scholarly journals The Effect of ZJXG Decoction on The Serum Level of Growth Hormone and The Expression of GH Receptor in Callus

2019 ◽  
Vol 12 ◽  
pp. 2320-2330
Author(s):  
Zhen Zhou ◽  
Guanxi Wang ◽  
Zhaogang Liu ◽  
Yunliang Guo
Keyword(s):  
Growth Hormone ◽  
Serum Level ◽  
Growth Hormone Receptor ◽  
Femur Fracture ◽  
Healing Process ◽  
Enzyme Linked Immunosorbent Assay ◽  
Middle Point ◽  
X Ray ◽  
Gh Receptor ◽  
Hematoxylin Eosin

The aim of experiment was to investigate the effects of Zhuangjin XuGu decoction (ZJXG decoction) on growth hormone (GH) serum and GH receptor (GHR) expression in callus. The femur fracture animal models were generated in 72 Wistar rats by cutting femur transversely at the middle point. The rats models were administered orally ZJXG decoction for 28 days. Anatomy, X-ray and hematoxylin- eosin (HE) staining were used to observe the healing process in rats. The expression of growth hormone receptor (GHR) in fibroblasts and osteoblasts in callus was evaluated by immunohistochemical assay (IHC). The serum level of GH was passed by enzyme linked immunosorbent assay (ELISA). Anatomy, X-ray and H-E staining indicated that the fibrous callus at the fracture-end increased and the fibrous granular tissue changed gradually to fibrous, cartilaginous and osseous callus. IHC and ELISA showed that after 28 days of ZJXG Decoction treatment, that GH in the fibroblasts and osteoblasts of callus and their serum level increased significantly. These results suggested that ZJXG decoction could enhance the fracture healing by enhancing GH activity and promoting the expression of GHR in the fibroblasts and osteoblasts of callus in rats.

The interrelationship between and the regulation of hepatic growth hormone receptors and circulating GH binding protein in the pig

1992 ◽  
Vol 126 (2) ◽  
pp. 155-161 ◽  
Author(s):  
Geoffrey R Ambler ◽  
Bernhard H Breier ◽  
Andrzej Surus ◽  
Hugh T Blair ◽  
Stuart N McCutcheon ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Hormone Receptor ◽  
Hormone Receptors ◽  
Binding Capacity ◽  
Binding Protein ◽  
Somatic Growth ◽  
Gh Receptor ◽  
Age Related ◽  
Igf I ◽  
Serum Gh

We evaluated the interrelationship between, and regulation of, the hepatic growth hormone receptor and serum GH binding protein (GH BP) in pigs treated with recombinant porcine growth hormone (rpGH). Infant and pubertal male pigs (N = 5 per group) received either rpGH 0.15 mg/kg daily or diluent intramuscularly for 12 days. Somatic growth, serum IGF-I and GH BP and [125I]bovine GH (bGH) binding to MgCl2-treated hepatic membrane homogenates were examined. Marked age-related increases were seen in serum GH BP (p<0.001) and [125I]bGH binding to hepatic membranes (p<0.001). GH BP was increased in rpGH treated animals (p = 0.03), from 13.8±1.2 (mean±1 x sem) (controls) to 17.8±2.0% in infants, and from 35.2±2.6 (controls) to 41.8±3.4% in pubertal animals. [125I]bGH binding to hepatic membranes was also increased by rpGH treatment (p<0.05), from 7.0±1.6 (controls) to 15.4±3.6% in infants and from 53.7±7.1 (controls) to 65.1±11.8% in pubertal animals. No significant interaction between age and treatment was seen. Overall, serum GH BP correlated significantly with [125I]bGH membrane capacity (r=0.82, p<0.001), with a correlation of r= 0.83 in the infant animals but no significant correlation in the pubertal animals considered alone (r=0.13). Serum IGF-I correlated significantly with serum GH BP (r=0.93, p<0.001) and [125]bGH membrane binding capacity (r = 0.91, p< 0.001). These observations suggest that serum GH BP levels reflect major changes of hepatic GH receptor status. In addition, the present study demonstrates that the hepatic GH receptor can be induced by GH in the infant pig, despite a developmentally low GH receptor population at this age, suggesting potential efficacy of GH at earlier ages than generally considered.

scholarly journals Order and disorder—An integrative structure of the full-length human growth hormone receptor

2021 ◽  
Vol 7 (27) ◽  
pp. eabh3805
Author(s):  
Noah Kassem ◽  
Raul Araya-Secchi ◽  
Katrine Bugge ◽  
Abigail Barclay ◽  
Helena Steinocher ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Lipid Membrane ◽  
Human Growth ◽  
Full Length ◽  
Saxs Data ◽  
X Ray ◽  
Human Growth Hormone Receptor

Because of its small size (70 kilodalton) and large content of structural disorder (>50%), the human growth hormone receptor (hGHR) falls between the cracks of conventional high-resolution structural biology methods. Here, we study the structure of the full-length hGHR in nanodiscs with small-angle x-ray scattering (SAXS) as the foundation. We develop an approach that combines SAXS, x-ray diffraction, and NMR spectroscopy data obtained on individual domains and integrate these through molecular dynamics simulations to interpret SAXS data on the full-length hGHR in nanodiscs. The hGHR domains reorient freely, resulting in a broad structural ensemble, emphasizing the need to take an ensemble view on signaling of relevance to disease states. The structure provides the first experimental model of any full-length cytokine receptor in a lipid membrane and exemplifies how integrating experimental data from several techniques computationally may access structures of membrane proteins with long, disordered regions, a widespread phenomenon in biology.

Mechanism of signaling by growth hormone receptor

1996 ◽  
Vol 76 (4) ◽  
pp. 1089-1107 ◽  
Author(s):  
L. S. Argetsinger ◽  
C. Carter-Su
Keyword(s):  
Growth Hormone ◽  
Protein Kinase ◽  
Growth Hormone Receptor ◽  
Second Messengers ◽  
Current Model ◽  
Mitogen Activated Protein Kinase ◽  
Gh Receptor ◽  
Insulin Receptor Substrates ◽  
Mitogen Activated Protein ◽  
Control Body

Growth hormone (GH) has long been known to stimulate linear growth and regulate metabolism. The cellular mechanism by which GH elicits these effects has only recently begun to be understood. This review provides an overview of a current model of GH signaling. Briefly, binding of GH to GH receptor induces receptor dimerization and activation of the tyrosine kinase JAK2. Tyrosyl phosphorylation of GH receptor and JAK2 recruits and activates signaling molecules such as Stat transcription factors, SHC, and insulin receptor substrates 1 and 2 that lead to the release of second messengers such as diacylglycerol, calcium, and nitric oxide and the activation of enzymes such as mitogen-activated protein kinase, protein kinase C, phospholipase A2, and phosphatidylinositol 3'-kinase. These pathways regulate cellular function including gene transcription, metabolite transport, and enzymatic activity that result in the ability of GH to control body growth and metabolism.

scholarly journals Dose-response effects of a new growth hormone receptor antagonist (B2036-PEG) on circulating, hepatic and renal expression of the growth hormone/insulin-like growth factor system in adult mice

2000 ◽  
Vol 167 (2) ◽  
pp. 295-303 ◽  
Author(s):  
JW van Neck ◽  
NF Dits ◽  
V Cingel ◽  
IA Hoppenbrouwers ◽  
SL Drop ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Factor ◽  
Receptor Antagonist ◽  
Growth Hormone Receptor ◽  
Binding Protein ◽  
Mrna Levels ◽  
Insulin Like Growth Factor ◽  
Gh Receptor ◽  
Igf I ◽  
Igfbp 3

The effects of growth hormone (GH) in regulating the expression of the hepatic and renal GH and insulin-like growth factor (IGF) system were studied by administering a novel GH receptor antagonist (GHRA) (B2036-PEG) at different doses (0, 1.25, 2.5, 5 and 10 mg/kg/day) to mice for 7 days. No differences were observed in the groups with respect to body weight, food consumption or blood glucose. However, a dose-dependent decrease was observed in circulating IGF-I levels and in hepatic and renal IGF-I levels at the highest doses. In contrast, in the 5 and 10 mg/kg/day GHRA groups, circulating and hepatic transcriptional IGF binding protein-3 (IGFBP-3) levels were not modified, likely resulting in a significantly decreased IGF-I/IGFBP-3 ratio. Hepatic GH receptor (GHR) and GH binding protein (GHBP) mRNA levels increased significantly in all GHRA dosage groups. Endogenous circulatory GH levels increased significantly in the 2.5 and 5 mg/kg/day GHRA groups. Remarkably, increased circulating IGFBP-4 and hepatic IGFBP-4 mRNA levels were observed in all GHRA administration groups. Renal GHR and GHBP mRNA levels were not modified by GHRA administration at the highest doses. Also, renal IGFBP-3 mRNA levels remained unchanged in most GHRA administration groups, whereas IGFBP-1, -4 and -5 mRNA levels were significantly increased in the 5 and 10 mg/kg/day GHRA administration groups. In conclusion, the effects of a specific GHR blockade on circulating, hepatic and renal GH/IGF axis reported here, may prove useful in the future clinical use of GHRAs.

Growth Hormone Receptor Antagonist Therapy in Acromegalic Patients Resistant to Somatostatin Analogs*

2000 ◽  
Vol 85 (8) ◽  
pp. 2958-2961 ◽  
Author(s):  
Vivien S. Herman-Bonert ◽  
Kenneth Zib ◽  
John A. Scarlett ◽  
Shlomo Melmed
Keyword(s):  
Growth Hormone ◽  
Receptor Antagonist ◽  
Growth Hormone Receptor ◽  
Hormone Secretion ◽  
Somatostatin Analogs ◽  
Growth Hormone Secretion ◽  
Primary Therapy ◽  
Gh Receptor ◽  
Gh Receptor Antagonist ◽  
Octreotide Therapy

Transsphenoidal surgical resection is the primary therapy for acromegaly caused by GH secreting pituitary adenomas. Medical therapy for patients not controlled by surgery includes primarily somatostatin analogs and secondarily dopamine agonists, both of which inhibit pituitary growth hormone secretion. A novel GH receptor antagonist (pegvisomant) binds to hepatic GH receptors and inhibits peripheral insulin-like growth factor-1 generation. Six patients resistant to maximal doses of octreotide therapy received pegvisomant—three received placebo or pegvisomant 30 mg or 80 mg weekly for 6 weeks and three received placebo and pegvisomant 10–20 mg/d for 12 weeks. Thereafter, all patients received daily pegvisomant injections of doses determined by titrating IGF-1 levels. Serum total IGF-1 levels were normalized in all six acromegalic patients previously shown to be resistant to somatostatin analogs via a novel mechanism of peripheral GH receptor antagonism. The GH receptor antagonist is a useful treatment for patients harboring GH-secreting tumors who are resistant to octreotide.

GROWTH HORMONE RECEPTOR GENE: NOVEL EXPRESSION IN PITUITARY TISSUE

1991 ◽  
Vol 128 (3) ◽  
pp. R9-R11 ◽  
Author(s):  
R.A. Fraser ◽  
K. Siminoski ◽  
S. Harvey
Keyword(s):  
Growth Hormone ◽  
Plasma Membranes ◽  
Growth Hormone Receptor ◽  
Radioligand Binding ◽  
Receptor Gene ◽  
Northern Analysis ◽  
Binding Studies ◽  
Human Pituitary ◽  
Gh Receptor ◽  
Pituitary Tissue

ABSTRACT Specific hybridization of polyadenylated RNA, extracted from rat, rabbit and human pituitary glands with a 638 bp rabbit GH receptor (rGHR) cRNA was demonstrated by Northern analysis. In-situ hybridization of tissue sections with the probe demonstrated the localization of rGHR mRNA throughout the rat pituitary gland and its presence in the anterior lobe of the rabbit pituitary. Growth hormone binding sites on pituitary membranes were not, however, demonstrated by radioligand binding studies. Thus, although the GH receptor gene is expressed in pituitary tissue, functional GH receptors may not be inserted into pituitary plasma membranes.

Expression of GH receptor mRNA in regenerating skeletal muscle of normal and hypophysectomized rats. An in situ hybridization study

1991 ◽  
Vol 125 (6) ◽  
pp. 595-602 ◽  
Author(s):  
Eva Jennische ◽  
Göran L. Andersson
Keyword(s):  
Skeletal Muscle ◽  
Growth Hormone ◽  
In Situ Hybridization ◽  
Growth Hormone Receptor ◽  
Receptor Expression ◽  
Muscle Fibres ◽  
Receptor Mrna ◽  
Gh Receptor ◽  
Hypophysectomized Rats

Abstract. Expression of growth hormone receptor mRNA was investigated by in situ hybridization in skeletal muscle from normal and hypophysectomized rats during the first seven days of regeneration after ischemic injury. A digoxigenin-labelled RNA probe directed against the extracellular part of the rat GH receptor was used. In both normal and hypophysectomized rats distinct expression of GH receptor mRNA could be demonstrated in the regenerating muscle cells at the myoblast/myotube stage. The GH receptor expression appeared to decline with increasing maturation of the regenerated muscle fibres. In hypophysectomized rats, the regeneration process and the expression of GH receptor mRNA was delayed compared with that in normal animals. It is concluded that growth hormone may affect also the early phase of muscle regeneration in normal animals. To what extent lack of growth hormone contributes to the delayed regeneration observed in the hypophysectomized rats remains to be elucidated.

scholarly journals Association of the Growth Hormone Receptor d3-Variant and Catch-up Growth of Preterm Infants with Birth Weight of Less Than 1500 Grams

2007 ◽  
Vol 92 (11) ◽  
pp. 4489-4493 ◽  
Author(s):  
Felix Schreiner ◽  
Sonja Stutte ◽  
Peter Bartmann ◽  
Bettina Gohlke ◽  
Joachim Woelfle
Keyword(s):  
Growth Hormone ◽  
Birth Weight ◽  
Low Birth Weight ◽  
Preterm Infants ◽  
Growth Pattern ◽  
Growth Hormone Receptor ◽  
Very Low Birth Weight ◽  
Postnatal Growth ◽  
Gh Receptor ◽  
Catch Up

Abstract Background: Preterm infants with very low birth weight frequently exhibit impaired longitudinal growth during the first years of life. Recently, the d3-isoform (genomic deletion of exon 3) of the GH receptor (GHR) has been linked to an increased responsiveness to GH. Objective: Our objective was to test whether the GHRd3 isoform is associated with postnatal catch-up growth in very low birth weight preterm infants. Design and Patients: We compared the postnatal growth pattern of 77 otherwise healthy preterm infants (mean gestational age, 28.5 wk; range, 23–35 wk) with a birth weight below 1500 g (mean birth weight, 941 g) to their GHR exon 3 genotype, which was analyzed by multiplex PCR. On examination, mean age of the children was 6.0 yr (range, 4.2–8.0 yr). Results: Children homozygous or heterozygous for the GHRd3 allele showed a significantly higher rate of postnatal catch-up, compared with those homozygous for the full-length allele. Conclusions: Our results define the GHR exon 3 genotype as a predictor for the postnatal growth pattern of very low birth weight preterm infants. Those who carry at least one GHRd3 allele are more likely to catch-up.

scholarly journals Order and disorder – an integrative structure of the full-length human growth hormone receptor

2020 ◽  
Author(s):  
Noah Kassem ◽  
Raul Araya-Secchi ◽  
Katrine Bugge ◽  
Abigail Barclay ◽  
Helena Steinocher ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Hormone Receptor ◽  
Growth Hormone Receptor ◽  
Lipid Membrane ◽  
Structural Information ◽  
Human Growth ◽  
Full Length ◽  
X Ray ◽  
Human Growth Hormone Receptor

ABSTRACTDespite the many physiological and pathophysiological functions of the human growth hormone receptor (hGHR), a detailed understanding of its modus operandi is hindered by the lack of structural information of the entire receptor at the molecular level. Due to its relatively small size (70 kDa) and large content of structural disorder (>50%), this membrane protein falls between the cracks of conventional high-resolution structural biology methods. Here, we study the structure of the full-length hGHR in nanodiscs with small angle-X-ray scattering (SAXS) as the foundation. We developed an approach in which we combined SAXS, X-ray diffraction and NMR spectroscopy obtained on the individual domains and integrated the data through molecular dynamics simulations to interpret SAXS data on the full-length hGHR in nanodiscs. The structure of the hGHR was determined in its monomeric state and provides the first experimental model of any full-length cytokine receptor in a lipid membrane. Combined, our results highlight that the three domains of the hGHR are free to reorient relative to each other, resulting in a broad structural ensemble. Our work exemplifies how integrating experimental data from several techniques computationally, may enable the characterization of otherwise inaccessible structures of membrane proteins with long disordered regions, a widespread phenomenon in biology. To understand orchestration of cellular signaling by disordered chains, the hGHR is archetypal and its structure emphasizes that we need to take a much broader, ensemble view on signaling.

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