Disease relevance of GH1

• GH is considered to play a role in the pathogenesis of diabetic retinopathy, causing neovascularization in the retina [1].
• Growth hormone interacts with the Marek's disease virus SORF2 protein and is associated with disease resistance in chicken [2].
• We examined an endogenous gene the growth hormone (GH) gene, and a stably transfected plasmid containing the chicken lysozyme silencer (F2) T3 response element (TRE) gene, F2-TRE-TK-CAT, both in pituitary tumor (GC) cells [3].
• GH was influenced to a greater extent by the rate of body weight gain than by increasing age in the genetically normal fast and slow growing strains [4].
• Based on these data, we suggest that the lack, or greatly reduced number, of GH receptors may be a major contributing factor to the dwarfism observed in these strains [5].

Psychiatry related information on GH1

• 1. In several experiments, hormonal changes in the somatotrophic axis, growth hormone (GH) sensitivity to a GH-secretagogue, thyroid hormones and their metabolising enzymes and plasma glucose levels were measured in relation to food deprivation and reinitiation after a single daily meal in 4- to 5-week-old male broiler chickens [6].
• When growth hormone (GH, 100 ng/50 microliters) was administered during the same critical period (day 3) no difference was observed in TH activity as compared to controls [7].
• 5. Water deprivation for periods of 6, 12, 18 or 24 h increases plasma prolactin markedly but did not affect GH secretion significantly [8].
• Therefore, in the present study, we compared the effect of intracerebroventricular (ICV) injection of C-RFa and mammalian PrRP (mPrRP) on feeding behavior and plasma PRL, growth hormone (GH), and corticosterone (CORT) concentrations [9].

High impact information on GH1

• Growth hormone, insulin and testosterone, which have been reported to be mitogenic for rat and chick embryo myoblasts, did not have significant effects on DNA synthesis in bovine myoblasts when compared to the FGF [10].
• Furthermore, polymorphism in the GH gene (GH1) is associated with the number of tissues with tumors in commercial White Leghorn chickens with the MHC B*2/B*15 genotype [2].
• There was no specific protection of the tripartite GH TRE at -180 bp against either DMS or DNase I in the absence or presence of T3 in either cell line [3].
• Whereas all treatments affected levels of GH mRNA, only CORT, GHRH, and SRIF significantly altered GHRH-R mRNA levels [11].
• We conclude that adrenal glucocorticoids may substantially impact pituitary GH responses to GHRH in the chicken through modulation of GHRH-R gene expression [11].

Chemical compound and disease context of GH1

• In contrast, hypothyroidism stimulates GH secretion in birds, in which thyroid hormone directly inhibits pituitary GH release [12].
• When chicken GH (500 micrograms/kg body weight) was injected i.v. into laying hens, tissue catecholamine (adrenaline, noradrenaline and dopamine) concentrations in the preoptic area (POA) and medial basal hypothalamus (MBH) were depleted for 2-24 h, as were concentrations of dihydroxyphenylacetic acid, a dopamine metabolite [13].
• Growth hormone decreased and T4 increased with age in all populations except the line selected for low body weight, whereas the pattern for T3 varied with genetic stock [14].
• In the present study the effects of TAM administration (1 mg/kg body weight on alternate days from 12 d of age) on testicular function, hypothalamic chicken gonadotropin-releasing hormone (cGn-RH-I), plasma luteinising hormone (LH), growth hormone (GH), prolactin (PRL) and testosterone were studied in juvenile White Leghorn cockerels [15].
• 1. Weekly variations in body weight, relative body-weight gain and plasma growth hormone (GH) concentrations were determined in control and cortisone-treated (5 mg cortisone acetate/bird d) chickens between 3 and 10 weeks of age [16].

Biological context of GH1

• The cGH gene consists of five exons and four introns as has been observed in the mammalian GH genes [17].
• The promoter region of the cGH gene has no overall homology with the corresponding regions of mammalian genes, but contains a short (24 bp) sequence which is highly homologous to the antisense strand sequence of the proximal binding site for a pituitary-specific transcription factor, GHF-1/Pit-1, in the promoter region of the rat GH gene [17].
• 3. Base sequence analysis of chicken GH-cDNA revealed only 70% similarity compared with duck GH-cDNA, and 97% similarity with a previously published chicken GH-cDNA sequence [18].
• 5. Comparisons of amino acid sequences of chicken and duck GH exhibit only three substitutions, while the amino acid sequences of GHs of chicken are identical [18].
• Ontogeny of growth hormone (GH)-secreting cells during chicken embryonic development: initial somatotrophs are responsive to GH-releasing hormone [19].

Anatomical context of GH1

• The concentrations of GH and IGF-I in serum and seminal plasma were measured with RIA and ELISA, respectively [20].
• GH immunoreactivity in the neural retina of embryos was primarily associated with proteins of 15 and 16 kDa, whereas only trace amounts of monomer (22-25 kDa) GH, the most abundant form in the pituitary gland, were present [21].
• In this study, GH cDNAs identical in size and sequence to the full-length pituitary transcript were generated by RT-PCR from mRNA extracted from the neural retinas of embryonic day (ED) 7 chick embryo eyes [21].
• The GH immunoreactivity in the neural retina of ED8 embryos was widespread, although GH staining was particularly abundant in retinal ganglion cells (RGCs) [21].
• We have investigated the role of GH in the serum requirement for the multiplication of chick embryo fibroblasts (CEF-S) in culture . Serum from hypophysectomized (hypox.) rats is much less effective than normal serum in stimulating the incorporation of (3H-methyl]thymidine into DNA [22].

Associations of GH1 with chemical compounds

• When used separately, both antagonists attenuated induction of GH mRNA by corticosterone [23].
• Although two preparations of pituitary bGH stimulated a significant (P less than 0.01) increase in glycerol production, neither rebGH nor recombinant-DNA-derived chicken GH was lipolytic [24].
• In the protein repletion time course study, T4 and T3 concentrations were normalized prior to or concurrent with plasma GH normalization [25].
• One-day-old male chicks were assigned to experimental groups and were treated either with thyroxine (T4) feed supplements or daily mammalian growth hormone (GH) injections or a combination of these treatments (T4/GH) [26].
• In the first hour of incubation, GH inhibited glucagon, 8-bromo-3',5'-cyclic adenosine monophosphate (8-bromo-cAMP), and 1-isobutyl-3-methyl-xanthine (IBMX) induced glycerol release [27].

Regulatory relationships of GH1

• Growth hormone secretion induced by thyrotropin-releasing hormone in adult chickens: evidence of dose-dependent induction of either refractoriness or sensitization [28].

Other interactions of GH1

• Therefore, a semiquantitative RT-PCR method was used to detect possible changes in GH and TSHbeta mRNA levels [29].
• Sex-linked dwarf chickens caused by the mutation of the growth hormone receptor gene are characterized by normal growth hormone (GH), very low insulin-like growth factor I (IGF-I) level in the blood, and reduced growth [20].
• Similarly, the expression profiles of 69 and 61 genes indicate a potential involvement in the induction of GH and PRL mRNA, respectively [30].
• Western blotting determined the molecular size of immunoreactive GH in RPE cells to be 80-84 kDa, similar to the computed molecular mass of s-cGH/GH receptor complex [1].
• The globular domain of chicken histone H1 (GH1) has been studied by 1H homonuclear and 1H-15N heteronuclear 2D NMR spectroscopy [31].

Analytical, diagnostic and therapeutic context of GH1

• Full-length GH mRNA was similarly located, by in situ hybridization, throughout the neural retina and concentrated in cells in the RGC layer [21].
• In the 17-d-old embryo, immunocytochemistry detected immunoreactive GH in retinal pigment epithelial (RPE) cells [1].
• Immunohistochemical staining and indirect immunofluorescence assay indicated that GH and SORF2 can be coexpressed in MDV-infected cells both in vitro and in vivo [2].
• The resulting cells were then subjected to the GH plaque assay under basal and GHRH-stimulated conditions [19].
• Northern blot analysis indicated that CORT increased GH mRNA levels after 1 d of treatment [32].

References