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The Growth Hormone Receptor

Michael J. Waters

10.1002/cphy.cp070513

Source: Supplement 24: Handbook of Physiology, The Endocrine System, Hormonal Control of Growth

Originally published: 1999

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Cloning of the Receptor
2 The Hematopoietic Cytokine Receptor Family
3 The Crystal Structure of the Growth Hormone Receptor and its Complex with the Hormone
3.1 Stoichiometry
3.2 Domain Structure
3.3 Binding to the Hormone
3.4 Comparison with the Prolactin Receptor
4 Structure of Growth Hormone and its Variants
4.1 Structural and Functional Studies on Human Growth Hormone
4.2 Nature of the Binding Specificity: Recruitment of Other Hormones
4.3 Improving the Binding Affinity
4.4 Binding to the Rabbit Growth Hormone Receptor
4.5 Determinants of Primate Specificity
5 Mechanisms for Generating the Biological Signals
5.1 Requirement for Dimerization
5.2 Apparent Exceptions to the Dimerization Requirement
5.3 Is Dimerization Sufficient? The Question of Conformational Change
6 The Growth Hormone Receptor Gene and the Syndrome of Growth Hormone Insensitivity
6.1 Structure of the Gene: Alternate Splicing
6.2 Primary Growth Hormone Insensitivity in Humans: Laron Dwarfism
7 The Growth Hormone‐Binding Protein
7.1 Early Studies
7.2 The Modern Era
7.3 Identity of the Growth Hormone–Binding Protein
7.4 Mode of Release of the Growth Hormone–Binding Protein
7.5 Functional Aspects of Growth Hormone–Binding Proteins
7.6 Utility of Serum Growth Hormone–Binding Protein as a Measure of Growth Hormone Receptor Expression
7.7 Physiological Considerations: Relation to Growth Potential
7.8 Methods of Measuring Growth Hormone–Binding Protein Status
7.9 Regulation of Growth Hormone–Binding Protein
8 Receptor Regulation
8.1 The Receptor Life Cycle
8.2 Short‐Term Processes: Downregulation
8.3 Long‐Term Regulation: Induction of Receptor Message
8.4 Ontogeny
8.5 Sex and Pregnancy
8.6 Growth Hormone
8.7 Steroids
8.8 Other Factors
9 Receptor Localization
10 Conclusion
Figure 1. Figure 1.

The hematopoietic receptor superfamily. The extracellular portions are at the top, the cell membrane is represented as a horizontal bar, and the cytoplasmic domains are the blue symbols below the membrane. Individual domains are shown by separate symbols, and extracellular modules with identical colors represent related structural units: pink, fibronectin type III module; yellow, cytokine receptor module; light blue, immunoglobulin module; green, fibronectin type III spacer. The conserved disulfide bonds in the cytokine receptor modules are shown, as is the position of the WSXWS box in the fibronectin type III modules. The receptors are labeled with the name of the ligand: GH, growth hormone; PRL, prolactin; IL‐4, interleukin 4; IL‐7, interleukin‐7; Epo, erythropoietin; G‐CSF, granulocyte colony‐stimulating factor; IL‐2, interleukin 2; IL‐3, interleukin 3; IL‐5, interleukin 5; GM‐CSF, granulocyte‐macrophage colony‐stimulating factor; IL‐6, interleukin 6; LIF/OSM, leukemia inhibitory factor/oncostatin M; CNTF, ciliary neurotrophic factor; MPL, the cellular counterpart of the viral mpl oncogene product.

From Kossiakoff et al. 225, with permission
Figure 2. Figure 2.

Structure of the human growth hormone–(extracellular receptor)2 complex. The hormone is shown in red, and receptor 1 is shown in green, except for the binding loops, which are shown in white. Receptor 2 is shown in turquoise, except for its binding loops, which are shown in yellow. In both cases, the upper β‐sandwich domain is referred to as domain 1 and the lower as domain 2. Because of the incompleteness of the crystal structure, some loops are not shown completely.
Figure 3. Figure 3.

Structure of the β‐sandwich domains. Strands A (domain 1, approx. residues 32–40) and A′ (domain 2, approx. residues 131–144) are shown in brown, strands B 46,47,48,49,50,51,52,53,54 and B′ 154,155,156,157,158,159,160,161,162,163,164,165,166,167 in red, strands C 64,65,66,67,68,69,70,71,72,73 and C′ 178,180,181,182,183,184,185,186 in turquoise, strands D 81,82,83,84,85,86,87,88,89 and D′ 192,193,194,195,196,197,198,199 in yellow, strands E 93,94,95,96,97,99,100,101,102,103 and E′ 203,204,205,207,208,209,210,211 in pink, strands F 109,110,111,112,113,114,116,117 and F′ 214,215,216,217,218,220,221,222,223 in blue, and strands G 121,122,123,124,125,126,127 and G′ 230,231,232,233,234,235,238,239,240,241,242,244,245,246 in green. Also shown are the disulfide bonds between cysteines 38 and 48, cysteines 83 and 94, and cysteines 108 and 122. Tryptophans 104 and 169 are also displayed.
Figure 4. Figure 4.

Map of alanine substitutions in human growth hormone (hGH) that disrupt binding of hGH‐binding protein (hGHBP) at either site 1 or site 2. The two sites are generally delineated by the large shaded circles. Residues for which alanine mutants reduce site 2 binding by two‐to‐fourfold, four‐to tenfold, ten‐to fiftyfold, and more than fiftyfold are shown by graduated squares (, , , and ), respectively. Residues marked by the symbols , , , and ○ represent sites where Ala mutations in site 1 of hGH cause reductions of two‐to fourfold, four‐to tenfold, greater than tenfold, or a fourfold increase in binding affinity for hGHBP, respectively, using the MAb 5 immunoprecipitation assay.

From Cunningham et al. 111, with permission
Figure 5. Figure 5.

Location of complementary “functional” epitopes for receptor (left) and hormone, site 1 (right). Residues are color‐coded for loss of binding energy upon alanine conversion.

From Clackson and Wells 97, with permission
Figure 6. Figure 6.

Display of site 1 electrostatic contacts between receptor Arg 43 and two charged or polar residues on hormone helix 4 (Asp 171 and Thr 175). The alkyl portion of the Arg 43 side chain packs beneath the indole ring of Trp 169 on the receptor, so Arg 43 may play an indirect structural role in supporting Trp 169 in addition to directly interacting with Asp 171 and Thr 175. Phe 176 sits across this view, over Trp 104. The observed energetic contributions of each side chain are indicated in parentheses.

From Clackson and Wells 97 with permission
Figure 7. Figure 7.

An example of the importance of both intramolecular and intermolecular alkyl‐aromatic stacking interactions in the hGH:hGHbp interface. The side‐chain of Trp 169 is sandwiched between Arg 43 of the receptor and Arg 64 of hGH. Both arginine residues are oriented by intermolecular charge‐mediated hydrogen bonds.

From Clackson et al. 98 with permission
Figure 8. Figure 8.

Receptor‐binding epitopes of human growth hormone defined by alanine scanning, showing residues which upon conversion to alanine resulted in a greater than twofold change in affinity. Diameter of sphere is proportional to magnitude of change. Light spheres for loss of affinity on alanine conversion, black spheres for gain in affinity.

From Lowman and Wells 246, with permission
Figure 9. Figure 9.

Receptor site 1 residues contributing to binding of human growth hormone, as defined by alanine substitution 97. In addition to the residues shown here, Bass et al. 38 found that alanine conversion of Glu 42, Thr 101, Val 125, and Asp 132 results in a reduction in affinity that is less than one‐sixth that of the native receptor.

From Clackson and Wells 97, with permission
Figure 10. Figure 10.

Relative change in on‐rates and off‐rates for residues in human growth hormone (hGH) site 1 upon conversion to alanine. Data obtained by use of a BIAcore sensor with immobilized hGH receptor (extracellular).

From Cunningham and Wells 114, with permission
Figure 11. Figure 11.

Comparison of the structure of the 1:1 human growth hormone (hGH)–(human prolactin extracellular receptor) complex (a) with that of the 1:2 hGH‐(hGH extracellular receptor)2 complex (b), showing close similarity in tertiary structure.

From Somers et al. 361, with permission
Figure 12. Figure 12.

Schematic of prolactin receptor‐binding site on human growth hormone, as defined by alanine scanning. Chelated Zn2+ is shown binding to His 18 and Glu 174, though binding to His 21 does not appear to occur in the hormone receptor complex.

From Cunningham and Wells 113, with permission
Figure 13. Figure 13.

Mechanism for signal transduction by the human growth hormone (hGH) receptor, as proposed by Fuh et al. 157. At low GH concentrations, a productive dimer forms, activating Janus Kinase 2 (JAK 2), whereas at high hormone concentrations all receptors are occupied by site 1 interactions with hormone and signaling is inhibited.

From Fuh et al. 157, with permission
Figure 14. Figure 14.

A: Close interaction between hormone residue Gly 120 and receptor residue Trp 104, critical in site 2 interactions. Substitution of arginine for glycine would clearly disrupt the position of Trp 104. B: Effect of lowering site 1 or site 2 affinity on proliferative signaling by a human growth hormone (hGH) receptor chimera. Open circles, wild‐type hGH dose response. Closed circles, response to mutant with lowered site 1 affinity (K172A/F176A). Squares, response to G120R hGH.

From Fuh et al. 157, with permission
Figure 15. Figure 15.

Effects of binding constants on the formation of dimeric complexes. The formation of receptor–hormone–receptor (dimer) complexes was simulated at steady state at three different values of Kd1 (A) and Kd2 (B). The predicted curves, expressed as a fraction of total receptor concentration (R0), are represented as a function of total receptor concentration (logarithmic scale). A: Simulated effects of Kd1 on dimer formation. Kd1 values for the curves from left to right are shown; Kd2 was kept constant at 0.5 nM. B: Simulated effects of Kd2 on dimer formation. Kd2 values for the curves from top to bottom are shown; Kd1 was kept constant at 0.5 nM.

From Hondo et al. 212, with permission
Figure 16. Figure 16.

Simulation of the Scatchard plot for the sequential dimerization model. Kd1 and Kd2 were kept constant at 0.5 nM. Total receptor concentration (R0) values for the three curves are shown. Note that the ordinate is normalized to R0.

From Hondo et al. 212, with permission
Figure 17. Figure 17.

Schematic map of point mutations in the growth hormone (GH) receptor gene identified in patients with GH insensitivity. The asterisk indicates the splice mutation identified in the Ecuadorean population.

From Rosenfeld et al. 323, with permission
Figure 18. Figure 18.

Location of known growth hormone (GH) receptor missense mutations resulting in Laron dwarfism, shown in red along with the GH inactivation mutation (R77C) 377. A second D112G mutant is not shown 378. The Ecuadorean splice deletion is shown in pink. See Table 2 for further details.
Figure 19. Figure 19.

Illustration of the effect of growth hormone–binding protein (GHBP) on a pulsatile GH secretory pattern.

From Veldhuis et al. 405, with permission


Figure 1.

The hematopoietic receptor superfamily. The extracellular portions are at the top, the cell membrane is represented as a horizontal bar, and the cytoplasmic domains are the blue symbols below the membrane. Individual domains are shown by separate symbols, and extracellular modules with identical colors represent related structural units: pink, fibronectin type III module; yellow, cytokine receptor module; light blue, immunoglobulin module; green, fibronectin type III spacer. The conserved disulfide bonds in the cytokine receptor modules are shown, as is the position of the WSXWS box in the fibronectin type III modules. The receptors are labeled with the name of the ligand: GH, growth hormone; PRL, prolactin; IL‐4, interleukin 4; IL‐7, interleukin‐7; Epo, erythropoietin; G‐CSF, granulocyte colony‐stimulating factor; IL‐2, interleukin 2; IL‐3, interleukin 3; IL‐5, interleukin 5; GM‐CSF, granulocyte‐macrophage colony‐stimulating factor; IL‐6, interleukin 6; LIF/OSM, leukemia inhibitory factor/oncostatin M; CNTF, ciliary neurotrophic factor; MPL, the cellular counterpart of the viral mpl oncogene product.

From Kossiakoff et al. 225, with permission


Figure 2.

Structure of the human growth hormone–(extracellular receptor)2 complex. The hormone is shown in red, and receptor 1 is shown in green, except for the binding loops, which are shown in white. Receptor 2 is shown in turquoise, except for its binding loops, which are shown in yellow. In both cases, the upper β‐sandwich domain is referred to as domain 1 and the lower as domain 2. Because of the incompleteness of the crystal structure, some loops are not shown completely.



Figure 3.

Structure of the β‐sandwich domains. Strands A (domain 1, approx. residues 32–40) and A′ (domain 2, approx. residues 131–144) are shown in brown, strands B 46,47,48,49,50,51,52,53,54 and B′ 154,155,156,157,158,159,160,161,162,163,164,165,166,167 in red, strands C 64,65,66,67,68,69,70,71,72,73 and C′ 178,180,181,182,183,184,185,186 in turquoise, strands D 81,82,83,84,85,86,87,88,89 and D′ 192,193,194,195,196,197,198,199 in yellow, strands E 93,94,95,96,97,99,100,101,102,103 and E′ 203,204,205,207,208,209,210,211 in pink, strands F 109,110,111,112,113,114,116,117 and F′ 214,215,216,217,218,220,221,222,223 in blue, and strands G 121,122,123,124,125,126,127 and G′ 230,231,232,233,234,235,238,239,240,241,242,244,245,246 in green. Also shown are the disulfide bonds between cysteines 38 and 48, cysteines 83 and 94, and cysteines 108 and 122. Tryptophans 104 and 169 are also displayed.



Figure 4.

Map of alanine substitutions in human growth hormone (hGH) that disrupt binding of hGH‐binding protein (hGHBP) at either site 1 or site 2. The two sites are generally delineated by the large shaded circles. Residues for which alanine mutants reduce site 2 binding by two‐to‐fourfold, four‐to tenfold, ten‐to fiftyfold, and more than fiftyfold are shown by graduated squares (, , , and ), respectively. Residues marked by the symbols , , , and ○ represent sites where Ala mutations in site 1 of hGH cause reductions of two‐to fourfold, four‐to tenfold, greater than tenfold, or a fourfold increase in binding affinity for hGHBP, respectively, using the MAb 5 immunoprecipitation assay.

From Cunningham et al. 111, with permission


Figure 5.

Location of complementary “functional” epitopes for receptor (left) and hormone, site 1 (right). Residues are color‐coded for loss of binding energy upon alanine conversion.

From Clackson and Wells 97, with permission


Figure 6.

Display of site 1 electrostatic contacts between receptor Arg 43 and two charged or polar residues on hormone helix 4 (Asp 171 and Thr 175). The alkyl portion of the Arg 43 side chain packs beneath the indole ring of Trp 169 on the receptor, so Arg 43 may play an indirect structural role in supporting Trp 169 in addition to directly interacting with Asp 171 and Thr 175. Phe 176 sits across this view, over Trp 104. The observed energetic contributions of each side chain are indicated in parentheses.

From Clackson and Wells 97 with permission


Figure 7.

An example of the importance of both intramolecular and intermolecular alkyl‐aromatic stacking interactions in the hGH:hGHbp interface. The side‐chain of Trp 169 is sandwiched between Arg 43 of the receptor and Arg 64 of hGH. Both arginine residues are oriented by intermolecular charge‐mediated hydrogen bonds.

From Clackson et al. 98 with permission


Figure 8.

Receptor‐binding epitopes of human growth hormone defined by alanine scanning, showing residues which upon conversion to alanine resulted in a greater than twofold change in affinity. Diameter of sphere is proportional to magnitude of change. Light spheres for loss of affinity on alanine conversion, black spheres for gain in affinity.

From Lowman and Wells 246, with permission


Figure 9.

Receptor site 1 residues contributing to binding of human growth hormone, as defined by alanine substitution 97. In addition to the residues shown here, Bass et al. 38 found that alanine conversion of Glu 42, Thr 101, Val 125, and Asp 132 results in a reduction in affinity that is less than one‐sixth that of the native receptor.

From Clackson and Wells 97, with permission


Figure 10.

Relative change in on‐rates and off‐rates for residues in human growth hormone (hGH) site 1 upon conversion to alanine. Data obtained by use of a BIAcore sensor with immobilized hGH receptor (extracellular).

From Cunningham and Wells 114, with permission


Figure 11.

Comparison of the structure of the 1:1 human growth hormone (hGH)–(human prolactin extracellular receptor) complex (a) with that of the 1:2 hGH‐(hGH extracellular receptor)2 complex (b), showing close similarity in tertiary structure.

From Somers et al. 361, with permission


Figure 12.

Schematic of prolactin receptor‐binding site on human growth hormone, as defined by alanine scanning. Chelated Zn2+ is shown binding to His 18 and Glu 174, though binding to His 21 does not appear to occur in the hormone receptor complex.

From Cunningham and Wells 113, with permission


Figure 13.

Mechanism for signal transduction by the human growth hormone (hGH) receptor, as proposed by Fuh et al. 157. At low GH concentrations, a productive dimer forms, activating Janus Kinase 2 (JAK 2), whereas at high hormone concentrations all receptors are occupied by site 1 interactions with hormone and signaling is inhibited.

From Fuh et al. 157, with permission


Figure 14.

A: Close interaction between hormone residue Gly 120 and receptor residue Trp 104, critical in site 2 interactions. Substitution of arginine for glycine would clearly disrupt the position of Trp 104. B: Effect of lowering site 1 or site 2 affinity on proliferative signaling by a human growth hormone (hGH) receptor chimera. Open circles, wild‐type hGH dose response. Closed circles, response to mutant with lowered site 1 affinity (K172A/F176A). Squares, response to G120R hGH.

From Fuh et al. 157, with permission


Figure 15.

Effects of binding constants on the formation of dimeric complexes. The formation of receptor–hormone–receptor (dimer) complexes was simulated at steady state at three different values of Kd1 (A) and Kd2 (B). The predicted curves, expressed as a fraction of total receptor concentration (R0), are represented as a function of total receptor concentration (logarithmic scale). A: Simulated effects of Kd1 on dimer formation. Kd1 values for the curves from left to right are shown; Kd2 was kept constant at 0.5 nM. B: Simulated effects of Kd2 on dimer formation. Kd2 values for the curves from top to bottom are shown; Kd1 was kept constant at 0.5 nM.

From Hondo et al. 212, with permission


Figure 16.

Simulation of the Scatchard plot for the sequential dimerization model. Kd1 and Kd2 were kept constant at 0.5 nM. Total receptor concentration (R0) values for the three curves are shown. Note that the ordinate is normalized to R0.

From Hondo et al. 212, with permission


Figure 17.

Schematic map of point mutations in the growth hormone (GH) receptor gene identified in patients with GH insensitivity. The asterisk indicates the splice mutation identified in the Ecuadorean population.

From Rosenfeld et al. 323, with permission


Figure 18.

Location of known growth hormone (GH) receptor missense mutations resulting in Laron dwarfism, shown in red along with the GH inactivation mutation (R77C) 377. A second D112G mutant is not shown 378. The Ecuadorean splice deletion is shown in pink. See Table 2 for further details.



Figure 19.

Illustration of the effect of growth hormone–binding protein (GHBP) on a pulsatile GH secretory pattern.

From Veldhuis et al. 405, with permission
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Article Title: The Growth Hormone Receptor
 

How to Cite

Michael J. Waters. The Growth Hormone Receptor. Compr Physiol 2011, Supplement 24: Handbook of Physiology, The Endocrine System, Hormonal Control of Growth: 397-444. First published in print 1999. doi: 10.1002/cphy.cp070513