High in vivo bioactivities of position 2/Ala15-substituted analogs of bovine growth hormone-releasing factor (bGRF) with improved metabolic stability

Peptides ◽  
1992 ◽  
pp. 85-87 ◽  
Author(s):  
T. M. Kubiak ◽  
A. R. Friedman ◽  
R. A. Martin ◽  
A. K. Ichhpurani ◽  
G. R. Alaniz ◽  
...  
1993 ◽  
Vol 36 (7) ◽  
pp. 888-897 ◽  
Author(s):  
Teresa M. Kubiak ◽  
Alan R. Friedman ◽  
Roger A. Martin ◽  
Avneet K. Ichhpurani ◽  
Glenn R. Alaniz ◽  
...  

1996 ◽  
Vol 85 (4) ◽  
pp. 396-401 ◽  
Author(s):  
Lawrence X. Yu ◽  
Todd P. Foster ◽  
Ron W. Sarver ◽  
William M. Moseley

1996 ◽  
Vol 85 (3) ◽  
pp. 396-401 ◽  
Author(s):  
Lawrence X. Yux ◽  
Todd P. Foster ◽  
Ron W. Sarver ◽  
William M. Moseley

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0.3 nM somatostatin was added 30 min into the base-line period and then was either continued throughout the study or withdrawn during the periods of GHRF infusion.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.


1980 ◽  
Vol 85 (1) ◽  
pp. 35-47 ◽  
Author(s):  
A. T. HOLDER ◽  
M. WALLIS ◽  
P. BIGGS ◽  
M. A. PREECE

SUMMARY Hypopituitary dwarf mice were found to have reduced levels of serum somatomedin-like activity compared with normal mice of the Snell strain. Treatment with bovine growth hormone for 3 and 7 days resulted in growth without significantly increased levels of serum somatomedin-like activity, as detected by in-vitro uptake of 35SO42− into normal rat cartilage; only after treatment for 14 days was somatomedin activity significantly raised. However, treatment for 2 days with bovine growth hormone, bovine prolactin or thyroxine resulted in a dose-dependent increase in in-vivo uptake of 35SO42− into dwarf mouse costal cartilage; growth hormone and thyroxine did not act synergistically. Ten days of treatment with growth hormone promoted a dose-dependent increase in both growth (increased weight gain and tail length) and in-vivo uptake of 35SO42−. Increase in tail length was correlated with uptake of 35SO42−. Thus, in-vivo uptake of 35SO42− into dwarf mouse costal cartilage provides a sensitive method for detecting a dose-related effect of growth hormone.


1971 ◽  
Vol 122 (5) ◽  
pp. 633-640 ◽  
Author(s):  
N. I. Swislocki ◽  
M. Sonenberg ◽  
M. Kikutani

Bovine growth hormone, subjected to DEAE-cellulose chromatography, yielded one major and several minor components. The various chromatographic fractions of bovine growth hormone were compared with the parent material for their ability to promote hormone effects in vivo and in vitro. The major component of bovine growth hormone was homogeneous by acrylamide-gel electrophoresis, rechromatography and sedimentation equilibrium. Its amino acid composition was similar to that of the parent hormone. The major component possessed all the qualitative activities present in the original heterogeneous material, including promotion of acute hypoglycaemia and hypolipaemia. In studies in vitro in adipose-tissue segments the major component of the hormone increased entry of glucose and its oxidation to CO2, conversion of glucose into glyceride glycerol, release of glycerol and incorporation of histidine into adiposetissue protein. Other chromatographic fractions of bovine growth hormone were not homogeneous and possessed some but not all of the metabolic activities attributed to the hormone preparations or its major component. Thus, the metabolic effects obtained with bovine growth-hormone preparations in vivo and in vitro can be obtained with the major homogeneous component of the hormone. This observation precludes the possibility that the metabolic effects obtained with bovine growth-hormone preparations are due to the combined actions of a number of components found therein.


Neuropeptides ◽  
1991 ◽  
Vol 19 (4) ◽  
pp. 223-229 ◽  
Author(s):  
J. Carretero ◽  
F. Sánchez ◽  
R. Vázquez ◽  
L. Cacicedo ◽  
F. Sánchez-Franco ◽  
...  

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