New Gaba-containing analogues of human Growth Hormone Releasing Hormene (1–30)-amide: II. Detailed in vivo biological examinations

1993 ◽  
Vol 16 (10) ◽  
pp. 799-805 ◽  
Author(s):  
Magdolna Kovàcs ◽  
I. Mezõ ◽  
I. Teplán ◽  
M. Hollósi ◽  
J. Kajtár ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth

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.

Design and in vivo evaluation of solid-in-oil suspension for oral delivery of human growth hormone

2008 ◽  
Vol 41 (2) ◽  
pp. 106-110 ◽  
Author(s):  
Hiromu Yoshiura ◽  
Yoshiro Tahara ◽  
Masakazu Hashida ◽  
Noriho Kamiya ◽  
Akihiko Hirata ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Oral Delivery ◽  
Human Growth ◽  
In Vivo Evaluation

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

Periodic interactions of GH-releasing factor and somatostatin can augment GH release in vitro

1987 ◽  
Vol 253 (5) ◽  
pp. E508-E514
Author(s):  
J. Weiss ◽  
M. J. Cronin ◽  
M. O. Thorner
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Male Rat ◽  
Base Line ◽  
Additive Effects ◽  
Growth Hormone Releasing Factor ◽  
The Impact

Growth hormone (GH) is secreted as pulses in vivo. To understand the signals governing this periodicity, we have established a perifusion-based model of pulsatile GH release. Male rat anterior pituitaries were dispersed and perifused with pulses of human growth hormone-releasing factor-(1--40) (GHRF), with or without a continuous or discontinuous somatostatin tonus. An experiment was composed of a 1-h base-line collection followed by four 3-h cycles; each contained single or paired 10-min infusion(s) of 3 nM GHRF. In testing the impact of somatostatin, the protocol was identical except that 0.3 nM somatostatin was added 30 min into the base-line period and then was either continued throughout the study or withdrawn during the periods of GHRF infusion. GH base lines with somatostatin were lower than vehicle base lines (P less than 0.05). GHRF pulses generated consistent peaks of GH release between 200 and 300 ng. min-1. (10(7) cells)-1, and these peaks were not altered by continuous somatostatin. In contrast, withdrawal of somatostatin during GHRF administration elicited markedly higher GH peaks (P less than 0.05) and more total GH release (P less than 0.05). This response could not be accounted for by the additive effects of GHRF and somatostatin withdrawal.

IN VITRO AND IN VIVO EFFECT OF GROWTH HORMONE ON ALDOSTERONE SECRETION

1960 ◽  
Vol 38 (1) ◽  
pp. 1069-1075
Author(s):  
O. J. Lucis ◽  
E. H. Venning
Keyword(s):  
Growth Hormone ◽  
Adrenal Gland ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Secretion Rate ◽  
Aldosterone Secretion ◽  
Hypophysectomized Rats

Porcine, monkey, and human growth hormone have no effect on the in vitro secretion of aldosterone by the rat adrenal gland. When monkey growth hormone is injected into hypophysectomized rats, the adrenals of these animals secrete, under in vitro conditions, increased amounts of aldosterone with no change in the secretion rate of corticosterone. The plasma of these rats contains a substance which appears to stimulate the secretion of aldosterone in the adrenals of normal rats.

Synthesis and purification of a deleted human growth hormone, hGHΔ135–146: sensitivity to plasmin cleavage and in vitro and in vivo bioactivities

2000 ◽  
Vol 78 (1) ◽  
pp. 49-59 ◽  
Author(s):  
Khorshed S.M Alam ◽  
Takahiko Fujikawa ◽  
Hideo Yoshizato ◽  
Minoru Tanaka ◽  
Kunio Nakashima
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth

In vivo interaction of human growth hormone (HGH) with subcellular structures of rat liver

1978 ◽  
Vol 12 (11) ◽  
pp. 1087
Author(s):  
M C POSTEL-VINAY ◽  
C KAYSER ◽  
B DESBUQUOIS
Keyword(s):  
Growth Hormone ◽  
Rat Liver ◽  
Human Growth Hormone ◽  
Human Growth

Parallel insulin-like actions of human growth hormone and its part sequence hGH 7–13

1983 ◽  
Vol 102 (4) ◽  
pp. 492-498 ◽  
Author(s):  
John McD. Armstrong ◽  
Joseph Bornstein ◽  
Janet O. Bromley ◽  
S. Lance Macaulay ◽  
Frank M. Ng
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Synthetic Peptide ◽  
Glycogen Synthase ◽  
Human Growth ◽  
Phosphorylase Activity ◽  
Insulin Dependent ◽  
Old Rats ◽  
Insulin Like Activity

Abstract. The insulin-like effects of human growth hormone and the synthetic part sequence, Nα-acetyl-hGH 7–13, on glycogen synthase and phosphorylase have been compared in an in vivo system using 16–18-day-old rats. Both the hormone and its part sequences had similar effects, increasing muscle glycogen synthase a activity and decreasing liver phosphorylase a activity, without affecting phosphorylase activity in muscle or synthase activity in liver. Insulin had similar effects, but also increased liver synthase a activity. The effects of all three substances could be abolished by prior treatment of the animals with anti-insulin serum, showing that the effects of growth hormone and its part sequences were insulin-dependent. Both growth hormone and the synthetic peptide increased the binding of insulin to liver plasma membrane. It is concluded that the insulin-like activity of human growth hormone is associated with a region containing residues 7 to 13 of the hormone molecule, and that this activity is insulin-dependent. It is suggested that both growth hormone and the synthetic peptide produce insulin-like activity by enhancing the binding of circulating insulin to its receptor.

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