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Kaitlyn A Colglazier Lilly Diabetes Center of Excellence, Indiana Biosciences Research Institute, Indianapolis, Indiana, USA

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Noyonika Mukherjee Department of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA

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Christopher J Contreras Division of Endocrinology, Department of Medicine, Roudebush VA Medical Center and Indiana University School of Medicine, Indianapolis, Indiana, USA

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Andrew T Templin Lilly Diabetes Center of Excellence, Indiana Biosciences Research Institute, Indianapolis, Indiana, USA
Department of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA
Division of Endocrinology, Department of Medicine, Roudebush VA Medical Center and Indiana University School of Medicine, Indianapolis, Indiana, USA
Center for Diabetes and Metabolic Diseases, Indiana University School of Medicine, Indianapolis, Indiana, USA

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.1073/pnas.1111008108 ) Alberts B Johnson A Lewis J Raff M Roberts K & Walter P 2002 Programmed cell death (apoptosis). In Molecular Biology of the Cell, 4th ed . New York, NY, USA : Garland Science . Ankarcrona M Dypbukt JM Bonfoco

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Aune Koitmäe Institute of Neuroanatomy, University Medical Center Hamburg, Hamburg, Germany

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Yannik Karsten Institute of Neuroanatomy, University Medical Center Hamburg, Hamburg, Germany
Department of Genetics and Molecular Biology, Institute of Biology, University of Magdeburg, Magdeburg, Germany

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Xiaoyu Li Institute of Neuroanatomy, University Medical Center Hamburg, Hamburg, Germany
Department of Endocrinology, Zhongda Hospital, School of Medicine, Southeast University, Jiangsu, China

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Fabio Morellini Research Group Behavioral Biology, Center for Molecular Neurobiology, Hamburg, Germany

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Gabriele M Rune Institute of Cell Biology and Neurobiology, Universitätsmedizin Charité Berlin, Berlin, Germany

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Roland A Bender Institute of Neuroanatomy, University Medical Center Hamburg, Hamburg, Germany

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Biochemistry and Molecular Biology 127 358 – 366 . ( https://doi.org/10.1016/j.jsbmb.2011.07.002 ) Fellini L Schachner M & Morellini F 2006 Adult but not aged C57BL/6 male mice are capable of using geometry for orientation . Learning and Memory 13

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Eugen Brailoiu Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Siok L Dun Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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G Cristina Brailoiu Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Keisuke Mizuo Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Larry A Sklar Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Tudor I Oprea Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Eric R Prossnitz Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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Nae J Dun Department of Pharmacology, Temple University School of Medicine, 3420 North Broad Street, Philadelphia, Pennsylvania 19140, USA
Department of Pathology,
Division of Biocomputing, Department of Biochemistry and Molecular Biology and
Department of Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131, USA

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human pre-osteoclastic cells. Journal of Steroid Biochemistry and Molecular Biology 59 233 –240. Funakoshi T , Yanai A, Shinoda K, Kawano MM & Mizukami Y 2006 G protein-coupled receptor 30 is an estrogen

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Sang-Nam Lee Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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Bonnie Peng Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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Roxane Desjardins Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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John E Pintar Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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Robert Day Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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Iris Lindberg Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, 1901 Perdido Street, New Orleans, Louisiana 70112, USA
Department of Neuroscience and Cell Biology, University of Medicine and Dentistry of NJ, Piscataway, New Jersey 08854, USA
Département de Pharmacologie, Faculté de Mèdecine et Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Québec, Canada JIH 5N4

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–21477. Murphy BE 1991 Treatment of major depression with steroid suppressive drugs. Journal of Steroid Biochemistry and Molecular Biology 39 239 –244. Ortego J , Wollmann G & Coca-Prados M

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Yi Zhao Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Tao Liu Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Nina Zhang Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Fenghua Yi Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Qinghua Wang Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Ivan George Fantus Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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Tianru Jin Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, University of Toronto, Ontario, Canada
Departments of Physiology,
Medicine and
Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
Banting and Best Diabetes Center, Faculty of Medicine, University of Toronto, Ontario, Canada

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. Journal of Molecular Biology 337 647 –660. Wang P , Branch DR, Li H, Huiqin Li, Bali M, Schultz GA, Goss PE & Jin T 2003 The POU homeodomain protein OCT3 as a potential transcriptional activator for fibroblast growth

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Stefan Cuoni Teilmann Laboratory of Reproductive Biology, Juliane Marie Center, Rigshospitalet, Copenhagen, Denmark
Department of Paediatric Surgery, Section 4072, Rigshospitalet, Copenhagen, Denmark
Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, The August Krogh Building, Universitetsparken 13, DK-2100 Copenhagen, Denmark

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Christian Alexandro Clement Laboratory of Reproductive Biology, Juliane Marie Center, Rigshospitalet, Copenhagen, Denmark
Department of Paediatric Surgery, Section 4072, Rigshospitalet, Copenhagen, Denmark
Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, The August Krogh Building, Universitetsparken 13, DK-2100 Copenhagen, Denmark

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Jørgen Thorup Laboratory of Reproductive Biology, Juliane Marie Center, Rigshospitalet, Copenhagen, Denmark
Department of Paediatric Surgery, Section 4072, Rigshospitalet, Copenhagen, Denmark
Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, The August Krogh Building, Universitetsparken 13, DK-2100 Copenhagen, Denmark

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Anne Grete Byskov Laboratory of Reproductive Biology, Juliane Marie Center, Rigshospitalet, Copenhagen, Denmark
Department of Paediatric Surgery, Section 4072, Rigshospitalet, Copenhagen, Denmark
Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, The August Krogh Building, Universitetsparken 13, DK-2100 Copenhagen, Denmark

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Søren Tvorup Christensen Laboratory of Reproductive Biology, Juliane Marie Center, Rigshospitalet, Copenhagen, Denmark
Department of Paediatric Surgery, Section 4072, Rigshospitalet, Copenhagen, Denmark
Department of Biochemistry, Institute of Molecular Biology and Physiology, University of Copenhagen, The August Krogh Building, Universitetsparken 13, DK-2100 Copenhagen, Denmark

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receptors: degradation, transcriptional synergy, and nuclear association. Journal of Steroid Biochemistry and Molecular Biology 85 147 –157. Robker RL , Russell DL, Espey LL, Lydon JP, O’Malley BW & Richards JS 2000

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P Sluka Prince Henry’s Institute of Medical Research, Level 4, Block E, Monash Medical Centre, 246 Clayton Road, Clayton, Victoria 3168, Australia
Department of Anatomy and Cell Biology, Monash University, Clayton, Victoria 3168, Australia
Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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L O’Donnell Prince Henry’s Institute of Medical Research, Level 4, Block E, Monash Medical Centre, 246 Clayton Road, Clayton, Victoria 3168, Australia
Department of Anatomy and Cell Biology, Monash University, Clayton, Victoria 3168, Australia
Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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J R Bartles Prince Henry’s Institute of Medical Research, Level 4, Block E, Monash Medical Centre, 246 Clayton Road, Clayton, Victoria 3168, Australia
Department of Anatomy and Cell Biology, Monash University, Clayton, Victoria 3168, Australia
Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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P G Stanton Prince Henry’s Institute of Medical Research, Level 4, Block E, Monash Medical Centre, 246 Clayton Road, Clayton, Victoria 3168, Australia
Department of Anatomy and Cell Biology, Monash University, Clayton, Victoria 3168, Australia
Department of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA

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a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque. Molecular Biology of the Cell 10 4327 –4339. Dierich A , Sairam MR, Monaco L, Fimia GM, Gansmuller A, LeMeur M

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Michael Hastings Division of Neurobiology, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

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John S O’Neill Division of Neurobiology, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

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Elizabeth S Maywood Division of Neurobiology, MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK

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Daily and seasonal rhythms in the endocrine system are co-ordinated by a hypothalamic pacemaker, the suprachiasmatic nuclei (SCN) that is synchronised to solar time by direct retinal afferents. Individual SCN neurons are circadian clocks, their intrinsic oscillator consisting of a series of interlinked autoregulatory transcriptional/post-translational feedback loops incorporating Period (Per) and Cryptochrome (Cry) genes. Mutations that alter the rate of transcription of Per and Cry genes or the stability of Per and Cry proteins affect clock speed. Molecular timekeeping in SCN neurons is synchronised and sustained by interneuronal neuropeptidergic signals. A molecular clock mechanism comparable to that of the SCN is present in most major organ systems. These tissue clocks are synchronised by endocrine, autonomic and behavioural cues that are dependent on the SCN, and in turn they drive the circadian expression of local transcriptomes, thereby co-ordinating circadian metabolism and physiology. Rhythmic glucocorticoid signalling is a prominent mediator of SCN output and internal synchroniser. The role of local SCN-synchronised clocks in controlling vital processes, including xenobiotic detoxification, cell division and nutrient metabolism, is essential to health, and disturbances to circadian timing arising from modern working schedules are becoming recognised as an increasingly relevant factor in major systemic illness. Moreover, the newly identified molecular components of circadian control systems provide novel avenues for therapeutic intervention.

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Elyse P Lemke
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Betty M Adams
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Albina Jablonka-Shariff Department of Animal Science, Department of Molecular Biology and Pharmacology, University of California, Davis, California 95616, USA

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Irving Boime Department of Animal Science, Department of Molecular Biology and Pharmacology, University of California, Davis, California 95616, USA

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Thomas E Adams
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The biopotency of single-chain analogs of human hFSH, human chorionic gonadotropin (hCG), and a dually active gonadotropin construct (FcCGβα) was examined. Sheep (bwt=61.4±1.1 kg; n=6 ewes/treatment) received a single injection (5 IU/kg, i.v.) of the hFSH analog (Fcα), the hCG analog (CGβα), FcCGβα, or Fcα and CGβα. Control animals received conditioned media. Ovulation was induced 3 days after analog administration using hCG (1000 IU, i.v.). Basal serum concentrations of estradiol (E2) were maintained in control animals. Neither Fcα nor CGβα alone induced significant E2 production during the pre-hCG period. Conversely, serum concentrations of E2 were increased (P<0.05) 2 days after administration of FcCGβα or Fcα+ CGβα. Although P4 concentrations were maintained at basal levels in control animals, significant increase was noted in all other treatment groups during the post-hCG period. Final ovarian weight was significantly increased (P<0.05) in animals receiving Fcα, Fcα+ CGβα, or FcCGβα, but not CGβα alone. Most of the ovarian enlargement was attributed to the formation of corpora lutea. Collectively, these observations demonstrate that the single-chain analogs of the human gonadotropins are active in sheep. The construct with singular FSH activity supports follicle development but not E2 production. Conversely, the construct that incorporates β-domains from both CG and FSH has dual activity. The long-lived nature of the single-chain constructs suggests that these recombinant gonadotropins may be effective alternatives to pituitary- or placenta-derived gonadotropins in out-of-season breeding and/or superovulation protocols.

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Carmen Sanz Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Isabel Roncero Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Patricia Vázquez Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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M Angeles Navas Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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Enrique Blázquez Department of Biochemistry and Molecular Biology, Faculty of Medicine, Complutense University, 28040 Madrid, Spain

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In an attempt to study the role of glucokinase (GK) and the effects of glucose and peptides on GK gene expression and on the activity of this enzyme in the hypothalamus, we used two kinds of biological models: hypothalamic GT1-7 cells and rat hypothalamic slices. The expression of the GK gene in GT1-7 cells was reduced by insulin (INS) and was not modified by different glucose concentrations, while GK enzyme activities were significantly reduced by the different peptides. Interestingly, a distinctive pattern of GK activities between the ventromedial hypothalamus (VMH) and lateral hypothalamus (LH) were found, with higher enzyme activities in the VMH as the glucose concentrations rose, while LH enzyme activities decreased at 2.8 and 20 mM glucose, the latter effect being prevented by incubation with INS. These effects were produced only by d-glucose and the modifications found were due to GK, but not to other hexokinases. In addition, GK activities in the VMH and the LH were reduced by glucagon-like peptide 1, leptin, orexin B, INS, and neuropeptide Y (NPY), but this effect was only statistically significant for NPY in LH. Our results indicate that the effects of both glucose and peptides occur on GK enzyme activities rather than on GK gene transcription. Moreover, the effects of glucose and INS on GK activity suggest that in the brain GK behaves in a manner opposite to that in the liver, which might facilitate its role in glucose sensing. Finally, hypothalamic slices seem to offer a good physiological model to discriminate the effects between different areas.

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