Plasma Growth Hormone (GH)-Binding Proteins: Effect on GH Binding to Receptors and GH Action*

Mannor, Dana A.; Winer, Lori M.; Shaw, Melissa A.; Baumann, Gerhard

doi:10.1210/jcem-73-1-30

Cited by 104 publications

(23 citation statements)

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“…This result is similar to that observed with GHBPs because GHBPs complex 45-55% of circulating GH under basal conditions (36 -38). This has been shown to slow the renal clearance of GH, thereby providing a longer lasting reservoir of hormone (39,40). Quantitative analysis of the molar concentration of the PRLBP, GH, and PRL indicated that the PRLBP is nearly saturated with somatolactogenic hormone, suggesting that the ligand-bound PRLBP may serve as a significant buffer to hormone levels.…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of the Prolactin-binding Protein in Human Serum and Milk

Kline

Clevenger

2001

Journal of Biological Chemistry

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The actions of prolactin (PRL) are mediated by its receptor, a member of the superfamily of single transmembrane cytokine receptors. High affinity binding proteins for the closely related growth hormone have been found in the sera of several species including humans and are generated by alternative splicing or proteolysis of the growth hormone receptor extracellular domain (ECD). In contrast, no conclusive evidence has been presented that an analogous prolactin-binding protein (PRLBP) is expressed in human serum. Using both monoclonal and polyclonal antibodies generated against hPRL and the ECD of the human prolactin receptor, co-immunoprecipitation analyses of human serum identified a 32-kDa hPRLBP capable of binding both hPRL and human growth hormone. A measurable fraction of circulating PRL (36%) was associated with the hPRLBP. Despite well documented sex differences in serum hPRL levels, there were no significant differences in the levels of hPRLBP found in the sera of normal adult males and females (15.3 ؎ 1.3 ng/ml versus 13.4 ؎ 0.8 ng/ml, respectively (mean ؎ S.E.)). Immunoprecipitation studies also detected the PRLBP in human milk albeit at lower concentrations than found in sera. Deglycosylation did not alter its electrophoretic mobility, indicating an absence of carbohydrate moieties and suggesting that the hPRLBP spans most of the PRLR ECD, a result confirmed by limited proteolysis and mass spectrometry. The potential function of this serum chaperone was assessed in vitro by the addition of recombinant hPRLBP to the culture medium of the PRL-dependent Nb2 T-cell line. These studies revealed that the hPRLBP antagonizes PRL action, inhibiting PRL-driven growth in a dose-dependent manner.

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Section: Discussionmentioning

confidence: 99%

Identification and Characterization of the Prolactin-binding Protein in Human Serum and Milk

Kline

Clevenger

2001

Journal of Biological Chemistry

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“…In vitro studies have shown that GHBP inhibits GH effects, regarding GH binding to GHR, as well as lipolysis, cell proliferation and IGF-I generation [81][82][83][84][85][86]. In contrast GHBP regulates GHR gene transcription in a human hepatoma cell line in a bidirectional manner: with low GHBP concentrations (50 pM) GH receptor gene transcription was increased, whereas high concentrations (500 pM) reduced GHR gene expression [87].…”

Section: Functional Roles Of Ghbpmentioning

confidence: 99%

Physiology and pathophysiology of growth hormone-binding protein: Methodological and clinical aspects

Fisker

2006

Growth Hormone & IGF Research

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“…Furthermore, GHBP may serve as a reservoir of GH, or it could play a role as transport protein presenting the GH molecule to the tissues. Alternatively, GHBP may compete with receptors for GH, and thereby inhibit GH actions [118][119][120], and determine the responsiveness to GH [121].…”

Section: Gh Binding Proteinsmentioning

confidence: 99%

Clinical pharmacological aspects of growth hormone administration

Laursen

2004

Growth Hormone & IGF Research

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Plasma Growth Hormone (GH)-Binding Proteins: Effect on GH Binding to Receptors and GH Action*

Cited by 104 publications

References 0 publications

Identification and Characterization of the Prolactin-binding Protein in Human Serum and Milk

Identification and Characterization of the Prolactin-binding Protein in Human Serum and Milk

Physiology and pathophysiology of growth hormone-binding protein: Methodological and clinical aspects

Clinical pharmacological aspects of growth hormone administration

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