiponectin were analyzed. Overall insulin sensitivity decreases with ageing. Calorie restriction improves global insulin sensitivity in 8- but not in 24-month-old rats. Insulin-stimulated glucose utilization in adipose tissues decreases in 8 months, while in oxidative muscles it reaches significance only in older rats. Calorie restriction restores adipose tissue insulin sensitivity only in 8-month-old rats and no changes are observed in muscles of 24-month-old rats. Resistin and leptin increase with ageing. Food restriction lowers resistin and increases adiponectin in 8-month-old rats and decreases leptin in both ages. Visceral and total fat increase with ageing and decrease after calorie restriction. We conclude that accretion of visceral fat plays a key role in the development of insulin resistance after sexual maturity, which is reversible by calorie restriction. With aging, accumulation of retroperitoneal and total body fat leads to impaired muscle glucose uptake and to a state of insulin resistance that is difficult to reverse.
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The aim of this study was to investigate the insulin clearance in diet-induced obese (DIO) mice submitted to acute endurance exercise (3h of treadmill exercise at 60–70% VO2max). Glucose-stimulated insulin secretion in isolated islets; ipGTT; ipITT; ipPTT; in vivo insulin clearance; protein expression in liver, skeletal muscle, and adipose tissue (insulin degrading enzyme (IDE), insulin receptor subunitβ(IRβ), phospho-Akt (p-Akt) and phospho-AMPK (p-AMPK)), and the activity of IDE in the liver and skeletal muscle were accessed. In DIO mice, acute exercise reduced fasting glycemia and insulinemia, improved glucose and insulin tolerance, reduced hepatic glucose production, and increased p-Akt protein levels in liver and skeletal muscle and p-AMPK protein levels in skeletal muscle. In addition, insulin secretion was reduced, whereas insulin clearance and the expression of IDE and IRβ were increased in liver and skeletal muscle. Finally, IDE activity was increased only in skeletal muscle. In conclusion, we propose that the increased insulin clearance and IDE expression and activity, primarily, in skeletal muscle, constitute an additional mechanism, whereby physical exercise reduces insulinemia in DIO mice.
Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Department of Morphological Sciences, Universidad de Córdoba, Córdoba, Spain
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Service of Endocrinology and Nutrition, Hospital Universitario Reina Sofía, Córdoba, Spain
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Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Department of Cell Biology, Physiology and Immunology, Universidad de Córdoba, Córdoba, Spain
Hospital Universitario Reina Sofía, Córdoba, Spain
CIBER Fisiopatología de la Obesidad y Nutrición (CIBERObn), Córdoba, Spain
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Somatostatin analogs (SSA) are the mainstay of pharmacological treatment for pituitary adenomas. However, some patients escape from therapy with octreotide, a somatostatin receptor 2 (sst2)-preferring SSA, and pasireotide, a novel multi-sst-preferring SSA, may help to overcome this problem. It has been proposed that correspondence between sst1-sst5 expression pattern and SSA-binding profile could predict patient’s response. To explore the cellular/molecular features associated with octreotide/pasireotide response, we performed a parallel comparison of their in vitro effects, evaluating sst1-sst5 expression, intracellular Ca2+ signaling ([Ca2+]i), hormone secretion and cell viability, in a series of 85 pituitary samples. Somatotropinomas expressed sst5>sst2, yet octreotide reduced [Ca2+]i more efficiently than pasireotide, while both SSA similarly decreased growth hormone release/expression and viability. Corticotropinomas predominantly expressed sst5, but displayed limited response to pasireotide, while octreotide reduced functional endpoints. Non-functioning adenomas preferentially expressed sst3 but, surprisingly, both SSA increased cell viability. Prolactinomas mainly expressed sst1 but were virtually unresponsive to SSA. Finally, both SSA decreased [Ca2+]i in normal pituitaries. In conclusion, both SSA act in vitro on pituitary adenomas exerting both similar and distinct effects; however, no evident correspondence was found with the sst1-sst5 profile. Thus, it seems plausible that additional factors, besides the simple abundance of a given sst, critically influence the SSA response.
