scholarly journals Long-Lasting Growth Hormone Regulated by the Ubiquitin-Proteasome System

2021 ◽  
Vol 22 (12) ◽  
pp. 6268
Author(s):  
Myung-Sun Kim ◽  
Kyunggon Kim ◽  
Su Kyung Oh ◽  
Gidae Lee ◽  
Jin-Ock Kim ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Half Life ◽  
Human Growth ◽  
Ubiquitin Proteasome System ◽  
Blood Stream ◽  
Growth Hormones ◽  
Ubiquitination Site ◽  
Lysine Residues ◽  
Arginine Residues ◽  
Ubiquitin Proteasome

To increase the half-life of growth hormones, we proposed its long-lasting regulation through the ubiquitin-proteasome system (UPS). We identified lysine residues (K67, K141, and K166) that are involved in the ubiquitination of human growth hormone (hGH) using ubiquitination site prediction programs to validate the ubiquitination sites, and then substituted these lysine residues with arginine residues. We identified the most effective substituent (K141R) to prevent ubiquitination and named it AUT-hGH. hGH was expressed and purified in the form of hGH-His, and ubiquitination was first verified at sites containing K141 in the blood stream. Through the study, we propose that AUT-hGH with an increased half-life could be used as a long-lasting hGH in the blood stream.

Regulation of immunity in rats by lactogenic and growth hormones

1983 ◽  
Vol 102 (3) ◽  
pp. 351-357 ◽  
Author(s):  
Eva Nagy ◽  
Istvan Berczi ◽  
Henry G. Friesen
Keyword(s):  
Growth Hormone ◽  
Contact Dermatitis ◽  
Blood Cells ◽  
Antibody Formation ◽  
Human Growth ◽  
Growth Hormones ◽  
Placental Lactogen ◽  
Bovine Growth Hormone ◽  
Human Placental Lactogen ◽  
Rat Growth

Abstract. Antibody formation to sheep red blood cells and the development of contact dermatitis in response to dinitrochlorobenzene are impaired in hypophysectomized (Hypo-X) rats. Rat prolactin, rat growth hormone, bovine prolactin, bovine growth hormone, human placental lactogen and human growth hormone all restored the immunological competence of Hypo-X animals. The possible mechanism of action of these hormones on immune reactions is discussed.

Comparison of the pharmacological properties of pituitary and biosynthetic human growth hormone

1987 ◽  
Vol 114 (1) ◽  
pp. 124-131 ◽  
Author(s):  
Karin Damm Jørgensen
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Growth Hormones ◽  
Pharmacological Properties ◽  
Obese Mice ◽  
Sleeping Time ◽  
Test Systems ◽  
Pharmacological Test ◽  
Hexobarbital Sleeping Time

Abstract. Biosynthetic human growth hormone was compared with pituitary human growth hormone and pituitary 22 K in the weight gain and the tibia test. The three preparations were found to be equipotent. Furthermore, the growth hormones were compared in various pharmacological test systems. All three preparations were found to have a marked antidiuretic and antinatriuretic effect in the rat and to cause a significant shortening of the hexobarbital sleeping time in mice. Biosynthetic and pituitary preparations had the same diabetogenic activity in obese mice, and the growth hormones did not differ with respect to pharmacological profiles in the test systems applied.

scholarly journals The Aspartyl Protease Ddi1 Is Essential for Erythrocyte Invasion by the Malaria Parasite

2021 ◽  
Author(s):  
Sophie Ridewood ◽  
Barbara Dirac-Svejstrup ◽  
Steven A Howell ◽  
Anne Weston ◽  
Christine Lehmann ◽  
...  
Keyword(s):  
Red Blood Cells ◽  
Blood Cells ◽  
Proteasome Inhibition ◽  
Ubiquitin Proteasome System ◽  
Blood Stream ◽  
Parasite Life Cycle ◽  
Erythrocyte Invasion ◽  
Multiple Components ◽  
Ubiquitin Proteasome ◽  
Inducible Protein

Malaria pathology is caused by the exponential replication of Plasmodium parasites in the blood stream. The bottleneck of the parasite life cycle is the invasion of erythrocytes immediately after parasites egress from infected red blood cells. DNA damage-inducible protein 1 (Ddi1) is a conserved eukaryotic proteasome shuttle protein containing an internal retroviral-like protease domain. Using conditional genetics, we now show that the proteolytic activity of the P. falciparum homologue, PfDdi1, is critically required for invasion of red blood cells. Furthermore, PfDdi1 disruption results in the accumulation of highly polyubiquitinated proteins that can be processed by purified PfDdi1 or distant eukaryotic homologues. We also show that PfDdi1 interacts with multiple components of the ubiquitin-proteasome system and that parasites lacking PfDdi1 are more sensitive to proteasome inhibition. Overall, this study establishes PfDdi1 as a key component of the eukaryotic ubiquitin-proteasome system and as a promising antimalarial target.

Human and rat growth hormones enhance guanylate cyclase activity

1981 ◽  
Vol 240 (2) ◽  
pp. E79-E82
Author(s):  
D. L. Vesely
Keyword(s):  
Growth Hormone ◽  
Guanylate Cyclase ◽  
Soluble Guanylate Cyclase ◽  
Human Growth ◽  
Growth Hormones ◽  
Cyclase Activity ◽  
Kidney Cortex ◽  
Guanylate Cyclase Activity ◽  
Rat Growth ◽  
Stimulation Of

The objective of this investigation was to determine whether physiological levels of growth hormone have part of their mechanism of action through stimulation of guanylate cyclase (EC 4.6.1.2.). Rat and human growth hormones enhanced the activity of soluble guanylate cyclase two- to fourfold in rat gracilis anticus skeletal muscle, liver, lung, heart, pancreas, and kidney cortex at a concentration of 10 nM. Dose-response relationships revealed that more than half-maximal stimulation of guanylate cyclase activity was seen at a concentration as low as 10 nM and nonstimulation of guanylate cyclase activity was seen when the concentration was decreased to 1 nM. Maximal enhancement was seen at 100 nM of growth hormone, and there was no further enhancement when the concentration was increased to the micromolar or millimolar range. Thus, the data in this investigation indicate that at concentrations at which growth hormone is known to cause its growth-promoting effects, growth hormone does cause an enhancement of the activity of the guanylate cyclase-cyclic GMP system.

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