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Department of Medicine, Clinical Sciences Centre (R.J.M.R., X.Y.S., S.V.L.)and Institute of Cancer Studies (P.R.M.D.) Sheffield University, Sheffield S5 7AU Department of Endocrinology (S.L.C.) St. Bartholomew’s Hospital London EC1A 7BE, UK INSERM unite 344 (N.E., M.-C. P.-V., J.F.) Endocrinologie Moleculaire Faculte de Medecine Necker 75730 Paris, France
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ABSTRACT |
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INTRODUCTION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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The human GHR and GHBP are products of a single gene (5). Exon 2 codes
for the signal peptide, the extracellular domain is coded by exons 3 to
7, the transmembrane domain is coded by exon 8, while exons 9 and 10
encode the cytoplasmic domain and the 3'-untranslated region (6).
Different isoforms for various members of the cytokine receptor
superfamily have been reported. For the GHR an exon 3 skipped isoform
(exon 3-) is expressed in placenta, liver, and various cultured cells
(7). For the rat PRL receptor, short isoforms with a limited or absent
cytoplasmic domain have been identified (8, 9). For PRL the short and
long isoforms are expressed in a tissue-specific manner and regulated
by estrus (10). Five different human granulocyte-colony stimulating
factor (G-CSF) isoforms, arising from alternative splicing, have been
isolated and are identical in the extracellular domain but differ in
their downstream sequences (11). Three different isoforms of the
-subunit of the granulocyte macrophage (GM)-CSF receptor have been
reported, one of which encodes a soluble receptor (12).
We postulated that there is alternative splicing of the human GHR around the transmembrane domain but that this may not have been identified on Northern blotting if all transcripts were of approximately the same size or if transcripts were of low abundance. To test this hypothesis we designed primers in exons 7 and 10 and, using a RT-PCR-based technique, tested for alternative splicing in mRNA from human liver and cultured cells. In this paper, we show that two variants could be identified, and functional studies indicate that, in spite of their low abundance, they could have a physiological role generating large amounts of GHBP and interacting with the full-length receptor.
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RESULTS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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) RT-PCR of human liver revealed three products at 453,
427, and 383 bp (Fig. 2). The individual bands were
extracted from polyacrylamide, cloned into pCRII, and sequenced. The
453-bp product had an identical sequence to that previously published
for the GHR (GHRfl) (5). The 427-bp (GHR1-279) product utilized an
alternative 3'-acceptor splice site in exon 9. Exon 8 was as expected
but spliced to a 3'-splice acceptor site within exon 9, thus omitting
the upstream 26 bp of exon 9. The nucleotide sequence at this
position in exon 9 matches the mammalian consensus for a 3'-acceptor
CAG/TT at position 944 in the Genbank sequence (X06562). The 383-bp
(GHR1-277) product skipped exon 9 with exon 8 splicing to exon 10. The
predicted peptides have been labeled by their amino acid number
according to Leung et al. (5).
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). The translated sequence is the same as
the full-length receptor for the first three to four amino acids of the
cytoplasmic domain of GHR1-279 and GHR1-277, respectively, but the
predicted peptides deviate from each other before the proline-rich box
I region of the receptor that is required for signal transduction (13, 14).
The alternative splice variants of the GHR were also identified in
cultured IM-9 cells. Since all three splice variants compete for the
same primers and PCR reagents in a common reaction, the relative
optical densities of the three bands were assumed to reflect the
proportion of the variants in the template cDNA. The 453 bp and 427 bp
products are clearly seen in Fig. 3a. The 383 product
was seen only on overexposed autoradiographs (data not shown).
Quantification on appropriately exposed autoradiographs by an image
densitometer revealed that the proportions of the alternative splice
products were similar in all experiments. Thus, GHR1-279 was 1–10% of
GHRfl, and GHR1-277 was consistently less than 1%. RNase protection
(Fig. 3b) confirmed the presence of the GHR1-279 alternative splice
product in human liver and IM-9 cells in similar proportions to the
full-length receptor as seen by RT-PCR. The GHR1-277 splice variant was
not identified by RNase protection.
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Cross-linking studies with [125I]-hGH on cells
transiently transfected with GHRfl or GHR1-279 cDNAs are shown in Fig. 4. In both cases specific complexes, displaced in the
presence of an excess of native hormone, were observed. In cells
transfected with GHRfl, the apparent sizes of the radioactive bands
(
140 and 260 kDa) were those expected for complexes of one or two
molecules of receptor and one hormone molecule, respectively. In cells
transfected with GHR1-279 cDNA, the amount of radioactivity in both
complexes is much higher than that observed with the full-length
receptor. This is consistent with the data from binding experiments
indicating that the number of receptors in the cell membrane is greater
after transfection with the GHR1-279 cDNA. The apparent sizes of the
two complexes are approximately 75 kDa and 150 kDa and correspond to
the sizes expected for one or two molecules of GHR1-279 bound to one
molecule of hormone.
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). The first peak was
completely displaced by an excess of native hGH, and its elution time
corresponded to that previously described for GHBP in human serum (15)
or media of human hepatoma cells (16). The second peak corresponds to
the free [125I]-hGH. Sixty percent of radioactivity was
in the first peak when 100 µl of culture media from cells transfected
with GHRfl were analyzed. A similar binding activity, corresponding to
GHBP, was found when only 5 µl GHR1-279 media were used,
demonstrating a 20-fold increase of GHBP in media from cells
transfected with GHR1-279.
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). The
expression of GHRfl was detected by immunoprecipitation using a
polyclonal antibody (GHR-intra) raised against an epitope in the
intracellular domain of human GHR (not present in GHR1-279) (2). To
purify the receptor in cells transfected with GHR1-279 alone, we
incubated the cells with biotinylated hGH and purified the complexes
with streptavidin beads after lysis. The soluble forms in media were
also purified with biotinylated hGH and streptavidin beads. In order to
detect a possible heterodimerization between GHRfl and GHR1-279, cells
were cotransfected with 5 µg of each cDNA and stimulated with hGH (in
order to induce dimerization) before lysis. The complexes formed were
then immunoprecipitated with the GHR-intra antibody. Western blots
were performed with mAb263, which recognizes all membrane and soluble
forms of the GHR. The results are shown in Fig. 6. GHRfl
appeared as a single band around 120 kDa (lane 1). GHR1-279 consisted
in two bands; the size of the major band was around 55-60 kDa; the
minor band, around 46 kDa, was likely a degradation product (lane 3).
Soluble receptors in the supernatant of cells transfected with either
GHRfl (lane 5) or GHR1-279 (lane 6) were single bands of apparently 60
kDa, similar in size to the upper band identified in normal serum (lane
7). In cells cotransfected with GHRfl and GHR1-279, three bands were
detected with the mAb263 (lane 2). The upper band migrated as the GHRfl
(lane 1), and the two other bands migrated as GHR1-279 (lane 3). No
band could be detected when lysates of cells transfected with GHR1-279
alone were immunoprecipitated with the GHR-intra antibody (lane 4).
These results demonstrate that GHRfl and GHR1-279 can heterodimerize on
GH stimulation.
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2 x 103 receptor sites per cell) and increasing
amounts of GHR1-279 cDNA. In conditions providing maximal stimulation
of the reporter gene (20 nM hGH), we observed a 12-fold
stimulation of luciferase activity in cells transfected with GHRfl
alone. No stimulation of luciferase was observed, as expected in cells
transfected with GHR1-279 alone. When increasing amounts of GHR1-279
cDNA (from 0.01 to 1.0 µg) were cotransfected with 0.1 µg of GHRfl
cDNA, a dose-dependent inhibition was observed (Fig. 7).
For a ratio similar to that observed in vivo (GHR1-279
vs. GHRfl = 10%), the inhibition of luciferase
activity was 5% when 20 nM hGH was used in the functional
test but 30% when a more physiological level, 1 nM hGH,
was used. This physiological hormone concentration induced a 3-fold
stimulation of the reporter gene in cells transfected with GHRfl. As
the degree of inhibition appears dependent on the concentration of hGH
in the medium, this suggests that the inhibition of GHRfl signaling by
the short form could be also due to a competition between GHRfl and
GHR1-279 for binding of GH.
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DISCUSSION |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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Following transfection of the short form, GHR1-279, in mammalian
cells we identified a 75-kDa protein in cell membranes by
cross-linking with GH. A similar size protein had been previously
identified in human liver (18). At that time, two molecular forms of
the hormone-receptor complex were observed in human liver with
estimated sizes of 124 and 75 kDa (18). It was not clear whether the
smaller form was a degradation product of the expected 124-kDa receptor
complex. Taking into account our current results it is possible it
could be generated from the splice variant that we detected in human
liver. In human choroid plexus, cross-linking studies identified only
one hormone-bound complex again at 75 kDa (19). In the rat there is
evidence for a short form of the receptor bound in the membrane of
adipocytes (20), and it has been speculated that similar forms will be
found in the human (21).
This paper investigated the functional significance of the most abundant alternative splice variant reported, GHR1-279. This short isoform of the receptor, which retains the transmembrane domain but is divergent in the cytoplasmic domain, was subcloned into an expression vector and transfected into 293 cells. Binding assays with entire cells indicated that in spite of its short cytoplasmic domain, GHR1-279 is held in the cell membrane. However, the GHR1-279 had a reduced affinity and increased binding capacity compared to the full-length receptor. The binding affinity (Ka) for GHRfl was 1.2 x 109 M-1 similar to that previously published for the human liver GHR (18). GHR1-279 had a 2-fold lower affinity of 0.6 x 109 M-1 similar to the GHBP in human serum (22), which has a 5-fold lower affinity compared to the human liver GHR (23). A possible explanation for these results is that the length of the cytoplasmic domain could affect the general structure of the receptor and its ligand affinity. The differences in the binding capacity for expressed GHR1-279 vs. GHRfl is consistent with that previously observed for truncated GHRs. In CHO clones stably expressing a truncated form of the rabbit GHR (which retains only 46 amino acids in its cytoplasmic domain) the number of binding sites for this mutant was 8 times higher than that for CHO clones stably expressing GHRfl (14). We have observed that the increase in binding sites correlates with an impaired internalization of the receptor (L. S. Moutoussamy et al., manuscript in preparation). A similar finding has been reported with short isoforms of the rat GHR (24). Critical residues for internalization of the receptor have been mapped for the rat GHR (24), which are located in a cytoplasmic domain that is absent in the truncated rabbit GHR or in GHR1-279. Recently the involvement of the ubiquitin system has been demonstrated in GHR internalization and the putative amino acid sequence for ubiquitination present in the GHR sequence is absent in GHR1-279 as well as in the short forms of rat and rabbit receptor mentioned above (25). However, when coexpressed in cells with the GHRfl, a proportion of GHR1-279 could be internalized through heterodimerization with GHRfl. The extent of this phenomenon remains to be established.
GHBP in the media of cells was studied by HPLC gel filtration and Western blotting after affinity purification. By HPLC, a GHBP with similar characteristics to human serum GHBP was identified in the media of cells transfected with GHR1-279. There was an increased amount of GHBP in the medium of cells transfected with GHR1-279 as compared with that measured in the media of cells transfected with GHRfl, when similar amounts of cDNA were transfected. This could be related to increased levels of the short isoform at the cell surface and/or reduced internalization allowing more receptor to be available for proteolysis. On Western blotting human serum revealed two bands of the expected sizes for the GHBP (60 and 55 kDa) (22, 23, 26). Media from cells transfected with GHRfl and GHR1-279 demonstrated a protein of 60 kDa similar to the predominant protein in human serum. We can postulate that, in spite of its low level of mRNA expression, the spliced variant could generate a proportion of the circulating GHBP.
Immunoprecipitation experiments demonstrated that heterodimers could be
formed between GHRfl and GHR1-279. Western blot analysis of the
complexes immunoprecipitated with a cytoplasmic domain antibody,
GHR-intra, and probed with an extracellular domain antibody, mAb263,
indicated that GHR1-279 could only be immunoprecipitated when complexed
with GHRfl. The identity of GHR1-279 in the heterodimeric complex was
assessed by its comigration with the very large band detected when
GHR1-279 was precipitated with streptavidin after binding to
biotinylated hGH. The finding of heterodimerization suggests that
GHR1-279 may act in a dominant negative fashion to inhibit receptor
signaling in addition to competitively binding GH.
GHR signaling involves GH-dependent receptor dimerization, activation of the tyrosine kinase JAK2, and the subsequent recruitment and tyrosine phosphorylation of various Stat proteins including Stat1, Stat3, and Stat5 (27). JAK2 activation is dependent on its association with the receptor that is mediated by the juxtamembranous region of the cytoplasmic domain, including the proline-rich region box1 (14, 28). Functional tests using a reporter gene containing the Stat5-binding element were performed to test the possibility that GHR1-279 could act as a negative regulator of the full-length receptor. We observed such an effect even when the ratio of the cDNAs transfected was 1:10 for GHR1-279 to GHRfl. As the degree of inhibition was dependent on the concentration of hGH, it suggests that inhibition was also related to a decreased availability of the ligand for the active GHRfl dimer when the short form receptor is expressed. Preliminary data have been reported suggesting a dominant negative effect for other GHR mutants (29), and a dominant negative effect was seen with the PRL receptor when similar proportions of cDNA encoding a short form were transfected (30). In addition, there is a report of a patient heterozygous for a GHR mutation resulting in the expression of a protein identical to GHR1-277 (31). This patient presented with short stature, and the authors suggest the short form of the receptor may act in a dominant negative fashion. Our data support this hypothesis. Studies with the G-CSF receptor have shown that expression of the various isoforms was tissue specific; aberrations in the expression of these various isoforms have been reported and postulated to play a role in the pathogenesis of disorders of granulopoiesis (11). Thus, it is possible that differential expression of GHR isoforms could play a role in the physiological regulation of receptor function in some genetic or acquired GH disorders.
The truncated receptor GHR1-279 has recently been identified in rabbit as well as in human tissues (32). Using PCR analysis there was differential expression of the truncated receptor with low abundance of the alternative splice in liver, kidney, and fibroblasts but similar expression to the full-length receptor in mammary gland and adipose tissue. The differential tissue expression of alternative splicing may regulate the production of GHBP. In addition, the truncated receptor may act to inhibit GH signaling in some tissues or act as a transport protein, as has been suggested for the truncated form of leptin receptor expressed in the choroid plexus (33).
Our results indicate that while only a single mRNA species is detected by Northern blotting, alternative forms of mRNA for the GHR are transcribed. These splice variants encode short forms of the receptor that could play a role in the generation of a GHBP in the human and can modulate the function of the full-length receptor.
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MATERIALS AND METHODS |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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RNA Extraction and RT-PCR
This was performed as described (34). Total RNA was
extracted using an acid phenol/guanidinium isothiocyanate method
(RNAzol B, Biogenesis, Poole, U.K.). RNA quantification was performed
spectrophotometrically and quality assessed by agarose-formaldehyde gel
electrophoresis. Complementary DNA was made using 5 µg total RNA with
200 U MMLV reverse transcriptase (BRL, Gaithersburg, MD), 5 µg random
hexamer primers (Boehringer Mannheim, Indianapolis, IN), and 200
µM final concentration of deoxynucleosidetriphosphate in
a 50-µl reaction. The reaction was performed at 24 C for 10 min, 37 C
for 60 min, and 92 C for 10 min. PCR amplification of GHR transcripts
was performed using 5 µl cDNA (equivalent to 0.5 µg total RNA) in a
50-µl volume with: 200 µM final concentration of
deoxynucleosidetriphosphate; 2.5 mM final concentration
MgCl2, 2 µM final concentration of each
primer, and 1 U Taq DNA polymerase. After heating to 94 C for 3 min, 30
cycles were performed at 94 C for 30 sec, 56 C for 1 min, and 72 C for
2 min, before a final step of 72 C for 10 min. All PCR reactions
included negative controls with water.
Primers (Fig. 1)
Primers were manufactured by Genosys (Cambridge, U.K.). For the
GHR, primer PS is in exon 7 starting at nucleotide 709
(5'-GGATAAGGAATATGAAGTGC-3') and was used with primer PAS in exon 10
starting at nucleotide 1161 (5'-GATTTCTCATGGTCACTGC-3') predicting a
product of 453 bp.
Cloning, Sequencing, and Southern Blotting
PCR products were cloned into the pCRII vector (Invitrogen, San
Diego, CA) according to the manufacturer’s protocol, and dideoxy
sequencing was with the Sequenase 2.0 kit according to the
manufacturer’s instructions (USB, Cleveland, OH). RT-PCR products were
transferred from polyacrylamide gels (6–12%) onto a nylon membrane
(Hybond N+, Amersham, Little Chalfont, U.K.) by electroblot (Bio-Rad,
Hemel Hempstead, U.K.). GHR cDNA probes were prepared by PCR using 0.1
µg of the GHR453 plasmid as a template; products were run on 1%
agarose, excised, purified (Geneclean, Bio 101) and random primer
labeled with 30 µCi [32P]dCTP (Oligolabeling kit,
Pharmacia, Piscataway, NJ). The probes were separated by a Sephadex G50
column. Prehybridization (4 h) and hybridization (18 h) were performed
at 42 C in 50% formamide. Posthybridization washes were twice in 2x
sodium citrate chloride/0.2% SDS for 30 min at room temperature, then
twice in 0.1 x sodium citrate chloride/0.1% SDS at 55 C for 30
min each. The membranes were exposed to Kodak XAR film.
Quantification
Autoradiographs were scanned by an image densitometer (GS 670,
Bio-Rad) and optical densities analyzed by Molecular Analyst software
(Bio-Rad). A standard PCR reaction was performed on normal liver cDNA
with product being sampled after every tenth cycle for 40 cycles to
assess the kinetics of the reaction.
IM-9 Cell Cultures
Human IM-9 lymphocytes were grown in RPMI 1640 medium (all
reagents, from Sigma, St. Louis, MO), containing 10% (vol/vol) FCS,
100 U/ml penicillin, and 100 µg/ml streptomycin, 2 nM
L-glutamine at 37 C in 5% CO2. The cells were
cultured to stationary phase, counted with a hemocytometer, centrifuged
at 200 x g, washed three times in RPMI 1640, and
resuspended in RPMI 1640 and 0.1% wt/vol BSA. After 24 h cells
were harvested and total RNA extracted as described above. HepG2 and
293 cells were cultured and transfected by the CaPO4 method
as previously described (17, 34).
RNase Protection
The GHR riboprobe was constructed using the GHR1-279
plasmid in pCRII (Invitrogen). The plasmid was linearized by digestion
with Ncol, and in vitro transcription by T7 RNA
polymerase produced an antisense probe of 385 bp, which was gel
purified. RNase protection was performed on 25 µg total RNA from
yeast (negative control), IM-9 cells, human liver, HepG2 cells, and
HepG2 cells stably transfected with the GHRfl (this stably transfected
cell line was used as a positive control for the full-length GHR
message). Total RNA was hybridized with labeled GHR antisense probe
(GHR1-279) overnight at 45 C in 80% (vol/vol) formamide, 40
mM piperazine N,N'-bis (2-ethanesulfonic acid, pH 6.4), 400
mM sodium chloride, and 1 mM EDTA. After
hybridization, 8 µg/ml RNase A and 0.4 µg/ml RNase T1 (Sigma,
Dorset, UK) were added and incubated for 1 h at 30 C to digest
nonhybridized RNA. Protected hybrids were isolated by ethanol
precipitation and separated on a 6% polyacrylamide/7 M
urea denaturing sequencing gel. The dried gel was exposed to x-ray
film. The expected protected fragments were 296 bp for the GHR1-279
alternate splice and 217 bp for the GHRfl (the smaller hybrid for the
full length as GHR1-279 was used as the probe).
Construction of GHRfl and GHR1-279 Expression Vectors
The full-length human GHR has proved difficult to assemble and
propagate in E. coli. This problem has been
overcome by changing 24 nucleotides largely in the transmembrane domain
while maintaining the native amino acid sequence (35). This construct,
kindly provided by Genetech, was subcloned into the expression vector
pcDNAI/Amp (Invitrogen) using the BamHI and SnaBI
restriction sites to produce the GHRfl. This construct contains a
unique BstBI site engineered at the end of exon 8, which is
not found in the native sequence. The expression vector GHR1-279 was
constructed by introducing a BstBI restriction site by PCR
amplification of GHR1-279, subcloning back into the pCRII vector
(Invitrogen), then digesting with BstBI and NotI,
and ligating into the GHRfl at the same sites. The construct was then
sequenced to confirm the modified sequence.
Binding Assays
Twenty four hours after transfection, the cells were serum
starved for 12 h. The culture media was removed and concentrated
(20x) to be analyzed for the presence of GHBP using gel filtration and
HPLC (15). Cells were then washed with PBS containing 1% BSA and
incubated with [125I]-hGH (5 x 105
cpm/well) for 3 h at room temperature in the absence or presence
of various concentrations of unlabeled hGH. The cells were then washed
in the same buffer and solubilized in 1 ml NaOH 1 N for
counting radiation.
Cross-Linking
Cells were grown in six-well plates and transfected with 5 µg
cDNA; 5 x 105 cpm/well of [125I]-hGH
were added to the dishes in the absence or presence of 5 µg/ml of
cold hGH, and incubated for 30 min at 37 C. The cells were then washed
with PBS, and 2 ml PBS were added to each well. Dissuccinimidylsuberate
(0.5 mM in dimethyl sulfoxide, Pierce, Rockford, IL) was
added to the cells, mixed, and incubated for 20 min at room
temperature. The reaction was stopped with 2 ml Tris, 50
mM, NaCl, 150 mM, and cells were lysed in 50
µl SDS-sample buffer. Electrophoresis was performed on a 8%
SDS-polyacrylamide gel. The gel was dried and exposed to x-ray
film.
Immunoprecipitations and Western Blotting
Human GH (Genotropin, Pharmacia) was biotinylated using
the Boeringher kit at a ratio of 1:5 molar. For immunoprecipitations,
5 x 106 cells were transfected with 10 µg of GHRfl
or GHR1-279 cDNA alone or with a combination of 5 µg of each cDNA.
Twenty four hours after transfection, cells were incubated in
starvation media for 16 h and then stimulated with either 2
µg/ml of hGH or biotinylated hGH for 5 min at 37 C. One milliliter of
normal human serum was also incubated with 2 µg biotinylated hGH.
Cell lysates were then incubated overnight at 4 C with 4 µg/ml
affinity-purified GHR-intra antibody (2) and protein A Sepharose or
with 30 µl of streptavidin beads. Supernatants (10 ml) and serum were
incubated with 30 µl of streptavidin beads. Purified proteins were
applied to a 10% polyacrylamide-SDS gel, transferred to a
nitrocellulose membrane, and probed with 5 µg/ml of the GHR antibody
mAb 263 (Biogenesis). Detection was performed with the chemiluminescent
detection system (Amersham).
Transcription Assays
293 cells were plated in six-well plates at 0.4 x
106 cells per well before being transfected with 0.1 µg
of the pcDNA1 expression vector containing the GHRfl and/or 0 to 1 µg
GHR1-279, 1.5 µg LHRE/TK-luciferase reporter gene (17), and 3 µg
pCH110 (fl-galactosidase expression vector, Pharmacia). Cells were then
incubated for 24 h in serum-free medium with or without 20 or 1
nM hGH. Cells were lyzed and luciferase and galactosidase
activities measured. Luciferase activity was normalized to the
galactosidase activity. All experiments were performed in
triplicate.
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ACKNOWLEDGMENTS |
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FOOTNOTES |
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S.L.C. is supported by a Wellcome Trust Clinician Scientist Fellowship, and S.V.L. by a grant from the YCRC. The work was supported by grants from the Clinical Endocrinology Trust, Royal Society, Northern General Hospital Research Committee, and Serono Laboratories, UK.
Received for publication April 11, 1996. Revision received December 19, 1996. Accepted for publication December 20, 1996.
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REFERENCES |
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TOPABSTRACTINTRODUCTIONRESULTSDISCUSSIONMATERIALS AND METHODSREFERENCES |
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M.-C. Lacroix, J. Guibourdenche, T. Fournier, I. Laurendeau, A. Igout, V. Goffin, J. Pantel, V. Tsatsaris, and D. Evain-Brion Stimulation of Human Trophoblast Invasion by Placental Growth Hormone Endocrinology, May 1, 2005; 146(5): 2434 - 2444. [Abstract] [Full Text] [PDF]
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G. M. Leong, S. Moverare, J. Brce, N. Doyle, K. Sjogren, K. Dahlman-Wright, J.-A. Gustafsson, K. K. Y. Ho, C. Ohlsson, and K.-C. Leung Estrogen Up-Regulates Hepatic Expression of Suppressors of Cytokine Signaling-2 and -3 in Vivo and in Vitro Endocrinology, December 1, 2004; 145(12): 5525 - 5531. [Abstract] [Full Text] [PDF]
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 K.-C. Leung, G. Johannsson, G. M. Leong, and K. K. Y. Ho Estrogen Regulation of Growth Hormone Action Endocr. Rev., October 1, 2004; 25(5): 693 - 721. [Abstract] [Full Text] [PDF]
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K. Iida, J. P. del Rincon, D.-S. Kim, E. Itoh, K. T. Coschigano, J. J. Kopchick, and M. O. Thorner Regulation of full-length and truncated growth hormone (GH) receptor by GH in tissues of lit/lit or bovine GH transgenic mice Am J Physiol Endocrinol Metab, September 1, 2004; 287(3): E566 - E573. [Abstract] [Full Text] [PDF]
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J. G. Miquet, A. I. Sotelo, A. Bartke, and D. Turyn Suppression of Growth Hormone (GH) Janus Tyrosine Kinase 2/Signal Transducer and Activator of Transcription 5 Signaling Pathway in Transgenic Mice Overexpressing Bovine GH Endocrinology, June 1, 2004; 145(6): 2824 - 2832. [Abstract] [Full Text] [PDF]
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 Y. Li, K. G. Suresh Kumar, W. Tang, V. S. Spiegelman, and S. Y. Fuchs Negative Regulation of Prolactin Receptor Stability and Signaling Mediated by SCF{beta}-TrCP E3 Ubiquitin Ligase Mol. Cell. Biol., May 1, 2004; 24(9): 4038 - 4048. [Abstract] [Full Text] [PDF]
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M. D. Lewis, M. Horan, D. S. Millar, V. Newsway, T. E. Easter, L. Fryklund, J. W. Gregory, M. Norin, C.-J. Del Valle, J. P. Lopez-Siguero, et al. A Novel Dysfunctional Growth Hormone Variant (Ile179Met) Exhibits a Decreased Ability to Activate the Extracellular Signal-Regulated Kinase Pathway J. Clin. Endocrinol. Metab., March 1, 2004; 89(3): 1068 - 1075. [Abstract] [Full Text] [PDF]
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A. Milward, L. Metherell, M. Maamra, M. J. Barahona, I. R. Wilkinson, C. Camacho-Hubner, M. O. Savage, C. M. Bidlingmaier, A. J. L. Clark, R. J. M. Ross, et al. Growth Hormone (GH) Insensitivity Syndrome due to a GH Receptor Truncated after Box1, Resulting in Isolated Failure of STAT 5 Signal Transduction J. Clin. Endocrinol. Metab., March 1, 2004; 89(3): 1259 - 1266. [Abstract] [Full Text] [PDF]
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S. R. Edmondson, S. P. Thumiger, G. A. Werther, and C. J. Wraight Epidermal Homeostasis: The Role of the Growth Hormone and Insulin-Like Growth Factor Systems Endocr. Rev., December 1, 2003; 24(6): 737 - 764. [Abstract] [Full Text] [PDF]
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 E. J. Pritham, Y. H. Zhang, C. Feschotte, and R. V. Kesseli An Ac-like Transposable Element Family With Transcriptionally Active Y-Linked Copies in the White Campion, Silene latifolia Genetics, October 1, 2003; 165(2): 799 - 807. [Abstract] [Full Text] [PDF]
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 X. Wang, K. He, M. Gerhart, J. Jiang, R. J. Paxton, R. K. Menon, R. A. Black, G. Baumann, and S. J. Frank Reduced Proteolysis of Rabbit Growth Hormone (GH) Receptor Substituted with Mouse GH Receptor Cleavage Site Mol. Endocrinol., October 1, 2003; 17(10): 1931 - 1943. [Abstract] [Full Text] [PDF]
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 K. C. Leung, N. Doyle, M. Ballesteros, K. Sjogren, C. K. W. Watts, T. H. Low, G. M. Leong, R. J. M. Ross, and K. K. Y. Ho Estrogen inhibits GH signaling by suppressing GH-induced JAK2 phosphorylation, an effect mediated by SOCS-2 PNAS, February 4, 2003; 100(3): 1016 - 1021. [Abstract] [Full Text] [PDF]
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C. V. Clevenger, P. A. Furth, S. E. Hankinson, and L. A. Schuler The Role of Prolactin in Mammary Carcinoma Endocr. Rev., February 1, 2003; 24(1): 1 - 27. [Abstract] [Full Text] [PDF]
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 X. Wang, K. He, M. Gerhart, Y. Huang, J. Jiang, R. J. Paxton, S. Yang, C. Lu, R. K. Menon, R. A. Black, et al. Metalloprotease-mediated GH Receptor Proteolysis and GHBP Shedding. DETERMINATION OF EXTRACELLULAR DOMAIN STEM REGION CLEAVAGE SITE J. Biol. Chem., December 20, 2002; 277(52): 50510 - 50519. [Abstract] [Full Text] [PDF]
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J. D. Veldhuis, M. Bidlingmaier, S. M. Anderson, W. S. Evans, Z. Wu, and C. J. Strasburger Impact of Experimental Blockade of Peripheral Growth Hormone (GH) Receptors on the Kinetics of Endogenous and Exogenous GH Removal in Healthy Women and Men J. Clin. Endocrinol. Metab., December 1, 2002; 87(12): 5737 - 5745. [Abstract] [Full Text] [PDF]
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J. Gent, P. van Kerkhof, M. Roza, G. Bu, and G. J. Strous Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis PNAS, July 23, 2002; 99(15): 9858 - 9863. [Abstract] [Full Text] [PDF]
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 F. A. Kondrashov and E. V. Koonin Origin of alternative splicing by tandem exon duplication Hum. Mol. Genet., November 1, 2001; 10(23): 2661 - 2669. [Abstract] [Full Text] [PDF]
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 H. Zarkesh-Esfahani, G. Pockley, R. A. Metcalfe, M. Bidlingmaier, Z. Wu, A. Ajami, A. P. Weetman, C. J. Strasburger, and R. J. M. Ross High-Dose Leptin Activates Human Leukocytes Via Receptor Expression on Monocytes J. Immunol., October 15, 2001; 167(8): 4593 - 4599. [Abstract] [Full Text] [PDF]
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M. Maamra, M. Bidlingmaier, M.-C. Postel-Vinay, Z. Wu, C. J. Strasburger, and R. J. M. Ross Generation of Human Soluble Leptin Receptor by Proteolytic Cleavage of Membrane-Anchored Receptors Endocrinology, October 1, 2001; 142(10): 4389 - 4393. [Abstract] [Full Text] [PDF]
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M. Bondanelli, A. Margutti, M. R. Ambrosio, L. Plaino, L. Cobellis, F. Petraglia, and E. C. degli Uberti Blood Growth Hormone-Binding Protein Levels in Premenopausal and Postmenopausal Women: Roles of Body Weight and Estrogen Levels J. Clin. Endocrinol. Metab., May 1, 2001; 86(5): 1973 - 1980. [Abstract] [Full Text]
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H. Lou and R. F. Gagel Alternative Ribonucleic Acid Processing in Endocrine Systems Endocr. Rev., April 1, 2001; 22(2): 205 - 225. [Abstract] [Full Text]
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R. J. M. Ross, K. C. Leung, M. Maamra, W. Bennett, N. Doyle, M. J. Waters, and K. K. Y. Ho Binding and Functional Studies with the Growth Hormone Receptor Antagonist, B2036-PEG (Pegvisomant), Reveal Effects of Pegylation and Evidence That It Binds to a Receptor Dimer J. Clin. Endocrinol. Metab., April 1, 2001; 86(4): 1716 - 1723. [Abstract] [Full Text]
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R. Guan, Y. Zhang, J. Jiang, C. A. Baumann, R. A. Black, G. Baumann, and S. J. Frank Phorbol Ester- and Growth Factor-Induced Growth Hormone (GH) Receptor Proteolysis and GH-Binding Protein Shedding: Relationship to GH Receptor Down-Regulation Endocrinology, March 1, 2001; 142(3): 1137 - 1147. [Abstract] [Full Text] [PDF]
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S. Fisker, K. Kristensen, A. M. Rosenfalck, S. B. Pedersen, L. Ebdrup, B. Richelsen, J. Hilsted, J. S. Christiansen, and J. O. L. Jørgensen Gene Expression of a Truncated and the Full-Length Growth Hormone (GH) Receptor in Subcutaneous Fat and Skeletal Muscle in GH-Deficient Adults: Impact of GH Treatment J. Clin. Endocrinol. Metab., February 1, 2001; 86(2): 792 - 796. [Abstract] [Full Text]
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K.-C. Leung, N. Doyle, M. Ballesteros, M. J. Waters, and K. K. Y. Ho Insulin Regulation of Human Hepatic Growth Hormone Receptors: Divergent Effects on Biosynthesis and Surface Translocation J. Clin. Endocrinol. Metab., December 1, 2000; 85(12): 4712 - 4720. [Abstract] [Full Text]
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Y. Zhang, J. Jiang, R. A. Black, G. Baumann, and S. J. Frank Tumor Necrosis Factor-{{alpha}} Converting Enzyme (TACE) Is a Growth Hormone Binding Protein (GHBP) Sheddase: The Metalloprotease TACE/ADAM-17 Is Critical for (PMA-Induced) GH Receptor Proteolysis and GHBP Generation Endocrinology, December 1, 2000; 141(12): 4342 - 4348. [Abstract] [Full Text] [PDF]
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S. H. Zarkesh-Esfahani, O. Kolstad, R. A. Metcalfe, P. F. Watson, S. Von Laue, S. Walters, A. Revhaug, A. P. Weetman, and R. J. M. Ross High-Dose Growth Hormone Does Not Affect Proinflammatory Cytokine (Tumor Necrosis Factor-{alpha}, Interleukin-6, and Interferon-{gamma}) Release from Activated Peripheral Blood Mononuclear Cells or after Minimal to Moderate Surgical Stress J. Clin. Endocrinol. Metab., September 1, 2000; 85(9): 3383 - 3390. [Abstract] [Full Text]
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M. Ballesteros, K.-C. Leung, R. J. M. Ross, T. P. Iismaa, and K. K. Y. Ho Distribution and Abundance of Messenger Ribonucleic Acid for Growth Hormone Receptor Isoforms in Human Tissues J. Clin. Endocrinol. Metab., August 1, 2000; 85(8): 2865 - 2871. [Abstract] [Full Text]
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 F. Beuschlein, C. J. Strasburger, V. Siegerstetter, D. Moradpour, P. Lichter, M. Bidlingmaier, H. E. Blum, and M. Reincke Acromegaly Caused by Secretion of Growth Hormone by a Non-Hodgkin's Lymphoma N. Engl. J. Med., June 22, 2000; 342(25): 1871 - 1876. [Full Text] [PDF]
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 A. E. Green, J. S. O'neil, K. F. Swan, R. P. Bohm Jr., M. S. Ratterree, and M. C. Henson Leptin Receptor Transcripts Are Constitutively Expressed in Placenta and Adipose Tissue with Advancing Baboon Pregnancy Experimental Biology and Medicine, April 1, 2000; 223(4): 362 - 366. [Abstract] [Full Text] [PDF]
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T. Amit, M. B. H. Youdim, and Z.'e. Hochberg Does Serum Growth Hormone (GH) Binding Protein Reflect Human GH Receptor Function? J. Clin. Endocrinol. Metab., March 1, 2000; 85(3): 927 - 932. [Abstract] [Full Text]
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E. van Garderen, H. J. A. van der Poel, J. F. Swennenhuis, E. H. J. Wissink, G. R. Rutteman, E. Hellmén, J. A. Mol, and J. A. Schalken Expression and Molecular Characterization of the Growth Hormone Receptor in Canine Mammary Tissue and Mammary Tumors Endocrinology, December 1, 1999; 140(12): 5907 - 5914. [Abstract] [Full Text]
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 M. J. Renzi, L. Feiner, A. M. Koppel, and J. A. Raper A Dominant Negative Receptor for Specific Secreted Semaphorins Is Generated by Deleting an Extracellular Domain from Neuropilin-1 J. Neurosci., September 15, 1999; 19(18): 7870 - 7880. [Abstract] [Full Text] [PDF]
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Y. Shuto, T. Nakano, N. Sanno, H. Domoto, H. Sugihara, and I. Wakabayashi Reduced Growth Hormone Receptor Messenger Ribonucleic Acid in an Aged Man with Chronic Malnutrition and Growth Hormone Resistance J. Clin. Endocrinol. Metab., July 1, 1999; 84(7): 2320 - 2323. [Abstract] [Full Text]
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N. D. Quinton, R. F. Smith, P. E. Clayton, M. S. Gill, S. Shalet, S. K. Justice, S. A. Simon, S. Walters, M.-C. Postel-Vinay, A. I. F. Blakemore, et al. Leptin Binding Activity Changes with Age: The Link between Leptin and Puberty J. Clin. Endocrinol. Metab., July 1, 1999; 84(7): 2336 - 2341. [Abstract] [Full Text]
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M. Maamra, J. Finidori, S. Von Laue, S. Simon, S. Justice, J. Webster, S. Dower, and R. Ross Studies with a Growth Hormone Antagonist and Dual-fluorescent Confocal Microscopy Demonstrate that the Full-length Human Growth Hormone Receptor, but Not the Truncated Isoform, Is Very Rapidly Internalized Independent of Jak2-Stat5 Signaling J. Biol. Chem., May 21, 1999; 274(21): 14791 - 14798. [Abstract] [Full Text] [PDF]
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K. Iida, Y. Takahashi, H. Kaji, M. O. Takahashi, Y. Okimura, O. Nose, H. Abe, and K. Chihara Functional Characterization of Truncated Growth Hormone (GH) Receptor-(1-277) Causing Partial GH Insensitivity Syndrome with High GH-Binding Protein J. Clin. Endocrinol. Metab., March 1, 1999; 84(3): 1011 - 1016. [Abstract] [Full Text]
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T. Amit, O. Bar-Am, F. Dastot, M. B. H. Youdim, S. Amselem, and Z.'e. Hochberg The Human Growth Hormone (GH) Receptor and Its Truncated Isoform: Sulfhydryl Group Inactivation in the Study of Receptor Internalization and GH-Binding Protein Generation Endocrinology, January 1, 1999; 140(1): 266 - 272. [Abstract] [Full Text]
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J. Wojcik, M. A. Berg, N. Esposito, M. E. Geffner, N. Sakati, E. O. Reiter, S. Dower, U. Francke, M.-C. Postel-Vinay, and J. Finidori Four Contiguous Amino Acid Substitutions, Identified in Patients with Laron Syndrome, Differently Affect the Binding Affinity and Intracellular Trafficking of the Growth Hormone Receptor J. Clin. Endocrinol. Metab., December 1, 1998; 83(12): 4481 - 4489. [Abstract] [Full Text]
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A. Edens and F. Talamantes Alternative Processing of Growth Hormone Receptor Transcripts Endocr. Rev., October 1, 1998; 19(5): 559 - 582. [Abstract] [Full Text]
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L. Grasso, M. Huang, C. D. Sullivan, C. J. Messler, M. B. Kiser, C. R. Dragwa, K. J. Holroyd, J.-C. Renauld, R. C. Levitt, and N. C. Nicolaides Molecular Analysis of Human Interleukin-9 Receptor Transcripts in Peripheral Blood Mononuclear Cells. IDENTIFICATION OF A SPLICE VARIANT ENCODING FOR A NONFUNCTIONAL CELL SURFACE RECEPTOR J. Biol. Chem., September 11, 1998; 273(37): 24016 - 24024. [Abstract] [Full Text] [PDF]
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A. L. Rosenbloom, J. Guevara-Aguirre, M. A. Berg, and U. Francke Stature in Ecuadorians Heterozygous for Growth Hormone Receptor Gene E180 Splice Mutation Does Not Differ From That of Homozygous Normal Relatives J. Clin. Endocrinol. Metab., July 1, 1998; 83(7): 2373 - 2375. [Abstract] [Full Text]
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X. Y. Shen, R. I. G. Holt, J. P. Miell, S. Justice, B. Portmann, M.-C. Postel-Vinay, and R. J. M. Ross Cirrhotic Liver Expresses Low Levels of the Full-Length and Truncated Growth Hormone Receptors J. Clin. Endocrinol. Metab., July 1, 1998; 83(7): 2532 - 2538. [Abstract] [Full Text]
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R. Govers, P. van Kerkhof, A. L. Schwartz, and G. J. Strous Di-leucine-mediated Internalization of Ligand by a Truncated Growth Hormone Receptor Is Independent of the Ubiquitin Conjugation System J. Biol. Chem., June 26, 1998; 273(26): 16426 - 16433. [Abstract] [Full Text] [PDF]
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J. Alele, J. Jiang, J. F. Goldsmith, X. Yang, H. G. Maheshwari, R. A. Black, G. Baumann, and S. J. Frank Blockade of Growth Hormone Receptor Shedding by a Metalloprotease Inhibitor Endocrinology, April 1, 1998; 139(4): 1927 - 1935. [Abstract] [Full Text] [PDF]
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K. Iida, Y. Takahashi, H. Kaji, O. Nose, Y. Okimura, H. Abe, and K. Chihara Growth Hormone (GH) Insensitivity Syndrome with High Serum GH-Binding Protein Levels Caused by a Heterozygous Splice Site Mutation of the GH Receptor Gene Producing a Lack of Intracellular Domain J. Clin. Endocrinol. Metab., February 1, 1998; 83(2): 531 - 537. [Abstract] [Full Text]
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H. Kaji, O. Nose, H. Tajiri, Y. Takahashi, K. Iida, T. Takahashi, Y. Okimura, H. Abe, and K. Chihara Novel Compound Heterozygous Mutations of Growth Hormone (GH) Receptor Gene in a Patient with GH Insensitivity Syndrome J. Clin. Endocrinol. Metab., November 1, 1997; 82(11): 3705 - 3709. [Abstract] [Full Text] [PDF]
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T. Amit, T. Bergman, F. Dastot, M. B. H. Youdim, S. Amselem, and Z.'e. Hochberg A Membrane-Fixed, Truncated Isoform of the Human Growth Hormone Receptor J. Clin. Endocrinol. Metab., November 1, 1997; 82(11): 3813 - 3817. [Abstract] [Full Text] [PDF]
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J. J. Berlanga, J. P. Garcia-Ruiz, M. Perrot-Applanat, P. A. Kelly, and M. Edery The Short Form of The Prolactin (PRL) Receptor Silences PRL Induction of the {beta}-Casein Gene Promoter Mol. Endocrinol., September 1, 1997; 11(10): 1449 - 1457. [Abstract] [Full Text]
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J.-F. Martini, A. Pezet, C. Y. Guezennec, M. Edery, M.-C. Postel-Vinay, and P. A. Kelly Monkey Growth Hormone (GH) Receptor Gene Expression. EVIDENCE FOR TWO MECHANISMS FOR THE GENERATION OF THE GH BINDING PROTEIN J. Biol. Chem., July 25, 1997; 272(30): 18951 - 18958. [Abstract] [Full Text] [PDF]
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J. E. Dinchuk, N. L. Henderson, T. C. Burn, R. Huber, S. P. Ho, J. Link, K. T O'Neil, R. J. Focht, M. S. Scully, J. M. Hollis, et al. Aspartyl beta -Hydroxylase (Asph) and an Evolutionarily Conserved Isoform of Asph Missing the Catalytic Domain Share Exons with Junctin J. Biol. Chem., December 8, 2000; 275(50): 39543 - 39554. [Abstract] [Full Text] [PDF]
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Y. Zhang, R. Guan, J. Jiang, J. J. Kopchick, R. A. Black, G. Baumann, and S. J. Frank Growth Hormone (GH)-induced Dimerization Inhibits Phorbol Ester-stimulated GH Receptor Proteolysis J. Biol. Chem., June 29, 2001; 276(27): 24565 - 24573. [Abstract] [Full Text] [PDF]
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