scholarly journals In cow anterior pituitary, growth hormone and prolactin can be packed in separate granules of the same cell.

1985 ◽  
Vol 100 (6) ◽  
pp. 2019-2024 ◽  
Author(s):  
G Fumagalli ◽  
A Zanini
Keyword(s):  
Growth Hormone ◽  
Golgi Complex ◽  
Anterior Pituitary ◽  
Relative Proportion ◽  
Protein A ◽  
Central Area ◽  
Ultrastructural Localization ◽  
Specific Antibodies ◽  
Gold Particles ◽  
Pituitary Growth Hormone

The ultrastructural localization of growth hormone and prolactin in cow anterior pituitary was studied by double immunocytochemical labeling using specific antibodies and protein A-gold particles of different sizes. The two hormones were found in specific somatotrophs and mammotrophs as well as in somatomammotropic cells which were multinucleated and predominantly arranged in clusters in the central area of the lobules. In these mixed cells the two hormones were packaged (a) in different granules of the same cell, (b) in the same granules where they were segregated in different portions of the granule content, or (c) in the same granules but evenly intermixed. The relative proportion of these three types of granules varied in somatomammotrophs of different animals. A single large Golgi complex was generally present in somatomammotrophs. Small, immature granules containing either growth hormone or prolactin or both hormones were found randomly distributed along Golgi stacks. This suggests that in these cells the two hormones are processed in the same Golgi cisternae and that mechanism(s) exist(s) to sort out the two hormones from each other.

scholarly journals The mobilization of lipid by anterior pituitary growth hormone

1953 ◽  
Vol 54 (3) ◽  
pp. 407-413 ◽  
Author(s):  
A. L. Greenbaum ◽  
Patricia McLean
Keyword(s):  
Growth Hormone ◽  
Anterior Pituitary ◽  
Pituitary Growth Hormone

Anterior Pituitary Growth Hormone (STH) and Pancreatic Secretion of Glucagon (HGF).

1953 ◽  
Vol 83 (4) ◽  
pp. 758-761 ◽  
Author(s):  
P. P. Foa ◽  
E. B. Magid ◽  
M. D. Glassman ◽  
H. R. Weinstein
Keyword(s):  
Growth Hormone ◽  
Pancreatic Secretion ◽  
Anterior Pituitary ◽  
Pituitary Growth Hormone

Galactopoietic Activity of Purified Anterior Pituitary Growth Hormone

Nature ◽  
1949 ◽  
Vol 164 (4180) ◽  
pp. 992-993 ◽  
Author(s):  
P. M. Cotes ◽  
J. A. Crichton ◽  
S. J. Folley ◽  
F. G. Young
Keyword(s):  
Growth Hormone ◽  
Anterior Pituitary ◽  
Pituitary Growth Hormone

scholarly journals Immunoelectron microscopic demonstration of S-100b protein-like in centriole, cilia, and basal body.

1988 ◽  
Vol 36 (6) ◽  
pp. 693-696 ◽  
Author(s):  
T Uchida ◽  
T Endo
Keyword(s):  
Basal Body ◽  
Colloidal Gold ◽  
Protein A ◽  
Ultrastructural Localization ◽  
Basal Bodies ◽  
Cell Organelles ◽  
Gold Particles ◽  
Microscopic Demonstration ◽  
S 100 ◽  
And Function

We report here the ultrastructural localization of S-100b protein-like immunoreactivity in the centriole, cilia, and basal body. Duodenum and trachea of guinea pigs and rats were fixed and immunostained by the protein A-gold method. All centrioles, cilia, and basal bodies observed showed clear S-100b protein-like immunoreactivity. Specific colloidal gold particles were located over the microtubules in these cell organelles. However, other microtubules scattered throughout the cytoplasm were devoid of immunoreactivity. Although the functional significance of S-100b protein-like immunoreactivity in the centriole, cilia, and basal bodies remains to be elucidated, the present results introduce new perspectives into the investigation of localization and function of S-100 proteins.

scholarly journals Quantitative immunocytochemical localization of Na+,K+-ATPase in rat ciliary epithelial cells.

1989 ◽  
Vol 37 (9) ◽  
pp. 1353-1361 ◽  
Author(s):  
T Okami ◽  
A Yamamoto ◽  
K Omori ◽  
M Akayama ◽  
M Uyama ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Aqueous Humor ◽  
Ciliary Body ◽  
Protein A ◽  
Ultrastructural Localization ◽  
Immunoblot Analysis ◽  
Alpha Subunit ◽  
Ciliary Epithelium ◽  
Immunocytochemical Localization ◽  
Gold Particles

Ultrastructural localization of Na+,K+-ATPase in rat ciliary epithelium was investigated quantitatively by the protein A-gold technique, using an affinity-purified antibody against the alpha-subunit of Na+,K+-ATPase. Immunoblot analysis showed that the antibody bound specifically to the alpha-subunit of Na+,K+-ATPase in the ciliary body. Gold particles were found mainly on the basolateral surfaces of both the pigmented epithelial (PE) and nonpigmented epithelial (NPE) cells with an approximately twofold higher labeling density in the PE cells. A few gold particles were also found on the apical and ciliary channel surfaces of the PE cells, whereas no significant binding was found on the apical surfaces of the NPE cells. The basolateral surfaces of PE and NPE cells are markedly infolded and are much greater in area than the apical surfaces. This means that Na+,K+-ATPase is almost exclusively located on the basolateral surfaces of both the NPE and PE cells. We suggest that the Na+,K+-ATPase of both the NPE and PE cells play an important role in the formation of aqueous humor.

ADMINISTRATION OF ANTERIOR PITUITARY GROWTH HORMONE TO RATS DURING COLD EXPOSURE

1963 ◽  
Vol 41 (1) ◽  
pp. 1449-1453
Author(s):  
John R. Beaton ◽  
T. Orme ◽  
J. Laufer ◽  
A. Turner
Keyword(s):  
Growth Hormone ◽  
Body Weight ◽  
Weight Gain ◽  
Cold Exposure ◽  
Anterior Pituitary ◽  
Body Weight Gain ◽  
Nitrogen Retention ◽  
Growing Rats ◽  
Pituitary Growth Hormone ◽  
Environmental Temperatures

Male, growing rats were injected daily with anterior pituitary growth hormone (3 mg/100 g body weight) and fed ad libitum for 7 days at environmental temperatures of 22 °C and 2–3 °C. Body weight gain, nitrogen retention, and four liver enzyme activities were measured. As observed previously, cold exposure retarded body weight gain and decreased nitrogen retention despite an increased food intake. These effects of cold were not eliminated by administration of growth hormone. The increased activities of liver arginase, alanine-glutamic transminase, and phosphate-activated glutaminase consequent upon cold exposure were not significantly affected by growth hormone although, at 22 °C, growth hormone decreased the activities of liver arginase and alanine-glutamic transaminase. Cold exposure eliminated the lowering effect of growth hormone on liver glutamic acid dehydrogenase activity observed at 22 °C. It is concluded that, under these conditions, growth hormone does not overcome the protein catabolic effects of cold exposure but rather, cold exposure eliminates the protein anabolic effects of the hormone.

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