The Growth Hormone Receptor

Waters, Michael J.

doi:10.1002/cphy.cp070513

Cited by 7 publications

(5 citation statements)

References 454 publications

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“…The effects of growth hormone on adipose tissue are complex at both the cellular and systemic levels (14–179). The mechanism by which GH elicits these effects at the cellular level is, therefore, not simple.…”

Section: Resultsmentioning

confidence: 99%

“…In most species two distinct GH binding moieties exist. These are termed the GH receptor and the GH binding protein, respectively (42). There appears to be at least two independent mechanisms for the generation of the GHBP.…”

Section: Gh Receptor Localization and Regulation In Adipose Tissuementioning

confidence: 99%

“…It is now apparent that alternate splicing of the GH receptor gene in humans generates a short membrane bound isoform of the receptor which preferentially generates the GHBP (43). In the rat, the alternatively spliced GH binding protein (BP) is also co‐ordinately expressed and regulated with the receptor in adipose tissue (41–44). Pregnancy does not regulate the level of adipose tissue GH receptor or GHBP expression in the mouse (45).…”

Section: Gh Receptor Localization and Regulation In Adipose Tissuementioning

confidence: 99%

“…Thus, in clonal cell lines (such as the 3T3‐F442A, 3T3‐L1 and Ob1771 cell lines) GH has been demonstrated to be antimitogenic (decreased proliferation of preadipocytes) (35–81). After the arrest of cellular proliferation, the differentiation programme under the control of insulin is executed resulting in the formation of mature adipocytes (35–78). In contrast to the clonal preadipocyte cell lines, GH stimulates the proliferation of preadipocytes in primary cultures obtained directly from rat and human adipose tissue and as a consequence inhibits the adipocyte differentiation process in these cells (82–89).…”

Section: Effect Of Gh On Adipocyte Functionmentioning

confidence: 99%

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The mechanism of effect of growth hormone on preadipocyte and adipocyte function

Nam

Lobie

2000

Obesity Reviews

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Growth hormone (GH) is not only the major regulator of postnatal somatic growth but also exerts profound effects on body composition through a combination of anabolic, lipolytic and antinatriuretic actions. GH enhancement of the lipolytic activity of adipose tissue in combination with a reduction of triglyceride accumulation via inhibition of lipoprotein lipase activity appears to be the major mechanism by which GH results in a reduction of the total fat mass. Recently, much progress has been made in understanding the molecular mechanism by which GH affects cellular function. This review provides a brief discourse and summary of the mechanism of effects of GH on preadipocyte/adipocyte function. It is intended to provide a functional understanding of the mechanism of action of GH as it relates to adipogenesis and adipocyte function.

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Section: Resultsmentioning

confidence: 99%

Section: Gh Receptor Localization and Regulation In Adipose Tissuementioning

confidence: 99%

Section: Gh Receptor Localization and Regulation In Adipose Tissuementioning

confidence: 99%

Section: Effect Of Gh On Adipocyte Functionmentioning

confidence: 99%

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The mechanism of effect of growth hormone on preadipocyte and adipocyte function

Nam

Lobie

2000

Obesity Reviews

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“…The GHR is a single-chain trans-membrane glycoprotein of 620 amino acids and member of the cytokine receptor family. Members of this family share limited homology in the extracellular domain, contain a single trans-membrane domain and lack intrinsic kinase activity (1,2). The multiple actions of GH start when one GH molecule interacts with two identical GHR molecules.…”

mentioning

confidence: 99%

The Ubiquitin-Proteasome Pathway Regulates the Availability of the GH Receptor

2002

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GH promotes not only longitudinal growth in children but is active throughout life in protein, fat, and carbohydrate metabolism. The multiple actions of GH start when GH binds to the cell surface-expressed GH receptor. Effectiveness of the hormone depends both on its presence in the circulation and the availability of receptors at the cell surface of target cells. In this study, we examined the role of the ubiquitin-proteasome pathway in regulating GH receptor availability. We show that receptor turnover is rapid, and almost 3-fold prolonged in the internalization-deficient mutant GH receptor (F327A). Using a monovalent GH antagonist, B2036, we could quantify the internalization of the nonactivated receptor. By comparing internalization of the receptor with shedding of the GH-binding protein, we show that in Chinese hamster lung cell lines, internalization followed by lysosomal degradation is the major pathway for receptor degradation and that the ubiquitin-proteasome pathway controls this process. Inhibition of endocytosis resulted in a 200% increase in receptor availability at the cell surface at steady state.

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