Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A total of 17 patients (14 boys, 3 girls) with poor growth due to idiopathic growth hormone deficiency (IGHD) were treated for 12 months with recombinant human growth hormone (rhGH; Saizen), 0.5 IU/kg body weight per week administered by subcutaneous injection on a daily basis. Therapy significantly increased growth velocity (GV) from 4.0 +/- 1.5 to 10.1 +/- 2.4 cm/year (p < 0.001). Correspondingly, GV standard deviation score (GV SDS) for chronological age (CA) increased from -2.7 +/- 1.6 to +4.5 +/- 2.8; GV SDS for bone age (BA) increased from -4.0 +/- 2.0 to +3.6 +/- 3.3; and patient height SDS-CA increased from -3.5 +/- 1.1 to -2.4 +/- 0.7. Changes in these parameters were significant at p < 0.001. During the course of the study, mean plasma IGF-1 levels rose significantly from 0.3 +/- 0.2 IU/ml to 1.3 +/- 1.2 IU/ml (p < 0.01). BA maturation proceeded at approximately 1 year per treatment year. Therapy was well tolerated. Anti-hGH antibodies were seen in only 1 patient at a low concentration, and did not appear to affect GV. This study demonstrates that rhGH is safe and efficacious when used to increase height in patients with IGHD.
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PMID:Spanish multicenter clinical trial of recombinant growth hormone produced in mammalian cells for treatment of growth failure due to idiopathic growth hormone deficiency. Spanish Multicenter Study Group. 149 Jun 64

Children with congenital CRF lose height potential mainly during two distinct growth periods; infancy and puberty. The onset of puberty is late, the pubertal growth spurt starts from a very low rate of growth velocity, and peak height velocity is lower than normal although the absolute increment of height velocity is comparable to the increment in normal children. Furthermore, the duration of pubertal growth spurt is reduced in CRF. During infancy and early childhood, malnutrition, electrolyte disturbances and metabolic acidosis are the main contributing factors for reduced growth, whereas hormonal disturbances are responsible for growth impairment during puberty. There is evidence for resistance to growth hormone in CRF, which starts in early childhood and persists until the end of puberty. Growth hormone secretion is normal in CRF, but GH half-life is prolonged. The binding activity of the stable growth hormone binding protein is reduced, which points to a low receptor expression in the liver. Hepatic IGF-I production is diminished. However, the serum concentration of IGF binding proteins (IGFBP) is increased due to reduced renal filtration of low molecular weight subunits of IGFBP. Mainly, the accumulation of IGFBP-3 leads to increased IGF-binding capacity of the uraemic serum. Both, reduced IGF-I production and increased binding of IGF to IGFBP-3 result in decreased IGF bioactivity. During infancy, loss of growth potential can be prevented by adequate nutrition. Later in life, catch-up growth cannot be induced by nutritional intervention or dialysis. Renal transplantation allows catch-up growth in only a small percentage of patients. Treatment with one IU rhGH/kg/week improves growth velocity and growth in all stages of renal disease. The mean increment of height in prepubertal children is +1.5 SDS within two treatment years. The effect of rhGH during puberty as well as the effect on final height remain to be determined.
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PMID:Growth failure in renal disease. 152 58

The effect on growth of long-term treatment with prednisolone was studied in 12 patients with steroid-sensitive nephrotic syndrome. Our patient's heights were found between the 10th and 25th percentile both at the first and last height measurement. There was no statistical difference between the first and last height standard deviation score (Ht SDS) (p greater than 0.05). When compared with chronological age, growth velocity (GV), GV SDS and bone age were found low but within the normal range for this age group. There was not any correlation between the last Ht SDS and relapse number, total doses and duration of daily and alternate-day steroid therapy (p greater than 0.05). Growth hormone (GH) responses to pharmacological stimuli were obtained as severe deficiency in 10 patients, partial deficiency in 1 patient and normal level in 1. There was statistical difference between the pulse number of the overnight GH profile of the patients and control group (p less than 0.05). But no statistical difference was found between GH pulse amplitude and GH concentration in patients and control group (p greater than 0.05).
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PMID:Effect of corticosteroids on growth in children with steroid-sensitive nephrotic syndrome. 160 74

The efficacy and safety of a 12-month treatment with recombinant human growth hormone from mammalian cells (r-hGH, Saizen) in growth hormone neurosecretory dysfunction (GHND) are evaluated in this study. r-hGH was administered subcutaneously, at a dosage of 0.5 IU/kg/week divided into 6 equal daily doses. A total of 16 (12 M and 4 F) poorly growing patients, height -2.3 SD or more below the mean for chronological age and sex, were included in the study. r-hGH therapy significantly increased the growth velocity; from 3.57 +/- 0.85 cm/year, before therapy, to 7.09 +/- 2.29 cm/year after 12 months (p less than 0.001). Patients' height SD score rose from -3.40 +/- 0.84 SDS to -2.98 +/- 0.69 SDS (p less than 0.01). Somatomedin C increased significantly from a baseline value of 0.59 +/- 0.32 U/ml to 1.26 +/- 0.66 U/ml after therapy (p less than 0.01). Finally, r-hGH therapy improved the pretreatment adult height prediction; from an initial prognosis of -2.66 +/- 0.79 SDS to -2.17 +/- 0.81 SDS after treatment (p less than 0.01). No side effects or adverse reactions were observed during treatment. Anti-r-hGH antibody formation was not found in any of the patients included in the study.
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PMID:Multicenter clinical trial to evaluate the therapeutic use of recombinant growth hormone from mammalian cells in the treatment of growth hormone neurosecretory dysfunction. 191 48

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

17 prepubertal children (12 male, 5 female) with growth hormone deficiency (GHD) were treated with a total of 12 IU/m2/week biosynthetic human growth hormone for at least three years. Growth hormone was administered daily by the subcutaneous route. Growth velocity (GV) increased from -2.75 SDS +/- 1.06 (3.58 cm +/- 0.87) to +2.91 SDS +/- 1.73 (8.6 +/- 1.3 cm) after one year of treatment. GV decreased subsequently, but remained above the pretherapeutic values. Height for chronological age increased from -2.68 SDS +/- 0.44 (pretreatment value) to -2.22 SDS +/- 0.49 SDS after one year and to -1.67 +/- 0.6 SDS after 3 years of GH therapy. Analysis of the height of each individual patient after each of the three years of treatment shows a positive correlation to the pretreatment height. Our data stress the need for early diagnosis and treatment of GHD patients because GV remains elevated for three years under therapy with 12 IU GH/m2/week in this group of GHD patients. This results in a height gain in the second and third year of treatment after catch up growth in the first year of therapy. Nevertheless, pretreatment height seems to be an important factor influencing the therapeutic results of GH administration in the individual GHD patient, stressing the need for improving the treatment schedule in patients with the most severe growth retardation.
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PMID:[Treatment of hypophyseal dwarfism with biosynthetic growth hormone]. 262 78

Growth hormone was purified from cod pituitary extract by a simple two-step procedure involving gel filtration and reversed-phase high-performance liquid chromatography (rpHPLC). At each stage of purification, fractions were monitored by rpHPLC, SDS-polyacrylamide gel electrophoresis, and immunoblotting using anti-chum salmon growth hormone (GH) antiserum. The yield of purified hormone was 1.3 mg/g pituitary. Cod GH was found to exist in two monomeric forms (Mr = 20K and 22K) and dimeric forms (Mr = 40K and 42K). The two monomeric forms have a pI of 5.8, an identical amino acid composition, histidine as the N-terminal residue, and an identical lysyl endopeptidase peptide map. Staining with concanavalin A was observed on the 20K component only, but analysis for total reducing sugar did not confirm these results. Cod GH was found to be a potent stimulator of growth in juvenile rainbow trout which received intraperitoneal injections of the hormone. The partial amino acid sequence has been determined.
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PMID:Isolation and characterization of growth hormone from Atlantic cod (Gadus morhua). 270 85

Growth hormone (GH) was extracted under alkaline conditions (pH 10) from pituitary glands (6.3 g) of bonito (Katsuwonus pelamis), and subsequently purified by gel filtration, ion exchange chromatography, and reversed-phase HPLC. The GH was monitored by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and by immunoblotting with yellowtail GH antiserum at each step of purification. GH activity was determined by an in vivo bioassay. The yield of this hormone was 4.8 mg/g wet tissue. Intraperitoneal injection of bonito GH at doses of 0.1 and 1 micrograms/g body wt at 7-day intervals resulted in a significant increase in body weight and length of juvenile rainbow trout. Bonito GH antiserum exhibited both species and hormone specificity in radioimmunoassay. However, the bonito GH antiserum as well as yellowtail GH antiserum exhibited hormone specificity but not species specificity in immunoblotting. A molecular weight of 21,000 and an isoelectric point of 7.0 for bonito GH were estimated by SDS-PAGE and gel electrofocusing, respectively. The complete amino acid sequence of 185 residues was determined by sequencing fragment peptides prepared by chemical and enzymatic cleavages. Sequence comparison of bonito GH with other GHs revealed that there is a significant deletion in the middle of the molecule.
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PMID:Isolation and characterization of growth hormone from a marine fish, bonito (Katsuwonus pelamis). 324 82

Growth hormone (GH) secretion, in mammary tissue from transgenic mice, containing a chimeric gene composed of the regulatory region of whey acidic protein gene and the structural region of GH gene, was compared to casein secretion. GH was expressed in milk and for a small percentage (1:1000) in blood as revealed by SDS-polyacrylamide gel electrophoresis and radioimmunoassay. As attested by immunofluorescence and immunogold electron microscopy, caseins and GH followed the same secretory pathway. However, contrary to caseins, which are essentially in micellar form, GH was detected in a nonaggregated form in secretory vesicles and in the lumen of the acini. Newly synthesized caseins and GH were carried simultaneously, mainly to the lumen of the acini, but also to the base of the cell. Secretion of newly synthesized proteins was increased by prolactin (PRL). As shown by immunoblotting, the proportion of GH versus other proteins, secreted in the presence of PRL was not modified, suggesting that GH secretion is subjected to the same hormonal regulation by PRL as other milk proteins. These results show that, in lactating mammary epithelial cells from transgenic mice, a recombinant GH and the caseins are carried simultaneously to the lumen and suggest that secretion of both proteins is increased by PRL during the same time course. Transport of these newly synthesized proteins occurs also to the base of the cell.
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PMID:Intracellular routing and release of caseins and growth hormone produced into milk from transgenic mice. 749 24

Growth hormone (GH) plays a central role in regulating growth and intermediary metabolism in vertebrates, although the mechanisms by which GH initiates these actions are largely unknown. The GH receptor, a member of the cytokine receptor superfamily, does not demonstrate homology with any known tyrosine kinases. However, addition of GH to cells in vitro has been shown to stimulate tyrosine phosphorylation of various intracellular proteins including mitogen-activated protein kinases (MAP kinases) and the newly described Janus kinase, JAK2. Subsequent steps in GH-mediated signal transduction have not been delineated. In the present study, we have examined early events in GH action in vivo. Hypophysectomized juvenile male rats were treated with GH for 15, 30, or 60 min. Rat liver whole cell and nuclear extracts were prepared and analyzed via SDS-polyacrylamide gel electrophoresis and Western blotting techniques. GH rapidly stimulated the tyrosine phosphorylation of at least 8 nuclear proteins of 205, 91, 83, 80, 65, 53, 44, and 42 kDa, and caused the dephosphorylation of a single approximately 149-kDa protein. Using specific antibodies, we have identified three of these nuclear phosphoproteins as 42- and 44-kDa MAP kinases, and as STAT91, a 91-kDa component of the interferon-stimulated gene factor-3 protein complex. One consequence of the activation of STAT91 in the nucleus is the appearance of GH-stimulated DNA binding activity, as assessed by gel-mobility shift assay using an oligonucleotide containing a c-sis-inducible element from the c-fos promoter. These results show that nuclear protein tyrosine phosphorylation is a prominent early event in GH action in vivo and demonstrate a link between GH-stimulated signal transduction and target gene expression.
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PMID:Rapid changes in nuclear protein tyrosine phosphorylation after growth hormone treatment in vivo. Identification of phosphorylated mitogen-activated protein kinase and STAT91. 751 Jun 76


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