Search Results
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Search for other papers by Yongho Lee in
Google Scholar
PubMed
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Search for other papers by Jeong Mo Kim in
Google Scholar
PubMed
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Department of Internal Medicine, Graduate School, Brain Korea 21 Project for Medical Science, Institute of Endocrine Research, Endocrinology, Biochemistry and Molecular Biology
Search for other papers by Eun Jig Lee in
Google Scholar
PubMed
, Germany). Luciferase activity was normalized as described previously ( Ishikawa et al . 2004 ). Real-time PCR To assess the level of gene expression, real-time RT-PCR was carried out on the experimental samples using ABI 7300 Sequence Detection System
Search for other papers by Jay H Lo in
Google Scholar
PubMed
Search for other papers by Pinwen Peter Chiou in
Google Scholar
PubMed
Search for other papers by C M Lin in
Google Scholar
PubMed
Search for other papers by Thomas T Chen in
Google Scholar
PubMed
Introduction Growth hormone (GH) is a pleiotropic hormone that mediates cellular metabolism, growth, and differentiation by regulating the expression of specific genes ( Schwartz et al. 2002 ). In mammals, several end target
Search for other papers by C L Render in
Google Scholar
PubMed
Search for other papers by K L Hull in
Google Scholar
PubMed
Search for other papers by S Harvey in
Google Scholar
PubMed
Abstract
It is well established that GH-like proteins and mRNA are present in extrapituitary tissues, but it is not known whether this reflects ectopic transcription of the pituitary GH gene or the expression of a closely related gene. This possibility was, therefore, further investigated.
Immunoreactive (IR) GH-like proteins were readily measured by RIA and immunoblotting in hypothalamic and extrahypothalamic brain tissues of the domestic fowl, in which GH-IR was similar in size and antigenicity to pituitary GH. RT-PCR of mRNA from these brain tissues, with oligonucleotide primers spanning the coding region of pituitary GH cDNA, also generated cDNA fragments identical in size (689 bp) to pituitary GH cDNA. The amplified brain cDNA sequences contained BamH1 and Rsa1 cleavage sites similar to those located in pituitary GH cDNA. These cDNA sequences also hybridized with a cDNA probe for chicken GH cDNA, producing moieties of expected size that were identical to the hybridizing moieties in pituitary tissue. The nucleotide sequences of the PCR products generated from hypothalamic and extrahypothalamic brain tissues, determined by a modified cycle dideoxy chain termination method, were also identical to pituitary GH cDNA. This homology extended over 594 bp of the hypothalamic cDNA fragment (spanning nucleotides 65 to 659 of the pituitary GH cDNA and its coding region for amino acids 4 to 201) and 550 bp of the extrahypothalamic cDNA fragment (spanning nucleotides 76 to 626 of pituitary GH cDNA and its coding region for amino acids 8 to 190).
These results clearly establish that pituitary GH mRNA sequences are transcribed in hypothalamic and extrahypothalamic tissues of the chicken brain, in which GH-IR proteins are abundantly located. However, as GH mRNA could not be detected in the chicken brain by Northern blotting, its turnover may be more rapid than in pituitary tissue. The local production of GH within the brain nevertheless suggests that it has paracrine roles in modulating neural or neuroendocrine function.
Journal of Endocrinology (1995) 147, 413–422
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Hannah J Welters in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Sabine Senkel in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Ludger Klein-Hitpass in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Silke Erdmann in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Heike Thomas in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Lorna W Harries in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Ewan R Pearson in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Coralie Bingham in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Andrew T Hattersley in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Gerhart U Ryffel in
Google Scholar
PubMed
Institut für Zellbiologie, Universitätsklinikum Essen, D-45122 Essen, Germany
Search for other papers by Noel G Morgan in
Google Scholar
PubMed
), although examination of the profile of genes that are up-regulated in response to the expression of this mutant in INS-1 cells suggests that it may be less active than the WT ( Thomas et al. 2004 ). The A263insGG (A263ins) mutant has no transactivation
Search for other papers by M Granado in
Google Scholar
PubMed
Search for other papers by A I Martín in
Google Scholar
PubMed
Search for other papers by T Priego in
Google Scholar
PubMed
Search for other papers by M A Villanúa in
Google Scholar
PubMed
Search for other papers by A López-Calderón in
Google Scholar
PubMed
corticosterone, whereas it decreases circulating IGF-I and its gene expression in the liver ( Soto et al. 1998 , Defalque et al. 1999 ). The adult liver is the main source of circulating IGF-I and its main serum-binding protein, IGF-binding protein-3 (IGFBP
Search for other papers by Ping Ye in
Google Scholar
PubMed
Search for other papers by Christopher J Kenyon in
Google Scholar
PubMed
Search for other papers by Scott M MacKenzie in
Google Scholar
PubMed
Search for other papers by Katherine Nichol in
Google Scholar
PubMed
Search for other papers by Jonathan R Seckl in
Google Scholar
PubMed
Search for other papers by Robert Fraser in
Google Scholar
PubMed
Search for other papers by John M C Connell in
Google Scholar
PubMed
Search for other papers by Eleanor Davies in
Google Scholar
PubMed
2003 ). Although these extra-adrenal sites are not capable of corticosteroid production on the same scale as the adrenal cortex, due to a much lower level of relevant gene expression, their proximity to glucocorticoid receptors (GR) and
Search for other papers by AM Holland in
Google Scholar
PubMed
Search for other papers by JK Findlay in
Google Scholar
PubMed
Search for other papers by JA Clements in
Google Scholar
PubMed
The kallikreins (KLKs) are a highly conserved multi-gene family of serine proteases that are expressed in a wide variety of tissues and act on a diverse range of substrates. KLK-like enzyme activity has variously been reported to increase or decrease during the period leading up to ovulation in the equine chorionic gonadotrophin (eCG)primed, human chorionic gonadotrophin (hCG)-stimulated immature rat ovary. These earlier studies, which used biochemical assays to detect enzyme activity, lacked the specificity and sensitivity necessary to characterise conclusively the activity of the individual KLK gene family members. In this study, we have used a gene-specific RT-PCR/Southern hybridisation strategy to delineate the expression patterns of six of the individual KLK genes expressed in the rat ovary (rKLK1-3 and rKLK7-9). We have identified three broad patterns of expression in the eCG/hCG-stimulated ovary in which there is either a post-eCG increase/pre-ovulatory decrease in rKLK expression (rKLK1, rKLK3), a peri-ovulatory decrease in expression (rKLK2, rKLK8) or a relatively unchanged pattern of expression (rKLK7, rKLK9). In addition to clarifying the earlier biochemical studies, these findings support a differential role for the individual KLKs in the ovulatory process.
Search for other papers by CR McCudden in
Google Scholar
PubMed
Search for other papers by MR Kogon in
Google Scholar
PubMed
Search for other papers by GE DiMattia in
Google Scholar
PubMed
Search for other papers by GF Wagner in
Google Scholar
PubMed
It is currently accepted that the fish stanniocalcin (STC) gene is expressed exclusively in the corpuscles of Stannius (CS), unique endocrine glands on the kidneys of bony fishes. In this study, we have re-examined the pattern of fish STC gene expression in the light of the recent evidence for widespread expression of the gene in mammals. Surprisingly, we found by Northern blotting that the fish gene was also expressed in the kidneys and gonads, in addition to the CS glands. Moreover, Southern blotting of RT-PCR products revealed STC mRNA transcripts in all tissues assayed, including brain, heart, gill, muscle and intestine. In situ hybridization studies using digoxigenin-labeled riboprobes localized STC mRNA to chondrocytes, and both mature and developing nephritic tubules. Immunocytochemical staining indicated that the STC protein was widespread in cells of the gill, kidney, brain, eye, pseudobranch and skin. We also characterized the salmon STC gene, establishing that it was comprised of five exons as opposed to four in mammals. A single transcription start site was identified by primer extension 99 bp upstream of the start codon. This is the first evidence of STC gene expression in fish tissues other than the CS glands and suggests that, as in mammals, fish STC operates via both local and endocrine pathways.
Search for other papers by S.R. Davis in
Google Scholar
PubMed
Search for other papers by Z. Krozowski in
Google Scholar
PubMed
Search for other papers by R.I. McLachlan in
Google Scholar
PubMed
Search for other papers by H.G. Burger in
Google Scholar
PubMed
ABSTRACT
We report inhibin α- and βA -subunit gene expression in the human corpus luteum and placenta using human α-subunit and bovine βA -subunit nucleic acid probes. In addition, we have demonstrated the presence of immunoreactive and bioactive inhibin in human corpora lutea. Our findings suggest that this tissue is a significant source of inhibin during the luteal phase of the normal human menstrual cycle.
Search for other papers by KL Houseknecht in
Google Scholar
PubMed
Search for other papers by CP Portocarrero in
Google Scholar
PubMed
Search for other papers by S Ji in
Google Scholar
PubMed
Search for other papers by R Lemenager in
Google Scholar
PubMed
Search for other papers by ME Spurlock in
Google Scholar
PubMed
Leptin, the product of the ob gene, is secreted from white adipocytes and regulates food intake and whole-body energy metabolism. In rodents and humans, leptin gene expression is under complex endocrine and metabolic control, and is strongly influenced by energy balance. Growth hormone (GH) has myriad effects on adipose tissue metabolism. The primary aim of this study was to determine the ability of GH to regulate leptin mRNA expression in bovine adipose tissue in vitro and in vivo. Incubation of subcutaneous adipose tissue explants for 24 h with GH alone had no effect on bovine leptin gene expression, whereas high concentrations of insulin or dexamethasone (DEX) potently stimulated bovine leptin mRNA abundance. GH, in combination with high concentrations of insulin, DEX, or both, attenuated the ability of insulin or DEX to stimulate leptin expression in vitro. These data indicate that GH can indirectly regulate leptin expression in vitro by altering the adipose tissue response to insulin or DEX. We extended these studies to examine the ability of GH to regulate leptin expression in vivo, using young castrate male cattle treated with no hormone (control) or GH (200 micrograms/kg body weight per day) for 3 days. GH increased plasma GH and insulin concentrations, but not those of cortisol or non-esterified fatty acid (NEFA) concentrations. GH treatment increased adipose tissue leptin and IGF-1 mRNA concentrations (n=9, P>0.001). In addition, leptin abundance was highly correlated with adipose tissue IGF-1 mRNA in GH-treated animals (P>0.001). The timing of GH-induced changes in leptin gene expression preceded measurable GH effects on adiposity.
