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A microdeletion in the ligand binding domain of human steroidogenic factor 1 causes XY sex reversal without adrenal insufficiency.
Correa RV, Domenice S, Bingham NC, Billerbeck AE, Rainey WE, Parker KL, Mendonca BB
(2004) J Clin Endocrinol Metab 89: 1767-72
MeSH Terms: Adrenal Glands, Adult, Base Sequence, DNA-Binding Proteins, Disorders of Sex Development, Female, Fushi Tarazu Transcription Factors, Gene Deletion, Genes, Dominant, Genitalia, Female, Homeodomain Proteins, Humans, Ligands, Mutation, Receptors, Cytoplasmic and Nuclear, Steroidogenic Factor 1, Transcription Factors, Transcription, Genetic
Show Abstract · Added October 13, 2015
Steroidogenic factor 1 (SF-1) is an orphan nuclear receptor that plays key roles in endocrine development and function. Knockout mice lacking SF-1 have adrenal and gonadal agenesis, impaired gonadotropin expression, and structural abnormalities of the ventromedial hypothalamic nucleus. Previous studies have identified three human subjects with mutations in SF-1 causing adrenocortical insufficiency with varying degrees of gonadal dysfunction. We now describe a novel 8-bp microdeletion of SF-1, isolated from a 46, XY patient who presented with gonadal agenesis but normal adrenal function, which causes premature termination upstream of sequences encoding the activation function 2 domain. In cell transfection experiments, the mutated protein possessed no intrinsic transcriptional activity but rather inhibited the function of the wild-type protein in most cell types. To our knowledge, this is the first example of an apparent dominant-negative effect of a SF-1 mutation in humans. These findings, which define a SF-1 mutation that apparently differentially affects its transcriptional activity in vivo in the adrenal cortex and the gonads, may be relevant to the cohort of patients who present with 46, XY sex reversal but normal adrenal function.
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18 MeSH Terms
Role of Cl- co-transporters in the excitation produced by GABAA receptors in juvenile bovine adrenal chromaffin cells.
Xie Z, Currie KP, Cahill AL, Fox AP
(2003) J Neurophysiol 90: 3828-37
MeSH Terms: Adrenal Glands, Animals, Bicuculline, Calcium, Calcium Channels, Catecholamines, Cats, Cattle, Cells, Cultured, Chromaffin Cells, Electrophysiology, GABA Agonists, GABA Antagonists, Intracellular Fluid, Lanthanum, Membrane Potentials, Muscimol, Patch-Clamp Techniques, Receptors, Cholinergic, Receptors, GABA-A, Symporters
Show Abstract · Added March 30, 2013
GABA is the primary inhibitory neurotransmitter in the adult mammalian brain. However, in neonatal animals, activation of Cl(-)-permeable GABA receptors is excitatory and appears to depend on the expression of a Na(+)-K(+)-2Cl- cotransporter (NKCC) that elevates intracellular Cl- levels, leading to a depolarized Cl- equilibrium potential (ECl). The change from excitation to inhibition appears to involve the expression of the K+/Cl- co-transporter, KCC2, which lowers intracellular Cl- levels resulting in a hyperpolarized ECl. In this study, we show that bovine chromaffin cells from 4- to 5-mo-old animals are excited by GABA. Activation of GABAA receptors depolarizes the cells, opens voltage-dependent Ca2+ channels, elevates [Ca2+]i, and promotes the release of catecholamines. Blockade of voltage-dependent Ca2+ channels prevents the elevation of [Ca2+]i by GABA. The extrapolated anion reversal potential in these cells is approximately -28 mV, indicating a resting intracellular anion concentration of approximately 50 mM. Expression of KCC2 protein was not detected in the juvenile chromaffin cells. In contrast, clear expression of NKCC1 was observed. Blockade of NKCC1 should reduce the intracellular Cl- concentration and hyperpolarize ECl. Bumetanide, an NKCC1 blocker, reduced the elevation of [Ca2+]i by GABA. In some cells, activation of GABAA receptors inhibits responses to excitatory neurotransmitters, even though GABA itself is depolarizing. Co-activation of cholinergic and GABAA receptors in chromaffin cells produced elevations in [Ca2+]i that were comparable to those produced by cholinergic receptors alone. Our data showing the selective expression of chloride co-transporters and the resulting strongly depolarized anion reversal potential may help explain how activation of GABAA receptors causes sufficient excitation to elicit catecholamine release from chromaffin cells.
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21 MeSH Terms
The hypothalamic-pituitary-adrenal axis in the pathogenesis of rheumatic diseases.
Crofford LJ
(2002) Endocrinol Metab Clin North Am 31: 1-13
MeSH Terms: Adrenal Glands, Animals, Arthritis, Rheumatoid, Disease Models, Animal, Feedback, Fibromyalgia, Humans, Hypothalamus, Immunity, Lupus Erythematosus, Systemic, Neurosecretory Systems, Pituitary Gland, Rheumatic Diseases
Show Abstract · Added September 18, 2013
Many studies have demonstrated altered HPA axis activity in patients with rheumatic diseases. In the case of autoimmune inflammatory diseases, circumstantial evidence suggests that failure of the neuroendocrine-immune regulatory loop may lead to insufficient production of endogenous glucocorticoid. Nevertheless, in human autoimmune disease, it is not possible to determine if altered HPA axis activity predates the onset of chronic inflammation. Animal studies and some early genetic studies in RA patients lend credibility to the argument that insufficient HPA axis response to inflammatory stimuli may increase susceptibility to, or severity of, these diseases. Most patients with rheumatic diseases complain of musculoskeletal pain. There is evidence of HPA axis involvement in acute and chronic pain. In the case of FM, pain cannot be explained on the basis of inflammation or altered musculoskeletal anatomy. This has led to the hypothesis that central nervous system mechanisms contribute to the symptom of somatic pain. Again, it is unclear if the observed HPA axis abnormalities reflect pre-existing vulnerability to the FM spectrum of disease, or whether chronic somatic symptoms alter HPA axis activity. Availability of technology to study better central components of the HPA axis may shed further light on its role in the pathogenesis of inflammatory autoimmune rheumatic diseases and musculoskeletal pain syndromes.
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13 MeSH Terms
Differential facilitation of N- and P/Q-type calcium channels during trains of action potential-like waveforms.
Currie KP, Fox AP
(2002) J Physiol 539: 419-31
MeSH Terms: Action Potentials, Adrenal Glands, Animals, Calcium Channels, N-Type, Calcium Channels, P-Type, Calcium Channels, Q-Type, Cattle, Cells, Cultured, Electric Stimulation, Electrophysiology, Ion Channel Gating, Neuronal Plasticity, Neurons, Neurotransmitter Agents, Patch-Clamp Techniques, Recombinant Proteins
Show Abstract · Added March 30, 2013
Inhibition of presynaptic voltage-gated calcium channels by direct G-protein betagamma subunit binding is a widespread mechanism that regulates neurotransmitter release. Voltage-dependent relief of this inhibition (facilitation), most likely to be due to dissociation of the G-protein from the channel, may occur during bursts of action potentials. In this paper we compare the facilitation of N- and P/Q-type Ca(2+) channels during short trains of action potential-like waveforms (APWs) using both native channels in adrenal chromaffin cells and heterologously expressed channels in tsA201 cells. While both N- and P/Q-type Ca(2+) channels exhibit facilitation that is dependent on the frequency of the APW train, there are important quantitative differences. Approximately 20 % of the voltage-dependent inhibition of N-type I(Ca) was reversed during a train while greater than 40 % of the inhibition of P/Q-type I(Ca) was relieved. Changing the duration or amplitude of the APW dramatically affected the facilitation of N-type channels but had little effect on the facilitation of P/Q-type channels. Since the ratio of N-type to P/Q-type Ca(2+) channels varies widely between synapses, differential facilitation may contribute to the fine tuning of synaptic transmission, thereby increasing the computational repertoire of neurons.
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16 MeSH Terms
Sonographic findings in infants with congenital adrenal hyperplasia.
Hernanz-Schulman M, Brock JW, Russell W
(2002) Pediatr Radiol 32: 130-7
MeSH Terms: Adrenal Glands, Adrenal Hyperplasia, Congenital, Diagnosis, Differential, Female, Humans, Infant, Infant, Newborn, Male, Sensitivity and Specificity, Sex Determination Analysis, Steroid 11-beta-Hydroxylase, Steroid 21-Hydroxylase, Ultrasonography
Show Abstract · Added March 24, 2014
BACKGROUND - Congenital adrenal hyperplasia (CAH) results from several autosomal recessive errors in adrenal steroidogenesis, leading to masculinization of female fetuses and potential salt-losing crises in male and female infants. Definitive diagnosis of CAH is made with biochemical studies, but results are not immediately available. Our purpose is to assess the utility of sonography in the accurate diagnosis of CAH.
PATIENTS AND METHODS - Sixteen patients with diagnosis of adrenogenital syndrome or ambiguous genitalia from January 1990 to January 1998 were identified: 9 patients with CAH, 7 patients without CAH who served as controls. Prospective sonographic diagnoses were correlated with biochemical diagnoses.
RESULTS - Of the 16 patients, 8 had prospectively enlarged adrenal glands, subsequently shown to have CAH due to 21-hydroxylase or 11beta-hydroxylase deficiency. Adrenals were normal in a pretreated infant, and in available follow-up scans. The seven patients without CAH had prospectively normal adrenal ultrasounds.
CONCLUSIONS - These data support the premise that sonography can be utilized as a rapid and accurate diagnostic tool in infants suspected of congenital adrenal hyperplasia.
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13 MeSH Terms
B-Myc is preferentially expressed in hormonally-controlled tissues and inhibits cellular proliferation.
Gregory MA, Xiao Q, Cornwall GA, Lutterbach B, Hann SR
(2000) Oncogene 19: 4886-95
MeSH Terms: Adrenal Glands, Animals, Brain, COS Cells, Cell Division, Cell Nucleus, Chlorocebus aethiops, Cysteine Endopeptidases, DNA, Complementary, Epididymis, Female, Fibroblasts, Gene Expression Regulation, Genes, myc, Growth Inhibitors, Hormones, Male, Mammary Glands, Animal, Mice, Multienzyme Complexes, Nerve Tissue Proteins, Organ Specificity, Ovary, Phosphorylation, Pituitary Gland, Prostate, Proteasome Endopeptidase Complex, Protein Processing, Post-Translational, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins c-myc, Rats, Recombinant Fusion Proteins, Transfection, Ubiquitins, Uterus
Show Abstract · Added March 5, 2014
The myc family of genes plays an important role in several cellular processes including proliferation, apoptosis, differentiation, and transformation. B-myc, a relatively new and largely unstudied member of the myc family, encodes a protein that is highly homologous to the N-terminal transcriptional regulatory domain of c-Myc. Here, we show that high level B-myc expression is restricted to specific mouse tissues, primarily hormonally-controlled tissues, with the highest level of expression in the epididymis. We also report the identification of the endogenous B-Myc protein from mouse tissues. Like other Myc family proteins, B-Myc is a short-lived nuclear protein which is phosphorylated on residues Ser-60 and Ser-68. Rapid proteolysis of B-Myc occurs via the ubiquitin-proteasome pathway. Finally, we found that overexpression of B-Myc significantly slows the growth of Rat la fibroblasts and COS cells suggesting B-Myc functions as an inhibitor of cellular proliferation.
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35 MeSH Terms
Synergistic effect of adrenal steroids and angiotensin II on plasminogen activator inhibitor-1 production.
Brown NJ, Kim KS, Chen YQ, Blevins LS, Nadeau JH, Meranze SG, Vaughan DE
(2000) J Clin Endocrinol Metab 85: 336-44
MeSH Terms: Adrenal Cortex Hormones, Adrenal Glands, Aldosterone, Angiotensin II, Animals, Blotting, Northern, Cells, Cultured, Chromosome Mapping, Dexamethasone, Genes, Reporter, Humans, Hydrocortisone, Hyperaldosteronism, Muscle, Smooth, Vascular, Mutagenesis, Site-Directed, Plasminogen Activator Inhibitor 1, Rats, Tissue Plasminogen Activator, Transfection
Show Abstract · Added December 10, 2013
Recent data suggest an interaction between the renin-angiotensin-aldosterone system and fibrinolysis. Although previous work has focused on the effect of angiotensin II (Ang II) on plasminogen activator inhibitor (PAI-1) expression, the present study tests the hypothesis that aldosterone contributes to the regulation of PAI-1 expression. To test this hypothesis in vitro, luciferase reporter constructs containing the human PAI-1 promoter were transfected into rat aortic smooth muscle cells. Exposure of the cells to 100 nmol/L Ang II resulted in a 3-fold increase in luciferase activity. Neither 1 micromol/L dexamethasone nor 1 micromol/L aldosterone alone increased PAI-1 expression. However, both dexamethasone and aldosterone enhanced the effect of Ang II in a dose-dependent manner. This effect was abolished by mutation in the region of a putative glucocorticoid-responsive element. A similar interactive effect of Ang II and aldosterone was observed in cultured human umbilical vein endothelial cells. The time course of the effect of aldosterone on Ang II-induced PAI-1 expression was consistent with a classical mineralocorticoid receptor mechanism, and the effect of aldosterone on PAI-1 synthesis was attenuated by spironolactone. To determine whether aldosterone affected PAI-1 expression in vivo, we measured local venous PAI-1 antigen concentrations in six patients with primary hyperaldosteronism undergoing selective adrenal vein sampling. PAI-1 antigen, but not tissue plasminogen activator antigen, concentrations were significantly higher in adrenal venous blood than in peripheral venous blood. Taken together, these data support the hypothesis that aldosterone modulates the effect of Ang II on PAI-1 expression in vitro and in vivo in humans.
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19 MeSH Terms
Structure and localization of the rabbit prostaglandin EP3 receptor.
Breyer RM, Emeson RB, Davis LS, Breyer MD
(1997) Adv Exp Med Biol 400A: 261-8
MeSH Terms: Adrenal Glands, Amino Acid Sequence, Animals, Autoradiography, Cell Membrane, Cloning, Molecular, Gastric Mucosa, Kidney, Molecular Sequence Data, Protein Conformation, Rabbits, Receptors, Prostaglandin E, Receptors, Prostaglandin E, EP3 Subtype, Recombinant Proteins, Stomach
Added December 21, 2013
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15 MeSH Terms
Murine double nullizygotes of the angiotensin type 1A and 1B receptor genes duplicate severe abnormal phenotypes of angiotensinogen nullizygotes.
Tsuchida S, Matsusaka T, Chen X, Okubo S, Niimura F, Nishimura H, Fogo A, Utsunomiya H, Inagami T, Ichikawa I
(1998) J Clin Invest 101: 755-60
MeSH Terms: Adrenal Glands, Anesthetics, Angiotensin II, Angiotensinogen, Animals, Benzimidazoles, Blood Pressure, Imidazoles, Infusions, Intravenous, Kidney, Losartan, Mice, Mice, Knockout, Myocardium, Phenotype, Pyridines, Receptor, Angiotensin, Type 1, Receptors, Angiotensin, Saralasin, Staining and Labeling, Tetrazoles, Thiopental, Zygote, beta-Galactosidase
Show Abstract · Added January 20, 2012
Rodents are the unique species carrying duplicated angiotensin (Ang) type 1 (AT1) receptor genes, Agtr1a and Agtr1b. After separately generating Agtr1a and Agtr1b null mutant mice by gene targeting, we produced double mutant mice homozygous for both Agtr1a and Agtr1b null mutation (Agtr1a-/-; Agtr1b-/-) by mating the single gene mutants. Agtr1a-/-, Agtr1b-/- mice are characterized by normal in utero survival but decreased ex utero survival rate. After birth they are characterized by low body weight gain, marked hypotension, and abnormal kidney morphology including delayed maturity in glomerular growth, hypoplastic papilla, and renal arterial hypertrophy. These abnormal phenotypes are quantitatively similar to those found in mutant mice homozygous for the angiotensinogen gene (Agt-/-), indicating that major biological functions of endogenous Ang elucidated by the abnormal phenotypes of Agt-/- are mediated by the AT1 receptors. Infusion of Ang II, AT1 blockers, or an AT2 blocker was without effect on blood pressure in Agtr1a-/-; Agtr1b-/- mice, indicating that AT2 receptor does not exert acute depressor effects in these mice lacking AT1 receptors. Also, unlike Agt-/- mice, some Agtr1a-/-; Agtr1b-/- mice have a large ventricular septum defect, suggesting that another receptor such as AT2 is functionally activated in Agtr1a-/-, Agtr1b-/- mice.
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24 MeSH Terms
The homeodomain protein Pbx1 is involved in cAMP-dependent transcription of human CYP17.
Ogo A, Waterman MR, McAllister JM, Kagawa N
(1997) Arch Biochem Biophys 348: 226-31
MeSH Terms: Adrenal Glands, Animals, Base Sequence, Binding Sites, Cattle, Cell Line, Consensus Sequence, Cyclic AMP, Cyclic AMP-Dependent Protein Kinases, DNA-Binding Proteins, Genes, Reporter, Homeodomain Proteins, Humans, Luciferases, Oligodeoxyribonucleotides, Pre-B-Cell Leukemia Transcription Factor 1, Promoter Regions, Genetic, Proto-Oncogene Proteins, Recombinant Fusion Proteins, Sequence Deletion, Steroid 17-alpha-Hydroxylase, Transcription, Genetic, Transcriptional Activation, Transfection, Tumor Cells, Cultured
Show Abstract · Added February 12, 2015
Pbx1 is a homeodomain transcription factor involved in cAMP-dependent transcriptional regulation of the bovine CYP17 gene. In this study, we have investigated the involvement of Pbx1 in the transcriptional regulation of the human CYP17 gene. Although a sequence identical to previously determined Pbx-binding sites is not present in the promoter region of the human CYP17 gene, three putative Pbx-binding sites are identified by sequence similarity analysis. Coexpression of Pbx1 and a catalytic subunit of protein kinase A (PKA) greatly enhances reporter gene transcription via the 5'-flanking region of the human CYP17 gene. Upon gel shift analysis utilizing nuclear extracts from human adrenal H295R cells, one of the three putative Pbx1-binding sites, -250/-241 bp, shows the typical intense doublet observed with other Pbx-binding sites. 5'-Deletion analyses of the reporter construct containing this Pbx-binding site showed approximately sixfold induction by coexpression of Pbx1 and PKA compared to the basal transcription, suggesting that Pbx1 binds the -250/-241 bp sequence and participates in cAMP-dependent regulation of the human CYP17 gene.
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25 MeSH Terms