Use of Athymic Nude Mice for in vivo Studies of Human Growth-Hormone-Secreting Pituitary Adenomas

1991 ◽  
Vol 35 (5) ◽  
pp. 198-204 ◽  
Author(s):  
Maximilian J.A. Puchner ◽  
Dieter K. Lüdecke ◽  
Wolfgang Saeger ◽  
Hans-Dietrich Herrmann
1994 ◽  
Vol 269 (32) ◽  
pp. 20806
Author(s):  
W.Y. Chen ◽  
N. Chen ◽  
J. Yun ◽  
T.E. Wagner ◽  
J.J. Kopchick

1994 ◽  
Vol 269 (22) ◽  
pp. 15892-15897
Author(s):  
W.Y. Chen ◽  
N.Y. Chen ◽  
J. Yun ◽  
T.E. Wagner ◽  
J.J. Kopchick

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick

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.


2008 ◽  
Vol 41 (2) ◽  
pp. 106-110 ◽  
Author(s):  
Hiromu Yoshiura ◽  
Yoshiro Tahara ◽  
Masakazu Hashida ◽  
Noriho Kamiya ◽  
Akihiko Hirata ◽  
...  

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

2004 ◽  
Vol 100 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Verena M. Leitner ◽  
Davide Guggi ◽  
Alexander H. Krauland ◽  
Andreas Bernkop-Schnürch

1987 ◽  
Vol 253 (5) ◽  
pp. E508-E514
Author(s):  
J. Weiss ◽  
M. J. Cronin ◽  
M. O. Thorner

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.


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