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K A Berghorn Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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P A Clark Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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B Encarnacion Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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C J DeRegis Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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J K Folger Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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M I Morasso Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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M J Soares Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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M W Wolfe Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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M S Roberson Department of Biomedical Sciences, Cornell University, Ithaca, New York, USA
Developmental Skin Biology Unit, NIAMS, Bethesda, Maryland, USA
Department of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas City, Kansas, USA
Department of Molecular and Integrative Physiology, University of Kansas Medical Center, Kansas City, Kansas, USA

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Distal-less 3 (Dlx3) is a homeobox factor that functions as a placental-specific transcriptional regulator. Dlx3 null mice (−/−) have compromised placental development and do not survive in utero past embryonic day (E) 9.5. The current studies were undertaken to examine the expression of Dlx3 in mouse placenta during gestation, and to determine whether Dlx3 was involved in placental progesterone production. Dlx3 was not detectable at E8.5 but was detected in E9.5 placenta with continuing but diminished expression through E15.5. Dlx3 immuno-localization was restricted to the labyrinth, was nuclear and was found in cytokeratin-positive cells. Previous studies in choriocarcinoma cell lines support the conclusion that Dlx3 is required for expression of 3′-hydroxysteroid dehydrogenase VI (3βHSD VI), an obligate enzyme in the production of progesterone by trophoblast giant cells. In a rat trophoblast stem cell line (Rcho-1), Dlx3 expression was non-detectable in Rcho-1 cells induced to differ-entiate using mitogen withdrawal. In vitro progesterone production in placental cultures and 3βHSD VI mRNA from Dlx3 (+/+), (+/−) and (−/−) mice were equivalent. In situ hybridization for 3βHSD VI revealed mRNA expression restricted to trophoblast giants cells with no detectable expression in the labyrinth suggesting that Dlx3 and 3βHSD VI were not colocalized within the placenta. These studies support the conclusion that Dlx3 protein expression is restricted to the labyrinth region of the murine placenta into late gestation and that Dlx3 does not appear to be expressed in trophoblast giant cells. Further, loss of Dlx3 was not correlated with synthesis of progesterone from E9.5 mouse placentas.

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06217
Volume/Issue:
Volume 186: Issue 2
Free access
Ya Liu Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Xiaoqing Zhou Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Ye Xiao Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Changjun Li Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Yan Huang Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Qi Guo Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Tian Su Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Lei Fu Department of Infectious Diseases, Xiangya Hospital of Central South University, Changsha, Hunan, China

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Liping Luo Department of Endocrinology, Endocrinology Research Center, Xiangya Hospital of Central South University, Changsha, Hunan, China

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obese db/db mice, leading us to hypothesize that miR-188 plays an important role in glucose and lipid homeostasis. After 3 months of high-fat diet feeding, the level of liver steatosis and hepatic insulin resistance was ameliorated in miR-188-null mice

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-20-0033
Volume/Issue:
Volume 245: Issue 3
Restricted access
Lucy V Norling Barts and The London School of Medicine, The William Harvey Research Institute, Centre for Biochemical Pharmacology, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK

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Mauro Perretti Barts and The London School of Medicine, The William Harvey Research Institute, Centre for Biochemical Pharmacology, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK

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Dianne Cooper Barts and The London School of Medicine, The William Harvey Research Institute, Centre for Biochemical Pharmacology, Queen Mary University of London, Charterhouse Square, London EC1M 6BQ, UK

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conditions. Table 1 outlines the phenotypes of these mice. Table 1 Phenotype of galectin null mice Disease model/inflammogen Phenotype References Null mouse Galectin-1 Peritonitis Increased neutrophil recruitment www.functionalglycomics.org/ IL1B

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-08-0512
Volume/Issue:
Volume 201: Issue 2
Free access
Run Yu UCLA School of Medicine, Cedars-Sinai Research Institute, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Room D3066, Los Angeles, California 90048, USA

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Martha Cruz-Soto UCLA School of Medicine, Cedars-Sinai Research Institute, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Room D3066, Los Angeles, California 90048, USA

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Sergio Li Calzi UCLA School of Medicine, Cedars-Sinai Research Institute, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Room D3066, Los Angeles, California 90048, USA

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Hongxiang Hui UCLA School of Medicine, Cedars-Sinai Research Institute, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Room D3066, Los Angeles, California 90048, USA

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Shlomo Melmed UCLA School of Medicine, Cedars-Sinai Research Institute, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Room D3066, Los Angeles, California 90048, USA

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-cell replication rather than differentiation was likely the major cause of diminished β-cell mass in PTTG-null mice. To study the mechanisms of defective β-cell replication after PTTG deletion, we next tested the hypothesis that murine PTTG (mPTTG

Article Type:
Research Article
DOI:
https://doi.org/10.1677/joe.1.06885
Volume/Issue:
Volume 191: Issue 1
Free access
Md Nurul Islam Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan

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Yuichiro Mita Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan
Systems Life Sciences Laboratory, Department of Medical Life Systems, Faculty of Life and Medical Sciences, Doshisha University, Kyoto, Japan

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Keisuke Maruyama Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan

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Ryota Tanida Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan
Department of Sports and Fitness, Faculty of Wellness, Shigakkan University, Aichi, Japan

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Weidong Zhang Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan

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Hideyuki Sakoda Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan

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Masamitsu Nakazato Division of Neurology, Respirology, Endocrinology and Metabolism, Department of Internal Medicine, Faculty of Medicine, University of Miyazaki, Miyazaki, Japan
CREST (Japan) Agency for Medical Research and Development (A-MED) 1-7-1 Otemachi, Tokyo, Japan

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ghrelin was introduced through the inferior vena cava. Two hours after ghrelin administration, plasma and tissue samples were collected for LEAP2 analysis. 38-week-old GHSR-null mice ( Zigman et al. 2005 ) which harbor a loxP-flanked transcriptional

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-19-0102
Volume/Issue:
Volume 244: Issue 1
Open access
S F Ahmed
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C Farquharson Developmental Endocrinology Research Group, Bone Biology Group, Division of Developmental Medicine, Department of Child Health, Royal Hospital For Sick Children, University of Glasgow, Yorkhill, Glasgow G3 8SJ, UK

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. In contrast, the locally produced skeletal IGF1 plays a more significant role in trabecular bone integrity. This is demonstrated in transgenic mice expressing IGF1 in osteoblasts and in conditional igf1 receptor null mice, which display decreased

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-10-0045
Volume/Issue:
Volume 206: Issue 3
Free access
Gulizar Issa Ameen Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK

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Silvia Mora Department of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK

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(catalogue number A2066, 1:2000) antibodies were from Sigma-Aldrich, and anti-GLUT4 antibody was a gift from Dr Jeffrey Pessin (Albert Einstein, NY, USA). Animals, genotyping and diet intervention c-Cbl-null mice on C57BL6/J background were obtained

Article Type:
Research Article
DOI:
https://doi.org/10.1530/JOE-17-0359
Volume/Issue:
Volume 236: Issue 1
Open access
Eugenia H Goulding Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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Sylvia C Hewitt Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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Noriko Nakamura Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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Katherine Hamilton Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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Kenneth S Korach Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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Edward M Eddy Gamete Biology Group, Receptor Biology Group, Laboratory of Reproduction and Developmental Toxicology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, North Carolina 27709, USA

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significantly higher in 6-week-old mice and significantly lower in adult ERα-null mice than those of WT mice; 2) epididymal sperm counts were significantly lower in 6-week-old and adult ERα-null mice than those of WT mice; 3) motility of sperm from the cauda

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-10-0290
Volume/Issue:
Volume 207: Issue 3
Free access
C D Simmons
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J M P Pabona
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Z Zeng
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M C Velarde
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D Gaddy
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F A Simmen
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R C M Simmen Department of Physiology and Biophysics, Arkansas Children's Nutrition Center, University of Arkansas for Medical Sciences, 4301 W Markham Street, Little Rock, Arkansas 72202, USA

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motifs that are important for binding to GC-rich sequences in DNA ( Imataka et al . 1992 ). By using Klf9 null mice and endometrial cell lines with KLF9 knockdown in vitro , our laboratory has shown that KLF9 is a progesterone receptor (PGR) co

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0474
Volume/Issue:
Volume 205: Issue 2
Free access
Chalida Nakalekha Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Chieko Yokoyama Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Hiroyuki Miura Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Neil Alles Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Kazuhiro Aoki Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Keiichi Ohya Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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Ikuo Morita Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School
Departments of, Cellular Physiological Chemistry, Fixed Prosthodontics, International Research Center for Molecular Science in Tooth and Bone Diseases (Global COE program), Institute of Cellular and System Medicine, Department of Hard Tissue Engineering (Pharmacology), Graduate School

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mice. Based on our results, the high bone mass phenotype in aged PGIS-null mice was a result from net favor of bone formation and mineralization. This phenotype was rescued in the offspring of PGIS-knockout mice crossbred with PGIS-transgenic mice. This

Article Type:
Research Article
DOI:
https://doi.org/10.1677/JOE-09-0376
Volume/Issue:
Volume 204: Issue 2
Free access