Actions of monoclonal antibodies on the activity of human growth hormone (GH) in an in vitro bioassay

2001 ◽  
Vol 174 (1-2) ◽  
pp. 11-19 ◽  
Author(s):  
D. Burbridge ◽  
M. Wallis
Keyword(s):  
Growth Hormone ◽  
Monoclonal Antibodies ◽  
Human Growth Hormone ◽  
Human Growth ◽  
In Vitro Bioassay

Bioactivity of human growth hormone in serum: validation of an in vitro bioassay.

Endocrinology ◽  
1993 ◽  
Vol 132 (5) ◽  
pp. 2073-2082 ◽  
Author(s):  
C M Foster ◽  
M Borondy ◽  
V Padmanabhan ◽  
J Schwartz ◽  
G B Kletter ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
In Vitro Bioassay

Reduced and S-carboxymethylated human growth hormone: a probe for diabetogenic action

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Mouse Mammary Gland ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Hypophysectomized Rats

The biological activity profile of reduced and S-carboxymethylated human growth hormone (RCM-hGH) was determined to establish its suitability for study of the diabetogenic property of hGH. RCM-hGH was found to have greatly attenuated in vivo growth-promoting activity in the 9-day weight-gain test in hypophysectomized rats (approximately 1%) and to have a similar low order of in vitro activity in stimulating amino acid incorporation into the protein of the isolated rat diaphragm. RCM-hGH also only had approximately 1% of the in vitro insulin-like activity of the native hormone on isolated adipose tissue from hypophysectomized rats. In contrast, RCM-hGH retained substantial in vivo diabetogenic activity in the ob/ob mouse, appearing to have approximately 50% of the activity of the native hormone. RCM-hGH was also found to retain significant, although attenuated (25%), in vitro lactogenic activity when tested for the ability to stimulate amino acid incorporation into a casein-rich protein fraction in mouse mammary gland explants. Because RCM-hGH exhibits a high degree of diabetogenic activity, although lacking significant anabolic or insulin-like activities, it will be useful as a "monovalent" probe for the study of the molecular mechanism of the diabetogenic action of GH.

Failure of Human Growth Hormone and Human Placental Lactogen to Affect Glucose Consumption by Human Erythrocytes and Leucocytes In Vitro

1972 ◽  
Vol 50 (10) ◽  
pp. 1014-1017
Author(s):  
Catherine L. Tanser ◽  
Nannie K. M. de Leeuw
Keyword(s):  
Growth Hormone ◽  
Glucose Oxidase ◽  
Human Growth Hormone ◽  
Glucose Utilization ◽  
Human Growth ◽  
Glucose Consumption ◽  
Inhibitory Effect ◽  
Placental Lactogen ◽  
Human Placental Lactogen

The effect of human growth hormone (HGH) and human placental lactogen (HPL) on glucose consumption by erythrocytes and leucocytes in vitro was investigated. Glucose consumption was measured by determining glucose utilization during 3 h incubation at 37 °C, using the glucose oxidase method.HGH and HPL showed no effect on glucose consumption by erythrocytes, and HPL showed no effect on glucose consumption by leucocytes in vitro. Our results do not confirm previous reports of an inhibitory effect of HGH on glucose consumption by erythrocytes in vitro.

Specific monoclonal antibodies and ultrasensitive immunoassays for 20K and 22K human growth hormone

2010 ◽  
Vol 20 (3) ◽  
pp. 239-244 ◽  
Author(s):  
Zida Wu ◽  
Emral Devany ◽  
Giovanna Balarini ◽  
Riia Junnila ◽  
Martin Bidlingmaier ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Monoclonal Antibodies ◽  
Human Growth Hormone ◽  
Human Growth

Nasal delivery of human growth hormone: in vitro and in vivo evaluation of a thiomer/glutathione microparticulate delivery system

2004 ◽  
Vol 100 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Verena M. Leitner ◽  
Davide Guggi ◽  
Alexander H. Krauland ◽  
Andreas Bernkop-Schnürch
Keyword(s):  
Growth Hormone ◽  
Delivery System ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Nasal Delivery ◽  
In Vivo Evaluation

Somatomedin activity measured as sulphation factor in culture media from normal human liver and connective tissues explants. Effects of human growth hormone

1981 ◽  
Vol 98 (1) ◽  
pp. 24-28 ◽  
Author(s):  
R. M. Schimpff ◽  
M. Donnadieu ◽  
M. Gautier ◽  
G. Polini ◽  
A. M. Repellin
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Culture Media ◽  
Human Growth ◽  
Connective Tissues ◽  
Normal Human Liver ◽  
Normal Human ◽  
Higher Doses ◽  
Human Explants

Abstract. Normal human explants from liver and from connective tissues (aponeurosis or skin) incubated in vitro released sulphation activity measurable in chick embryo cartilage. Addition of human Growth Hormone (hGH) at physiological levels (10 ng/ml) increased the sulphation activity after 6 hours incubation time. Higher doses failed to increase the sulphation activity produced by connective tissues and decreased the sulphation activity produced by the liver.

Monoclonal Antibodies for the Study of Human Growth Hormone Forms and Variants

1988 ◽  
pp. 101-112
Author(s):  
F. Frankenne ◽  
J. Closset ◽  
F. Gomez ◽  
G. Pirens ◽  
J. Smal ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Monoclonal Antibodies ◽  
Human Growth Hormone ◽  
Human Growth

scholarly journals Investigation of sequon engineering for improved O-glycosylation by the human polypeptide N-acetylgalactosaminyl transferase T2 isozyme and two orthologues

2021 ◽  
Vol 478 (19) ◽  
pp. 3527-3537
Author(s):  
Nicole K. Thompson ◽  
Leif T. N. LeClaire ◽  
Samantha Rodriguez Perez ◽  
Warren W. Wakarchuk
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Therapeutic Proteins ◽  
Human Growth ◽  
Bacterial Expression ◽  
Intact Protein ◽  
Human Interferon ◽  
Kinetic Properties

We have been developing bacterial expression systems for human mucin-type O-glycosylation on therapeutic proteins, which is initiated by the addition of α-linked GalNAc to serine or threonine residues by enzymes in the GT-27 family of glycosyltransferases. Substrate preference across different isoforms of this enzyme is influenced by isoform-specific amino acid sequences at the site of glycosylation, which we have exploited to engineer production of Core 1 glycan structures in bacteria on human therapeutic proteins. Using RP-HPLC with a novel phenyl bonded phase to resolve intact protein glycoforms, the effect of sequon mutation on O-glycosylation initiation was examined through in vitro modification of the naturally O-glycosylated human interferon α-2b, and a sequon engineered human growth hormone. As part of the development of our glycan engineering in the bacterial expression system we are surveying various orthologues of critical enzymes to ensure complete glycosylation. Here we present an in vitro enzyme kinetic profile of three related GT-27 orthologues on natural and engineered sequons in recombinant human interferon α2b and human growth hormone where we show a significant change in kinetic properties with the amino acid changes. It was found that optimizing the protein substrate amino acid sequence using Isoform Specific O-Glycosylation Prediction (ISOGlyP, http://isoglyp.utep.edu/index.php) resulted in a measurable increase in kcat/KM, thus improving glycosylation efficiency. We showed that the Drosophila orthologue showed superior activity with our human growth hormone designed sequons compared with the human enzyme.

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