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The results suggest that both of the possible single mutation-containing heteromeric GH-GHR complexes, as well as the double GHR mutant complex result in perturbation of complex structures, with altered ability of the GHR dimers to interact with the GH peptide.
These results implicate TIMP3 (show TIMP3 Proteins) as a modulator of cell surface GHR abundance and the ability of GH to promote cellular signaling.
GHR and PRLR (show PRLR Proteins) associate in complexes comprised of GHR-GHR/PRLR-PRLR (show PRLR Proteins) heteromers consisting of GHR homodimers and PRLR (show PRLR Proteins) homodimers, rather than GHR-PRLR (show PRLR Proteins) heterodimers.
d3/d3 GHR genotype was found twice as frequent in appropriate for gestational age (AGA (show AGA Proteins)) and large for gestational age (LGA (show GLS2 Proteins)) cohorts compared to small for gestational age (SGA) subjects, whereas no significant differences in the frequency distribution of the GHR genotypes between LGA (show GLS2 Proteins) and AGA (show AGA Proteins) newborns were detected.
Molecular interactions of EphA4 (show EPHA4 Proteins), growth hormone receptor, Jak2 (show JAK2 Proteins), and STAT5B (show STAT5B Proteins) have been described.
GHR levels correlate with levels of lipases and lipid droplet-associated proteins crucial for lipolysis. Thus, higher GHR expression in the abdominal depot when compared with the gluteal depot may underlie the in vivo effect of GH to specifically reduce abdominal adipose tissue mass.
There was a strong relationship between growth hormone receptor (GHR)-d3/fl gene polymorphism status and leptin (show LEP Proteins) levels in acromegalic patients
GHR exon 3 genotype appears to have no clinical significance, at least in Brazilian acromegaly patients.
No differences were observed in GHR genotype distribution between the idiopathic growth hormone (show GH1 Proteins) deficiency (IGHD)patients and the control group. Patients with IGHD did not differ among each other depending on their genotype (fl/fl (show FLT3LG Proteins)-GHR or fl/d3-GHR) in terms of growth velocity before introducing therapy or growth rate after one year of recombinant human GH therapy.
GHR-exon 3 polymorphisms did not show any consistent association with clinical and laboratory features of acromegalic patients even after treatment.
A role for GH in influencing hormone signaling in adipose tissue in a depot-dependent manner in GHR-/- knock-out mice.
disruption of cardiomyocyte GH-induced signaling in adult GhrKO mice does not affect cardiac function, but it does play a role in systemic glucose homeostasis, in part through modulation of circulating IGF-1 (show IGF1 Proteins).
Snell, GHKRO, and PAPPA (show PAPPA Proteins)-KO mice express high levels of two proteins involved in DNA repair, O-6-methylguanine-DNA methyltransferase (MGMT (show MGMT Proteins)) and N-myc downstream-regulated gene 1 (NDRG1 (show NDRG1 Proteins)).
adult-onset growth hormone receptor knockout mice (aGHRKO mice), like GHRKO animals, displayed retarded growth and high adiposity with improved insulin (show INS Proteins) sensitivity. Importantly, female aGHRKO animals showed an increase in their maximal lifespan, whereas the lifespan of male aGHRKO mice was not different from controls.
Similar to other mice with decreased GH action, female GHA mice display reduced age-related lipid redistribution and improved insulin (show INS Proteins) sensitivity, but no change in cellular senescence.
The dwarf phenotype was partially corrected via plasmid containing the growth hormone gene administrated intramuscularly, depending on age at treatment.
GHR-dependent downregulation of NLRP3 (show NLRP3 Proteins) inflammasome in macrophages is linked to pro-longevity effects that maintain immune system homeostasis in aging.
both brown adipose tissue (BAT (show BAAT Proteins)) and white adipose tissue (WAT) contribute in different ways to phenotypes in GHRKO mice, with Ghr ablation blunting inflammation in BAT (show BAAT Proteins) as well as cellular metabolism and mitochondrial biogenesis in WAT
Data (including data from studies in knockout mice) suggest Socs2 (suppressor of cytokine signaling 2 (show SOCS2 Proteins)) regulates liver regeneration rate after partial hepatectomy, Ghr level via ubiquitination/proteolysis, and serum Igf1 (insulin-like growth factor-1 (show IGF1 Proteins)).
It was concluded that endogenously secreted PTH (show PTH Proteins) and GHR signaling in bone are necessary to establish radial bone growth and optimize mineral acquisition during growth.
There was no association between the genotypes of GH and IGF-IS and fertility of Holstein cows raised in semiextensive or intensive regimes, while the STAT5 (show STAT5A Proteins) ABstEII polymorphism was associated with calving-first heat interval in Holstein cows raised in the intensive system.
hepatic growth hormone receptor and suppressor of cytokine signaling (SOCS (show CISH Proteins))2 (show SOCS2 Proteins) messenger RNA expression appeared to be promptly and sensitively regulated by increased estradiol levels before ovulation of dairy heifers
Comparatively studied genetic diversity of growth hormone receptor (GHR) in Tibetan cattle and Chinese Holstein cow.
This work confirms the importance of CAPN1 (show CAPNL1 Proteins) and CAST for tenderness in beef, provides a new effect of CAST on beef tenderness, and questions the utility of GHR as a selection marker for beef quality.
the data support the high potential of the growth hormone receptor F279Y polymorphism as a marker for the improvement of milk traits in selection programs
6 of the published GHR SNPs and 7 of the novel GHR SNPs were associated with at least 1 of the traits--milk yield, fat yield, protein yield, fat percentage, protein percentage, somatic cell score, calving interval, survival and growth and size traits.
Effects of GHR p.Phe279Tyr mutations on milk, fat and protein yield, as well as fat and protein percentage in the milk of 1222 Holstein cows was found to be significantly associated with protein percentage.
Food deprivation-induced decrease in circulating IGF-I (show IGF1 Proteins) in steers is associated with decrease in expression of different IGF-I (show IGF1 Proteins) mRNA variants and specific decrease in expression of growth hormone receptor mRNA variants 1C3 and 1A in liver.
Insulin (show INS Proteins) regulates the efficiency of GH signaling in liver and adipose tissue of dairy cows by acting as a rheostat of GHR synthesis.
Results show that chicken ovalbumin upstream promoter transcription factor (show NR2F1 Proteins) II (COUP-TFII (show NR2F2 Proteins)), hepatocyte nuclear factor 4alpha (HNF-4alpha (show HNF4A Proteins)) and HNF-4gamma regulate growth hormone receptor 1A promoter activity by binding to a common DNA element
Castration significantly reduced the serum growth hormone (show GH1 Proteins) and the responses of the growth hormone receptor (GHR)
GHR double-allelic knockout pigs were 50% smaller than that of the controls.
Growth hormone (GH (show GH1 Proteins)) in maturation medium did not increase cumulus expansion in porcine cumulus-oocyte complexes but did improve nuclear maturation, GH had no effect on porcine fertilization and embryo development.
subunit alignment is critical for effective signaling in GH receptor activation
Fos-zippered GHR tails and Jak2 (show JAK2 Proteins), both purified from baculovirus-infected insect cells, interacted via box1 with a binding affinity of approximately 40nM.
Jak2 (show JAK2 Proteins) binding to the growth hormone receptor prevents endocytosis in a non-catalytic manner
GHR gene may be a candidate gene responsible for butcher trait in rabbit.
This gene encodes a member of the type I cytokine receptor family, which is a transmembrane receptor for growth hormone. Binding of growth hormone to the receptor leads to receptor dimerization and the activation of an intra- and intercellular signal transduction pathway leading to growth. Mutations in this gene have been associated with Laron syndrome, also known as the growth hormone insensitivity syndrome (GHIS), a disorder characterized by short stature. In humans and rabbits, but not rodents, growth hormone binding protein (GHBP) is generated by proteolytic cleavage of the extracellular ligand-binding domain from the mature growth hormone receptor protein. Multiple alternatively spliced transcript variants have been found for this gene.
, growth hormone binding protein
, serum binding protein
, somatotropin receptor
, Growth hormone receptor precursor (GH receptor) (GH binding protein) (GHBP) (Serum binding protein)
, growth hormone receptor/binding protein
, growth hormone receptor precursor splice variant D56
, growth hormone receptor variant d5-6
, growth hormone receptor
, growth hormone-binding protein
, serum-binding protein
, Somatotropin receptor