Cellular localization of growth hormone receptors/binding proteins in immune tissues

Hull, Kerry; Thiagarajah, Angeline Sharmila; Harvey, S.

doi:10.1007/s004410050676

Cited by 40 publications

(19 citation statements)

References 54 publications

(69 reference statements)

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“…This group [58] subsequently reported that cells expressing GHR also expressed receptors for PRL. Similarly, GHR mRNA was found to be widely distributed in the lymphoid tissues of fowl [59]. Chen, et al, [60] examined cells from bovine fetal spleen and thymus tissue and found GHR expression in early to mid-gestational age with expression diminishing in later gestation.…”

Section: Distribution Of Gh and Prl Receptorsmentioning

confidence: 98%

Neuroendocrine hormones such as growth hormone and prolactin are integral members of the immunological cytokine network

Redelman¹,

Taub

et al. 2008

Cellular Immunology

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Neuroendocrine hormones such as growth hormone (GH) and prolactin (PRL) have been demonstrated to accelerate the recovery of the immune response after chemotherapy and bone marrow transplantation and to enhance the restoration of immunity in individuals infected with HIV and in normal individuals with compromised immune systems associated with aging. As the mechanism of action of these hormones has been elucidated, it has become clear that they are integral members of the immunological cytokine/chemokine network and share regulatory mechanisms with a wide variety of cytokines and chemokines. The members of this cytokine network induce and can be regulated by members of the suppressor of cytokine signaling (SOCS) family of intracellular proteins. In order to take advantage of the potential beneficial effects of hormones such as GH or PRL, it is essential to take into consideration the overall cytokine network and the regulatory effects of SOCS proteins.

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Section: Distribution Of Gh and Prl Receptorsmentioning

confidence: 98%

Neuroendocrine hormones such as growth hormone and prolactin are integral members of the immunological cytokine network

Redelman¹,

Taub

et al. 2008

Cellular Immunology

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“…GH receptor (GHR) immunoreactivity was detected using a polyclonal antibody (at a concentration of 1:400) raised in rabbits against recombinant chicken GH binding protein (rcGHBP) (Huang et al 1993, Hull et al 1996, using the ABC technique, as detailed above. The specificity of staining was demonstrated by replacement of the primary antibody with non-immune rabbit serum (NRS) or PBS.…”

Section: Immunocytochemistrymentioning

confidence: 99%

Growth hormone in neural tissues of the chick embryo

Harvey

Johnson²,

Sanders³

2001

Journal of Endocrinology

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Growth hormone (GH) gene expression predominantly occurs in the pituitary gland, although it also occurs in many extrapituitary sites, including the brain. The cellular location and ontogeny of neural GH production is, however, largely unknown. This has therefore been determined during chick embryogenesis.In chicks, the brain develops from the neural tube at embryonic day (ED) 3. At this age, the divisions of the brain (the telencephalon, diencephalon, mesencephalon, metencephalon and myelencephalon) have intense GH immunoreactivity (GH-IR) (detected by two polyclonal antibodies and a monoclonal antibody for chicken GH). The otic and optic vesicles were also strongly GH immunoreactive, as were the Vth (semi-lunar), VIIth (facial), VIIIth (acoustic) and IXth (glossopharyngeal) nerve ganglia. This GH-IR was specific for GH and was lost when the antibodies were preabsorbed with recombinant chicken GH. The widespread distribution of GH-IR in the neural tissues of ED 3 embryos was mirrored by the distribution of GH receptor (GHR) immunoreactivity, detected by an antibody raised against the chicken GHR.In ED 6/ED 7 embryos, the neural retina of the eye and the epithelial and lens fiber cells were intensely stained for GH-IR, as was Rathke's pouch and the wall of the diencephalon. In contrast, only a few scattered cells were immunoreactive in the surrounding mesoderm. At ED 14, the GH-IR in the brain was restricted to specific tissues and cells. For instance, immunoreactive cells were present in the molecular and pyramidal layers of the cerebral cortex, in the gray matter of the cerebellum, in the choroid plexus, and in the walls of the ventricles.In summary, GH-and GHR-like proteins are abundant in neural tissues of the chick during the first third of incubation, becoming discretely localized to specific tissues and cells during later incubation. The localization of GH and GHR in these tissues, prior to the ontogeny of plasma GH, suggests autocrine or paracrine roles for GH during early embryogenesis.

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“…The possibility that SLD serum and liver may be deficient in immunoreactive GHBP/GHR or contain GHBPs or GHRs of anomalous size was evaluated by Western blot analysis, as previously described (Hull et al 1996a). GHR/ GHBP-like proteins in hepatic homogenates and serum aliquots were detected by a rabbit polyclonal antiserum ( cGHBP at a final dilution of 1:2000) (Hull et al 1996a).…”

Section: Western Blot Analysismentioning

confidence: 99%

“…GHR/ GHBP-like proteins in hepatic homogenates and serum aliquots were detected by a rabbit polyclonal antiserum ( cGHBP at a final dilution of 1:2000) (Hull et al 1996a). For comparative purposes, another polyclonal antibody ( CH17) raised in mice against a putative membranebound chicken GHBP (Dr W Baumbach, American Cyanmid, Princeton, NJ, USA) was also used.…”

Section: Western Blot Analysismentioning

confidence: 99%

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A missense mutation in the GHR gene of Cornell sex-linked dwarf chickens does not abolish serum GH binding

Hull¹,

Marsh²,

Harvey³

1999

Journal of Endocrinology

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Sex-linked dwarfism (SLD) in chickens is characterized by impaired growth despite normal or supranormal plasma growth hormone (GH) levels. This resistance to GH action is thought to be due to mutations of the GH receptor (GHR) gene that reduce or prevent GH binding to target sites. The genetic lesion causing GH resistance in Cornell SLD chickens is, however, not known. Previous studies have shown that hepatic GH-binding activity is abnormally low in these birds, yet the GHR gene is transcribed into a transcript of appropriate size and abundance. Point mutations or defects in translation could therefore account for the impaired GHR activity in this strain. These possibilities were addressed in the present study.A missense mutation resulting in the substitution of serine for the conserved phenylalanine was identified in the region of the GHR cDNA encoding the extracellular domain. Translation of this mutant transcript was indicated by the presence of GHR/GH-binding protein (GHBP)-immunoreactive proteins in liver (55, 70 and 100 kDa) and serum (70 kDa) of normal (K) and SLD birds. Radiolabelled GH did not, however, bind to the hepatic membranes of most SLD chickens. Serum GH-binding activity, in contrast, was readily detectable, although at significantly lower levels than in normal birds. The missense mutation in the SLD GHR gene may thus affect targeting of GHRs to hepatic plasma membranes.

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Cellular localization of growth hormone receptors/binding proteins in immune tissues

Cited by 40 publications

References 54 publications

Neuroendocrine hormones such as growth hormone and prolactin are integral members of the immunological cytokine network

Neuroendocrine hormones such as growth hormone and prolactin are integral members of the immunological cytokine network

Growth hormone in neural tissues of the chick embryo

A missense mutation in the GHR gene of Cornell sex-linked dwarf chickens does not abolish serum GH binding

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