scholarly journals Receptors and Sites of Synthesis and Storage of γ-Aminobutyric Acid in Human Pituitary Glands and in Growth Hormone Adenomas

2005 ◽  
Vol 124 (4) ◽  
pp. 550-558 ◽  
Author(s):  
Katrin End ◽  
Katia Gamel-Didelon ◽  
Heike Jung ◽  
Markus Tolnay ◽  
Dieter Lüdecke ◽  
...  
1965 ◽  
Vol 49 (1) ◽  
pp. 1-16 ◽  
Author(s):  
M. Apostolakis

ABSTRACT A method for the extraction of prolactin from human pituitary glands is described. It is based on acetone drying, distilled water extraction, acetone and isoelectric precipitation. Two main products are obtained: Fraction R8 with a mean prolactin activity of 12.2 IU/mg and fraction U8 with a mean prolactin activity of 8.6 IU/mg. The former fraction does not contain any significant gonadotrophin activity and the latter contains on an average 50 HMG U/mg. In both cases contamination with ACTH and MSH is minimal. The growth hormone activity of both these fractions is low. It is postulated that in man too, prolactin and growth hormone are two distinct hormones. A total of 1250 human pituitary glands have been processed by this method. The mean prolactin content per pituitary gland has been found to be 73 IU.


1970 ◽  
Vol 48 (4) ◽  
pp. 639-647 ◽  
Author(s):  
PATRICIA M. NICHOLSON

SUMMARY Polyacrylamide disc gel electrophoresis of aqueous extracts of individual human anterior pituitary glands failed to identify a protein with lactogenic activity which was characteristic of pregnancy and the post-partum period. Lactogenic activity, determined by a semi-quantitative rabbit mammary gland organ culture assay, was largely associated with the growth hormone fraction. The total prolactin activity of individual anterior pituitary glands was determined by a 'local' intradermal pigeon crop sac method. The glands from pregnant and parturient women did not contain a higher concentration of prolactin than those of men or non-pregnant non-lactating women. These results do not provide any evidence for the existence of a human pituitary prolactin distinct from growth hormone. Reasons for this are discussed.


1993 ◽  
Vol 328 (5) ◽  
pp. 358-359 ◽  
Author(s):  
Clarence J. Gibbs ◽  
David M. Asher ◽  
Paul W. Brown ◽  
Judith E. Fradkin ◽  
D. Carleton Gajdusek

1984 ◽  
Vol 107 (1) ◽  
pp. 36-41 ◽  
Author(s):  
T. R. Hall ◽  
S. Harvey ◽  
A. Chadwick

Abstract. Anterior pituitary glands from chickens (Gallus domesticus) were incubated with or without single, mediobasal chicken hypothalami in medium containing histamine, alone or together with the antagonist diphenhydramine or in medium containing gamma-aminobutyric acid (GABA), alone or together with the antagonists bicuculline or picrotoxin. The release of prolactin (Prl) and growth hormone (GH) was measured by homologous radioimmunoassay. Histamine had no direct effect on the release of either hormone but stimulated Prl (in a dose-related way) and GH release when anterior pituitary glands were co-incubated with hypothalami. Diphenhydramine also had no direct effect on Prl or GH secretion but blocked the stimulatory effect of histamine on hypothalamusinduced Prl and GH release. When anterior pituitary glands were incubated without hypothalami, GABA, bicuculline and picrotoxin had no effect on the release of Prl or GH. However, GABA inhibited the release of both hormones in a concentration-related manner, when anterior pituitary glands were co-incubated with hypothalami. This inhibition was blocked by both bicuculline and picrotoxin. These results suggest that histamine and GABA may be involved in controlling the secretion of Prl and GH from the avian pituitary gland, possibly by modifying the secretion of hypothalamic releasing and/or release-inhibiting hormones.


1961 ◽  
Vol 39 (11) ◽  
pp. 1659-1668 ◽  
Author(s):  
Alfred E. Wilhelmi

A method of serial extraction of human pituitary glands is described. FSH, LH, and TSH are predominantly found in the first extract. A second extraction, under different conditions, yields principally growth hormone and some prolactin. A third extraction, under more extreme conditions of pH and temperature, yields, especially for acetone-preserved glands, an additional amount of growth hormone and the greater part of the prolactin. The method is presented as a contribution to the more efficient use of scarce and valuable human pituitaries.


1994 ◽  
Vol 12 (2) ◽  
pp. 167-172 ◽  
Author(s):  
A Hüttner ◽  
E F Adams ◽  
M Buchfelder ◽  
R Fahlbusch

ABSTRACT The structure of the GH gene in human somatotrophinomas was examined in terms of promoter region sequence and degree of methylation. In six tumours, the promoter sequence did not differ from that observed in the corresponding genomic (white blood cell-derived) DNA, suggesting that it is unlikely that excessive GH production is due to a point mutation within this region. In contrast, Southern blot analysis using the methylation-sensitive restriction enzymes HpaII and HhaI revealed lower levels of methylation of the GH gene in somatotrophinomas when compared with that found in DNA derived from normal pituitary glands. We conclude that hypomethylation of the GH gene in human somatotrophinomas may play at least a partial role in excessive GH production.


1962 ◽  
Vol 40 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Zvi Laron ◽  
Sara Assa

ABSTRACT Human growth hormone (HGH) prepared from human pituitary glands by the method of Raben (1959) showed two components on agar gel electrophoresis. Fraction I corresponded to a slow alpha-globulin, and fraction II had a mobility between alpha and beta-globulin. On agar gel immunoelectrophoresis using HGH and rabbit antiserum to HGH, these two components showed immunological identity. By using agar gel immunoelectrophoresis and the haemagglutination technique HGH preparations of both Raben and Li type were shown to be contaminated with human albumin. Antiserum to human growth hormone containing also antibodies against human albumin was purified by adsorption with human albumin. It is postulated that part of the difficulties encountered in the use of the haemagglutination-inhibition technique to determine growth hormone concentration in serum, is due to impurities in the human growth hormone preparations and antisera to these preparations in use.


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