Ultrastructural localization of corticotropin, ?-lipotropin, and ?and ?-endorphin in the porcine anterior pituitary

1981 ◽  
Vol 215 (1) ◽  
Author(s):  
Fran�oise Dacheux
Keyword(s):  
Anterior Pituitary ◽  
Ultrastructural Localization

scholarly journals Ultrastructural localization of prolactin in the rat anterior pituitary glands by preembedding peroxidase-labeled antibody method: observations in normal, castrated, or estrogen-stimulated specimen.

1982 ◽  
Vol 30 (9) ◽  
pp. 919-925 ◽  
Author(s):  
R Y Osamura ◽  
N Komatsu ◽  
S Izumi ◽  
S Yoshimura ◽  
K Watanabe
Keyword(s):  
Anterior Pituitary ◽  
Secretory Granules ◽  
Ultrastructural Localization ◽  
Pronounced Increase ◽  
Alternative Pathways ◽  
Antibody Method ◽  
Pituitary Glands ◽  
Normal Rat ◽  
Estrogen Stimulation

Ultrastructural localization of prolactin (PRL) was studied immunocytochemically (preembedding peroxidase-labeled antibody method) in a variety of pituitaries, including those from 1) normal, 2) castrated, and 3) castrated and estrogen-stimulated rats. In the normal rat, PRL was observed in cisternae of the rough endoplasmic reticulum (RER), perinuclear spaces, Golgi saccules, and secretory granules. In the castrated rats, PRL cells were rather atrophic and were filled with many small PRL-positive secretory granules. RER and Golgi saccules were rather inconspicuous and were almost devoid of PRL localization. The serum PRL level was markedly lowered. With estrogen stimulation after castration, the serum PRL level was markedly elevated and PRL cells showed a pronounced increase of PRL filled cisternae in the RER. From these observations, the role of secretory granules, Golgi apparatus, and RER in hormonal secretion was defined, and it was postulated that some peptide hormones would be secreted along two alternative pathways, i.e., either 1) a long (regulated) pathway or 2) a short (accelerated) pathway, in accordance with their secretory activities, which could be altered by various stimulations such as the use of estrogen.

Different ultrastructural localization of VIP and prolactin in anterior pituitary cells of rats chronically treated with estrogen

Endocrine ◽  
1996 ◽  
Vol 5 (2) ◽  
pp. 219-223 ◽  
Author(s):  
K. Köves ◽  
I-Li Chen ◽  
T. J. Görcs ◽  
J. G. Scammell ◽  
A. Arimura
Keyword(s):  
Anterior Pituitary ◽  
Ultrastructural Localization ◽  
Pituitary Cells ◽  
Anterior Pituitary Cells

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.

Arginine-Vasopressin in Anterior Pituitary Cells: In situ Hybridization of mRNA and Ultrastructural Localization of Immunoreactivity

1991 ◽  
Vol 54 (3) ◽  
pp. 303-311 ◽  
Author(s):  
Chantal Terrier ◽  
Jean-Guy Chabot ◽  
Gerard Pautrat ◽  
Lydie Jeandel ◽  
Dave Gray ◽  
...  
Keyword(s):  
In Situ Hybridization ◽  
Arginine Vasopressin ◽  
Anterior Pituitary ◽  
Ultrastructural Localization ◽  
Pituitary Cells ◽  
Anterior Pituitary Cells

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

Ultrastructural Localization of Acid Mucosubstance in Skeletal Muscle

1967 ◽  
Vol 25 ◽  
pp. 52-53 ◽  
Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer
Keyword(s):  
Striated Muscle ◽  
Divalent Cations ◽  
Ultrastructural Localization ◽  
Major Elements ◽  
Frozen Sections ◽  
Thorium Dioxide ◽  
Iron Solution ◽  
Coupling System ◽  
Psoas Muscles ◽  
Formalin Fixed

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.

Immunoenzymatic demonstration of the simultaneous presence of transferrin, hemopexin and albumin in a same hepatocyte and their ultrastructural localization

1978 ◽  
Vol 36 (2) ◽  
pp. 88-89
Author(s):  
M. Kraemer ◽  
J. Foucrier ◽  
J. Vassy ◽  
M.T. Chalumeau
Keyword(s):  
Plasma Proteins ◽  
Rat Hepatocytes ◽  
Ultrastructural Localization ◽  
Carrier Proteins ◽  
Normal Cells ◽  
Adult Rat ◽  
Adult Rat Hepatocytes ◽  
Monospecific Antisera ◽  
Different Levels

Some authors using immunofluorescent techniques had already suggested that some hepatocytes are able to synthetize several plasma proteins. In vitro studies on normal cells or on cells issued of murine hepatomas raise the same conclusion. These works could be indications of an hepatocyte functionnal non-specialization, meanwhile the authors never give direct topographic proofs suitable with this hypothesis.The use of immunoenzymatic techniques after obtention of monospecific antisera had seemed to us useful to bring forward a better knowledge of this problem. We have studied three carrier proteins (transferrin = Tf, hemopexin = Hx, albumin = Alb) operating at different levels in iron metabolism by demonstrating and localizing the adult rat hepatocytes involved in their synthesis.Immunological, histological and ultrastructural methods have been described in a previous work.

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