Gene/Protein Disease Symptom Drug Enzyme Compound
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Nine children with growth retardation due to chronic renal failure were treated with recombinant human growth hormone (rhGH) for 12-36 months. Results demonstrated a significant increase in height velocity at each 12-month interval compared with that achieved during the year prior to treatment. However, the increase in bone age was no greater than the increase in chronological age during the period of treatment. The mean calculated creatinine clearance did not decrease significantly during the 36 months of treatment; however, two patients required institution of dialysis at 18 and 30 months following initiation of rhGH treatment. There was no exacerbation of the glucose intolerance of uraemia following treatment. Currently, 6 of 7 patients who have been treated for more than 24 months have achieved sufficient acceleration in height velocity to attain an SDS of less than -2.00 and are above the 5th centile for chronological age on the growth curve. These updated data indicate that rhGH treatment of growth retarded children with chronic renal failure continues to result in accelerated height velocity during the second and third year of treatment, and demonstrate the potential for such children to achieve normal stature (+/- 2 SD) for chronological age despite the continued presence of chronic renal failure.
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PMID:Recombinant human growth hormone treatment of children with chronic renal failure: update 1990. 226 Apr 57

We have studied the growth of 144 children after treatment of brain tumours distant from the hypothalamo-pituitary axis. All had cranial irradiation and 87 spinal irradiation. In 56 patients observed without intervention for 3 years, height SDS in the cranial (CR) group (n = 20) declined from 0.02 to -0.44 and in the craniospinal (CS) group (n = 36) from -0.28 to -1.11. Failure of spinal growth had a marked effect in the CS group. The onset of puberty was slightly but not significantly advanced; median ages at onset of puberty were 10.3 years in girls and 12.1 years in boys. Of the total group 86.4% had clinical and biochemical evidence of growth hormone insufficiency. Fifty-two children, 33 (28 CS; 5 CR) of whom were prepubertal, received biosynthetic human growth hormone, in a dose of 15 mU/m2/week by daily injection for a period of one year. Height velocity SDS increased significantly in both groups from -2.74 to +1.90 (CS) and from -1.0 to +4.26 (CR). Spinal response to GH treatment was restricted in the craniospinal group.
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PMID:Growth and growth hormone secretion in children following treatment of brain tumours with radiotherapy. 226 67

It has been suggested that the functional diversity of growth hormone (GH) is related to its molecular complexity. Here we report a characterization of charge and mass variants of chicken growth hormone (cGH) through a variety of electrophoretic systems [nondenaturing (ND-PAGE), denaturing (SDS-PAGE), under reducing and nonreducing conditions, isoelectrofocusing (IEF), and bidimensional electrophoresis] followed by Western blot and immunostaining with a specific antibody directed against pure cGH. We also report the biological properties of two charge variants on two homologous assays. The studies were carried out with purified cGH and with fresh chicken pituitary extracts. Three charge variants were obtained by ND-PAGE (Rf = 0.23, 0.30, and 0.35), which showed the same molecular weight (26 kDa), while in IEF eight isoforms were observed, the most conspicuous being those with pI = 6.86, 7.5, 7.9, 8.05, and 8.18. In SDS-PAGE under reducing conditions four immunoreactive bands were observed: the monomer (26 kDa), a dimer (52 kDa), a fragment (16 kDa), and a minor band at 22 kDa. Higher MW variants were found under nonreducing conditions. Bidimensional analysis also showed several charge variants for the monomer and the dimer. Bioactivity of two charge variants (0.23 and 0.3) was evaluated with a lipolytic and an antilipolytic assay on chicken adipose tissue explants. It was shown that variant 0.23 was mainly lipolytic, in a dose-dependent response, but lacked antilipolytic effect. On the other hand, variant 0.30 did not show lipolytic effect but presented a clear antilipolytic activity.
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PMID:Molecular isoforms of chicken growth hormone (cGH): different bioactivities of cGH charge variants. 227 80

The release of growth hormone (GH) during the 120 min following a bolus venous injection of 1-44 GH-releasing hormone (GHRH) 2 micrograms/kg was studied in 52 prepubertal children aged 8.4 +/- 2.1 years, having a nonfamilial growth deficiency of prenatal onset (-3.26 +/- 1.13 SDS at birth, -3.22 +/- 0.88 SDS at the time of study) and a normal response to conventional GH stimulation tests. GH release reached a peak level of 96.1 +/- 60.2 microU/ml, being significantly higher than that found in 68 non-GH-deficient very short children whose growth failure had a postnatal onset, and not significantly correlated with the response to conventional tests. 26 of the 52 intrauterine growth retardation (IUGR) patients were re-tested with GHRH in similar conditions after 6-12 months of daily subcutaneous injections of GH and 2 days without. They reached at the second test a peak plasma GH level of 91.7 +/- 56.1 microU/ml, not different from their response to the first test. These data could be taken into consideration for long-term studies of the clinical effects of GH in IUGR children with persisting severe growth deficiency.
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PMID:Growth hormone response to a bolus injection of 1-44 growth-hormone-releasing hormone in very short children with intrauterine onset of growth failure. 227 7

Highly purified growth hormone (GH) has been isolated from Atlantic salmon (Salmo salar) pituitaries by extraction with acid acetone, acidic precipitation, and reversed-phase high-performance liquid chromatography (HPLC). The yield was 2.5 mg/g wet tissue. The Atlantic salmon GH (sGH) emerged as a single symmetrical peak after HPLC on a reverse phase C18 column. SDS-gel electrophoresis revealed only one band with an estimated molecular weight of 23,000. Atlantic sGH showed a uniform molecular weight, but two-dimensional (2D) gel electrophoresis of the purified sGH revealed charge heterogeneity with pI's ranging from 6.5 to 8.2. Treatment of the purified sGH with alkaline phosphatase concentrated these different forms into a single more alkaline position (pI 8.2) indicating removal of acidic groups. These results were documented using both silver- and immunostaining of the 2D SDS gels. The purified sGH was phosphorylated in vitro by a calmodulin-dependent protein kinase. Phosphorylation of sGH may be a post-translational modification resulting in several molecular forms with variable acidity. Analysis of the amino acid composition of Atlantic sGH revealed homology with GHs isolated from other teleost species and the amino-terminal sequence showed only three different amino acids within the first 25 residues compared to GH isolated from chum salmon (Oncorhynchus keta) and coho salmon (Oncorhynchus kisutch) pituitaries. Atlantic sGH had a methionine as the amino-terminal residue. Antibodies against chum sGH cross-reacted with Atlantic sGH. Antibodies against either Atlantic or chinook (Oncorhynchus tschawytscha) salmon prolactin or human GH did not cross-react with Atlantic sGH. Atlantic sGH was shown to have a slight growth-promoting activity in the rat tibia assay.
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PMID:Purification and characterization of Atlantic salmon growth hormone and evidence for charge heterogeneity. 228 75

Mid-to-late gestation rat placenta synthesizes a number of proteins related to prolactin, including rat placental lactogen II (rPL-II), rat prolactin-like protein A (rPLP-A) and rat prolactin-like protein B (rPLP-B). This study identifies a new family of proteins synthesized and secreted by gestation day 15 placental explants which exhibit amino acid homology to growth hormone precursors from several species. Placental explant medium was fractionated by ammonium sulfate precipitation and analyzed by two-dimensional SDS-polyacrylamide gel electrophoresis to isolate four distinct proteins with Mr values of 28,000, 23,000, 25,000 and 30,000 and pI values of 5.7, 5.7, 5.4 and 5.3, respectively. These proteins represent a major fraction of secretory proteins with Mr in the 20,000 to 30,000 range. Immunoblot analysis showed that none of the four proteins crossreacted with antipeptide antisera against rPL-II, rPLP-A, or rPLP-B. These proteins were electrophoretically transferred from two-dimensional SDS-polyacrylamide gels onto an Immobilon PVDF membrane and N-terminal amino acid microsequencing carried out with a gas phase sequencer. N-terminal sequences of 45, 37, 37 and 32 amino acid residues were identified for proteins 1, 2, 3 and 4, respectively. The four proteins exhibit 76% to 97% homology. Computer analysis further revealed a 28% identity in a 32 amino acid overlap which begins at residue 14 of the 28,000 Mr protein (protein 1) and at residue 31 of growth hormone precursors of rat, mouse and human. The 32 amino acid overlap is 78% homologous if conservative amino acid replacements are included.
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PMID:Identification of a novel family of growth hormone-related proteins secreted by rat placenta. 235 Nov 17

Protein formation in the anterior pituitary was investigated in vitro in thyroidectomized (TX) and/or adrenalectomited (AX) rats treated with a single dose of 100 micrograms/100 g of 3,5,3'-triiodothyronine (T3) and/or with a single dose of 10 micrograms/100 g of dexamethazone (DEX) 12 h before sacrifice. Male Wistar rats of a specific pathogen free colony 6 weeks after TX and/or AX receiving 1% calcium chloride and/or saline after surgery were used in the experiments. Non-pooled anterior pituitaries (in acellular condition) complemented with all essential amino acids, CPK, creatine phosphate in a HEPES buffer containing potassium acetate, magnesium acetate and dithiothreitol, were incubated with 35S-methionine at 28 degrees C for 10 or 40 min. The reaction was stopped by EDTA followed by RNAase plus DNAase treatment and the samples were analyzed for total 35S-methionine incorporation or by SDS 12.5% polyacrylamide gel slab electrophoresis (PAGE). As compared to intact rats (100%), TX and/or AX caused a significant diminution of the total 35S-methionine incorporation into protein ranging from 33% to 68% that may be easily restored to 107% by T3 plus DEX treatment. PAGE analysis reflects an appreciable relation between T3 administration and 21.5 kDa protein (growth hormone) formation in the anterior pituitary. In addition, the effect 5,5'-diphenylhydantoine (DPH) on 35S-methionine incorporation in relation to T3 nuclear specific binding was investigated. The data suggest that the decreased protein synthesis de novo is due to a significant diminution of T3 specific binding to nuclear receptors in the anterior pituitary.
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PMID:Anterior pituitary: triiodothyronine and/or dexamethasone induced changes in protein formation in thyroidectomized and/or adrenalectomized rats. 236 68

Contamination of medicines produced in E. coli by recombinant DNA methodology with host-cell proteins is considered a potential problem with this type of method. In this report techniques for the detection of trace quantities of host-cell proteins in SDS-gel electrophoretograms were examined. Detection of E. coli proteins by immunoblotting, using antisera raised in rabbits to lysates of E. coli, was compared with detection using the ultrasensitive silver stain. Silver staining detected a larger number of E. coli proteins in a one-dimensional electrophoresis system than did immunoblotting. Proteins that were markedly antigenic in the rabbit were detected at a greater sensitivity by the immunoblotting approach. Both techniques detected contaminant proteins in a preparation of methionyl human growth hormone produced in E. coli known to be contaminated with host-cell proteins. No contaminating proteins were seen by either technique in more rigorously purified preparations of growth hormone. A combination of these two approaches would provide useful evidence of purity of medicines produced by recombinant DNA technology, and is potentially applicable to a wide range of host-vector systems.
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PMID:Detection of host-derived contaminants in products of recombinant DNA technology in E. coli: a comparison of silver-staining and immunoblotting. 241 2

This report describes the purification of human growth hormone from crude pituitary extract and lysate of recombinant E. coli by an immunoadsorbent purification with monoclonal antibody coupled to solid phase. By a single-immunoaffinity chromatography step pure hGH can be obtained from either origin as revealed by SDS-PAGE followed by silver staining or immunoblotting. An additional ion-exchange chromatography step results in homogeneous 22 kDa hGH preparations. Furthermore, this method may be used for isolation of a pituitary hGH variant which has higher binding affinity for this monoclonal antibody than the major 22 kDa form. This study clearly illustrates the potential of monoclonal antibody immunoadsorbents for purification of different molecular forms of hGH.
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PMID:Purification of pituitary and biosynthetic human growth hormone using monoclonal antibody immunoadsorbent. 242 99

Recombinant DNA derived human growth hormone (rhGH), Genotropin, has been expressed in E. coli cells as a pre-hormone, where the heat stable enterotoxin II signal peptide (STII) was linked to hGH to get secretion of the hormone to the periplasmatic space. The pre-hormone was efficiently cleaved during secretion, by an endogenous signal peptidase generating the correct N-terminal (Phe) end as shown by protein sequence analysis. The purity of rhGH was studied by SDS-PAGE, in combination with laser densitometry and HI-HPLC. These techniques showed that the level of modified rhGH forms, e.g. aggregated and proteolytically cleaved (16 and 6 kDa) in the preparation was in the 0.5-1% range. Furthermore, evidence that the correct disulphide bonds (Cys53-Cys165; Cys182-Cys189) were formed in rhGH during secretion has been shown by a combination of tryptic fingerprint and amino acid analysis. CD-spectroscopic analysis suggested an identical secondary structure to that of pituitary derived human growth hormone (pit-hGH). Isoelectric focusing revealed an isoelectric point (pI) for rhGH of 5.0 similar to pit-hGH and in excellent agreement with the theoretical value 5.1, based on the primary sequence. Finally, an apparent molecular weight of 22,000 was obtained for rhGH, by SDS-PAGE. All these physico-chemical studies suggest that rhGH is structurally identical to pit-hGH, somatotropin.
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PMID:Characterisation of a secreted form of recombinant derived human growth hormone, expressed in Escherichia coli cells. 248 18


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