Growth hormone as an early embryonic growth and differentiation factor

Sanders, Esmond J.; Harvey, S.

doi:10.1007/s00429-004-0422-1

Cited by 66 publications

(55 citation statements)

References 134 publications

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“…Whereas roles for lung GH in lung development are currently unknown, it may participate in its vascularization, as GH stimulates angiogenesis in other tissues (Struman et al, 1999;Corbacho et al, 2002). It may also participate in cellular differentiation (Sanders and Harvey, 2004) or regulate immune function within the lung (Batchelor et al, 1998;Waters et al, 1999;Allen et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Local actions of GH within immune (van Garderen et al, 1997), mammary (Zhang et al, 1997), and orthodontic tissues (Mertani et al, 2001), and GH-expressing cell lines (e.g., Kaulsay et al, 1999) are now well established, and a similar local mechanism may be operative in the lung during development. Such actions, however, may be indirect and mediated by an array of growth factor mediators (Sanders and Harvey, 2004), including insulin-like growth factors (IGFs).…”

Section: Discussionmentioning

confidence: 99%

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Growth hormone expression in the perinatal and postnatal rat lung

Beyea

Olson

Harvey

2005

Developmental Dynamics

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It is now established that the lung is a target site for pituitary growth hormone (GH) action, because pathophysiological states of pituitary GH excess and deficiency are associated with impaired pulmonary function. The onset of lung development and differentiation is, however, before the ontogenic differentiation of pituitary somatotrophs. GH may be involved, nevertheless, in lung development, because it is present in extrapituitary tissues of preimplantation mouse embryos and in the lung buds of embryonic chickens. The possibility that GH may be expressed in the rat lung during fetal and neonatal development, therefore, has been assessed. GH mRNA was detected in the lung, and its 693-bp sequence was identical to that in the pituitary gland. By in situ hybridization, this transcript was found to be abundantly expressed in the lungs of embryonic day (ED) 17 rats in mesenchymal, mucosal epithelial, and smooth muscle cells. This transcript was expressed in neonates until at least day 14 postnatally and was localized to type I and II epithelial cells and to pulmonary tissue macrophages and alveolar macrophages. GH immunoreactivity paralleled GH mRNA cellular localization throughout the time course studied. This immunoreactivity was specific and was lost after antibody preabsorption. The perinatal and postnatal lung is, therefore, an extrapituitary site of GH gene expression during development. Given that the GH receptor is present in the lung from early development, lung GH may have autocrine and/or paracrine roles in lung growth or differentiation or in pulmonary function.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Growth hormone expression in the perinatal and postnatal rat lung

Beyea

Olson

Harvey

2005

Developmental Dynamics

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“…Kaye 2002), actions that might be mediated through an array of other growth factors (Waters et al 1999;Sanders and Harvey 2004). Of relevance, insulin-like growth factor (IGF) is abundantly present in the lungs of embryonic chicks (Tanaka et al 1996) in which transforming growth factor (TGF)-β-4 (Jakowlew et al 1992), TGF-β-2 (Maina et al 2003;Calvitti et al 2004), and interleukin-1 (Calvitti et al 2004) are also widely expressed, possibly with effects on lung development.…”

Section: Discussionmentioning

confidence: 98%

Expression of growth hormone and its receptor in the lungs of embryonic chicks

et al. 2005

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The lung is well established as being a postnatal target site for growth hormone (GH) action, since pathophysiological states of GH excess and deficiency are both associated with impaired pulmonary function. Pituitary GH is therefore probably involved in normal lung growth or development, although perinatal lung development occurs prior to the differentiation of pituitary somatotrophs and the ontogeny of pituitary GH secretion. The lung itself may, however, be a site of GH production during prenatal development, since a specific GH-response gene (a marker of GH activity) is expressed in the lungs of early chick embryos, in which GH immunoreactivity is widespread in many other peripheral tissues. We have assessed this possibility in embryonic chicks. A 690-bp cDNA, identical in size and nucleotide sequence to the full-length pituitary GH transcript, was amplified by reverse transcription/polymerase chain reaction from total RNA extracted from the lungs of embryos at 11, 13, 15, and 18 days of the 21-day incubation period. This transcript was localized by in situ hybridization to mesenchymal and epithelial cells of the developing lungs, in which specific GH immunoreactivity was similarly located. Intense GH immunoreactivity was also present after embryonic day 15 (ED15) in the smooth muscle surrounding blood vessels in the lung and surrounding the bronchioles. Lung GH immunoreactivity was primarily associated with a 15-kDa protein, rather than the 26-kDa protein in the pituitary gland. After the onset of pituitary GH secretion (at ED17), GH mRNA was barely detectable in the lungs of ED20 embryos, at the start of lung breathing. GH immunoreactivity was, however, still present in some cells in the lungs of ED20 embryos. GH-receptor mRNA and immunoreactivity were also widespread and abundant within the embryonic lung. Lung GH may thus have autocrine or paracrine roles in lung development or in pulmonary function prior to the ontogeny of the pituitary gland and the appearance of GH in peripheral plasma.

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“…Human pituitary GHs are known to regulate growth, metabolism and development [2][3][4][5][6][7][8][9][10] and they constitute approximately 10% of the gland's dry weight [1,[11][12][13][14][15][16][17][18][19]. The predicted protein product of the normal hGH gene is a 22 kDa polypeptide chain of 191 amino acids possessing two intramolecular disulfide bridges [20][21][22].…”

Section: Introductionmentioning

confidence: 99%

Preparative alkaline urea gradient PAGE: Application to purification of extraordinarily‐stable disulfide‐linked homodimer of human growth hormone

et al. 2007

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The 40-60 pituitary human growth hormone (hGH) isoforms are so similar in their physico-chemical properties (charge, size, hydrophobicity) that the limited resolutions of chromatographic separation methodologies have not permitted most of them to be isolated. However, application of high-resolution preparative alkaline urea gradient PAGE has facilitated isolation of a disulfide-linked mercaptoethanol-resistant (MER) 45 kDa hGH dimer. Human pituitary extracts were separated by Sephadex G-100 chromatography under alkaline conditions. Pooled fractions containing MER-45 kDa hGH, as determined by SDS-PAGE, were then separated by Sephadex G-100 chromatography under acidic conditions followed by diethylaminoethyl (DEAE) anion-exchange chromatography. Pooled DEAE fractions containing MER-45 kDa hGH and other hGH isoforms were then separated by preparative electrophoresis in an alkaline polyacrylamide gradient (5-20%) slab gel containing 8 M urea into five distinct protein zones. One electroeluted zone contained pure MER-45 kDa hGH. The dimeric hGH isoform was immunoreactive at low concentrations (effective dose to produce 50% response (ED(50)) +/- S.E. = 58 +/- 5.00 pM) in a hGH radioimmunoassay, similar to that of standard monomeric hGH (ED(50) +/- S.E. = 22.93 +/- 3.90 pM), indicating that is was conformationally intact. Alkaline urea gradient PAGE is a valuable tool for preparative separation of structurally similar proteins such as isoforms of the hGH family.

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Growth hormone as an early embryonic growth and differentiation factor

Cited by 66 publications

References 134 publications

Growth hormone expression in the perinatal and postnatal rat lung

Growth hormone expression in the perinatal and postnatal rat lung

Expression of growth hormone and its receptor in the lungs of embryonic chicks

Preparative alkaline urea gradient PAGE: Application to purification of extraordinarily‐stable disulfide‐linked homodimer of human growth hormone

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