scholarly journals Molecular and cellular actions of a structural domain of human growth hormone (AOD9401) on lipid metabolism in Zucker fatty rats

2000 ◽  
Vol 25 (3) ◽  
pp. 287-298 ◽  
Author(s):  
FM Ng ◽  
WJ Jiang ◽  
R Gianello ◽  
S Pitt ◽  
P Roupas
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Chronic Treatment ◽  
Solid Phase ◽  
Human Growth ◽  
The Body ◽  
Laboratory Animals ◽  
Zucker Rats ◽  
Structural Domain ◽  
Average Cell

A lipolytic domain (AOD9401) of human growth hormone (hGH) which resides in the carboxyl terminus of the molecule and contains the amino acid residues 177-191, has been synthesized using solid-phase peptide synthesis techniques. AOD9401 stimulated hormone-sensitive lipase and inhibited acetyl coenzyme A carboxylase (acetyl CoA carboxylase) in isolated rat adipose tissues, in a similar manner to the actions of the intact hGH molecule. The synthetic lipolytic domain mimicked the effect of the intact growth hormone on diacylglycerol release in adipocytes. Chronic treatment of obese Zucker rats with AOD9401 for 20 days reduced the body weight gain of the animals, and the average cell size of the adipocytes of the treated animals decreased from 110 to 80 microm in diameter. Unlike hGH, synthetic AOD9401 did not induce insulin resistance or glucose intolerance in the laboratory animals after chronic treatment. The results suggest that AOD9401 has the potential to be developed into a therapeutic agent for the control of obesity.

scholarly journals In Vivo Bioassay of Recombinant Human Growth Hormone Synthesized inB. moriPupae

2010 ◽  
Vol 2010 ◽  
pp. 1-6 ◽  
Author(s):  
Hanglian Lan ◽  
Zuoming Nie ◽  
Yue Liu ◽  
Zhengbing Lv ◽  
Yingshuo Liu ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Recombinant Human Growth Hormone ◽  
Expression System ◽  
Human Growth ◽  
The Body ◽  
Control Group ◽  
Prokaryotic Expression System ◽  
Significant Difference ◽  
Baculovirus System

The human growth hormone (hGH) has been expressed in prokaryotic expression system with low bioactivity previously. Then the effectiveB. moribaculovirus system was employed to express hGH identical to mature hGH successfully in larvae, but the expression level was still limited. In this work, the hGH was expressed inB. moripupae by baculovirus system. Quantification of recombinant hGH protein (BmrhGH) showed that the expression of BmrhGH reached the level of approximately 890 μg/mL pupae supernatant solution, which was five times more than the level using larvae. Furthermore, Animals were gavaged with BmrhGH at the dose of 4.5 mg/rat.day, and the body weight gain (BWG) of treated group had a significant difference (P<.01) compared with the control group. The other two parameters of liver weight and epiphyseal width were also found to be different between the two groups (P<.05). The results suggested that BmrhGH might be used as a protein drug by oral administration.

Solid-phase radioimmunoassay for human growth hormone

1969 ◽  
Vol 6 (5) ◽  
pp. 699-713 ◽  
Author(s):  
J.B. Baumann ◽  
J. Girard ◽  
M. Vest
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Human Growth ◽  
Solid Phase Radioimmunoassay

Modified solid-phase (tube) radioimmunoassay of human growth hormone

1969 ◽  
Vol 47 (9) ◽  
pp. 803-814
Author(s):  
R. M. Bala ◽  
K. A. Ferguson ◽  
J. C. Beck
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Protein Concentration ◽  
Solid Phase ◽  
Ionic Composition ◽  
Rabbit Antiserum ◽  
Human Growth ◽  
Phase System ◽  
Nonspecific Binding ◽  
Free Antibody

Polystyrene tubes were coated with rabbit antiserum to human growth hormone (HGH). Bovine serum albumin (BSA) in buffer, HGH standard or unknown samples, and 125I-HGH were added to the antibodycoated tubes. After incubation the radioactivity in each tube was counted, the incubate discarded, the tubes were washed, and radioactivity was recounted. The sensitivity of the assay was consistently 0.05 mμg HGH or less. Nonspecific binding by uncoated tubes was less than 1%. It was preferable to control the surface area exposed to excess antiserum rather than limit the concentration of the antiserum. Polypropylene and polystyrene tubes gave similar results. Variation of ionic composition or pH of the incubate had no significant effects. Maximum precision and sensitivity occurred with incubation at 4 °C for 40 to 60 h. Addition of posthypophysectomy human plasma or varying the protein concentration had similar effects. The immobilized antibody may be more selective in binding with antigen than is free antibody in solution. Our modifications combine favorable features of the solid-phase system with an increase in sensitivity and greater economy of materials.

scholarly journals Solid-Phase Radioimmunoassay of Human Growth Hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 31C-33C ◽  
Author(s):  
Kevin Catt ◽  
H. D. Niall ◽  
G. W. Tregear
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Human Growth ◽  
Solid Phase Radioimmunoassay

scholarly journals Recombinant human growth hormone treatment in short children with renal disease: Our first experience

2010 ◽  
Vol 138 (3-4) ◽  
pp. 197-203
Author(s):  
Brankica Spasojevic-Dimitrijeva ◽  
Mirjana Kostic ◽  
Amira Peco-Antic ◽  
Divna Kruscic ◽  
Mirjana Cvetkovic ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Recombinant Human Growth Hormone ◽  
Control Period ◽  
Human Growth ◽  
The Body ◽  
Height Velocity ◽  
First Year ◽  
Rhgh Therapy ◽  
Rhgh Treatment

Introduction. Growth retardation is a hallmark of chronic illnesses such as chronic kidney disease in children, and it is associated with increased morbidity and mortality. The growth hormone (GH) resistance observed in uraemia can be overcome by supraphysiological doses of exogenous GH. Objective. We would like to present our first results of recombinant human growth hormone (rhGH) treatment, mainly in children on haemodialysis. Methods. Sixteen children, aged 4.5-17.1 years (mean age 11.25?3.57) with height below -2.0 standard deviation score (SDS) for age or height velocity below -2.0 SDS for age, were selected to receive rhGH therapy at our Nephrology and Haemodialysis Department. Most of them were on haemodialysis (14 children) with mean spent time 2.88?2.68 years (0-9 years) before the initiation of rhGH therapy. One half of patients were prepubertal (8 children) and the second half were in early puberty (testicular volume between 4 and 8 ml for boys and breast development B2 or B3 in girls). All patients received 28-30IU/m? rhGH per week by daily subcutaneous injection. The year before rhGH therapy served as a control period. Results. During the first year of treatment, mean height velocity in haemodialysis patients increased from 2.25 cm/year to 6.59 cm/year (p<0.0001) and in the second year it was 5.25 cm/ year (p=0.004). The mean height SDS in haemodialysis children did not improve significantly during the first year of rhGH treatment (from -3.01 SDS to -2.77 SDS, p=0.063). Neither weight nor the body mass index varied compared with the pretreatment period. Two patients developed worsened secondary hyperparathyroidism and were excluded from the study, but the relationship with rhGH remains uncertain. Conclusion. Mean height velocity significantly improved during rhGH therapy in haemodialysis patients. No significant side-effects were observed in children during three-year treatment with GH.

A thiol functionalized cryogel as a solid phase for selective reduction of a cysteine residue in a recombinant human growth hormone variant

2014 ◽  
Vol 173 ◽  
pp. 76-85 ◽  
Author(s):  
Gry Ravn Jespersen ◽  
Finn Matthiesen ◽  
Anja Kallesøe Pedersen ◽  
Henrik Sune Andersen ◽  
Harald Kirsebom ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Recombinant Human Growth Hormone ◽  
Selective Reduction ◽  
Human Growth ◽  
Cysteine Residue
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