Luteinizing Hormone Releasing Hormone-Biosynthesis by Rat Hypothalamus in Vitro. Influence of Castration

1974 ◽  
Vol 147 (2) ◽  
pp. 434-437 ◽  
Author(s):  
J. A. Moguilevsky ◽  
M. A. Enero ◽  
B. Szwarcfarb
1987 ◽  
Vol 12 (7) ◽  
pp. 651-657 ◽  
Author(s):  
Jerome M. Goldman ◽  
Ralph L. Cooper ◽  
Georgia L. Rehnberg ◽  
Scott Gabel ◽  
W. Keith McElroy ◽  
...  

1987 ◽  
Vol 45 (3) ◽  
pp. 191-196 ◽  
Author(s):  
Akira Miyake ◽  
Shirou Ohtsuka ◽  
Takamichi Nishizaki ◽  
Keiichi Tasaka ◽  
Toshihiro Aono ◽  
...  

1975 ◽  
Vol 79 (1) ◽  
pp. 7-15 ◽  
Author(s):  
E. C. Griffiths ◽  
K. C. Hooper ◽  
C. R. N. Hopkinson

ABSTRACT Luteinizing hormone-releasing hormone (LH-RH) is known to be inactivated by peptidases in the rat hypothalamus with consequent loss of LH-releasing ability. To make a further study of the peptidases' action on the decapeptide, synthetic LH-RH and its [1–9NH2] analogue were incubated with the supernatant hypothalamic fraction containing the enzyme activity. Using an assay system measuring gonadotrophin release in ovariectomized/steroid-primed rats, both LH-RH and the [1–9NH2] analogue were found to be inactivated to different extents after incubation with the fraction, the analogue completely losing both LH- and FSH-releasing activity, and the releasing hormone almost completely losing its LH- and totally losing its FSH-releasing activity. The findings extend the initial studies by showing that the peptidases can remove both the decapeptide's intrinsic LH- and FSH-releasing activity and that these enzymes act on LH-RH at a site other than the C-terminal glycinamide, since they are able to inactivate the [1–9NH2] analogue lacking this residue.


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