Dopamine enters lactotrophs and reaches their secretory granules

1985 ◽  
Vol 104 (1) ◽  
pp. 23-NP ◽  
Author(s):  
M. G. P. Gallardo ◽  
M. Bilinski ◽  
S. R. Chiocchio ◽  
J. H. Tramezzani
Keyword(s):  
Electron Microscopy ◽  
Light Microscopy ◽  
Anterior Pituitary ◽  
Secretory Granules ◽  
Pituitary Cells ◽  
Histochemical Reaction ◽  
Anterior Pituitary Cells ◽  
Biochemical Assays ◽  
Pituitary Lactotroph

ABSTRACT The presence of dopamine in the lactotroph cell, as well as in isolated prolactin secretory granules, was demonstrated by means of an histochemical reaction for electron microscopy. Biochemical assays further confirmed the presence of dopamine in the secretory granules. Autoradiographic preparations examined by light microscopy showed dopamine internalization in dispersed anterior pituitary cells. Isolated anterior pituitary lactotroph cells incorporated more [3H]dopamine than a fraction containing other anterior pituitary cells. J. Endocr. (1985) 104, 23–28

Synaptobrevin isoforms in secretory granules and synaptic-like microvesicles in anterior pituitary cells

Life Sciences ◽  
1998 ◽  
Vol 62 (7) ◽  
pp. 607-616 ◽  
Author(s):  
Glòria Majó ◽  
Fernando Aguado ◽  
Juan Blasi ◽  
Jordi Marsal
Keyword(s):  
Anterior Pituitary ◽  
Secretory Granules ◽  
Pituitary Cells ◽  
Anterior Pituitary Cells

scholarly journals Detection of insulin synthesis in mammalian anterior pituitary cells by immunohistochemistry and demonstration of insulin-related transcripts by in situ RNA-DNA hybridization.

1986 ◽  
Vol 34 (5) ◽  
pp. 673-678 ◽  
Author(s):  
G C Budd ◽  
B Pansky ◽  
B Cordell
Keyword(s):  
Growth Hormone ◽  
Nucleic Acid ◽  
Dna Hybridization ◽  
Anterior Pituitary ◽  
Secretory Granules ◽  
Pituitary Cells ◽  
Insulin Synthesis ◽  
Anterior Pituitary Cells ◽  
Pancreatic B Cells

Insulin or highly homologous transcripts is shown to be synthesized in cultures of mammalian anterior pituitary cells using cloned insulin-specific cDNA probes and nucleic acid cytochemistry. The insulin-hybridizing cells are less abundant than the growth hormone-producing cells, occurring in the cultures at approximately one tenth the frequency. Immunocytochemistry demonstrates that insulin or insulin-like proteins is also synthesized by the cultured pituitary cells and that the insulin immunoreactivity is contained within secretory granules. It appears that many of these secretory granules are concentrated around the periphery of the cell, unlike the insulin-containing granules in pancreatic B-cells.

scholarly journals Visualization of the Nuclear Lamina in Mouse Anterior Pituitary Cells and Immunocytochemical Detection of Lamin A/C by Quick-freeze Freeze-substitution Electron Microscopy

2005 ◽  
Vol 53 (4) ◽  
pp. 497-507 ◽  
Author(s):  
Takao Senda ◽  
Akiko Iizuka-Kogo ◽  
Atsushi Shimomura
Keyword(s):  
Electron Microscopy ◽  
Nuclear Membrane ◽  
Anterior Pituitary ◽  
Freeze Substitution ◽  
Nuclear Lamina ◽  
Immunogold Electron Microscopy ◽  
Lamin A ◽  
Pituitary Cells ◽  
Inner Nuclear Membrane ◽  
Anterior Pituitary Cells

We examined the nuclear lamina in the quickly frozen anterior pituitary cells by electron microscopic techniques combined with freeze substitution, deep etching, and immunocytochemistry and compared it with that in the chemically fixed cells. By quick-freeze freeze-substitution electron microscopy, an electron-lucent layer, as thick as 20 nm, was revealed just inside the inner nuclear membrane, whereas in the conventionally glutaraldehyde-fixed cells the layer was not seen. By quick-freeze deep-etch electron microscopy, we could not distinguish definitively the layer corresponding to the nuclear lamina in either fresh unfixed or glutaraldehyde-fixed cells. Immunofluorescence microscopy showed that lamin A/C in the nucleus was detected in the acetone-fixed cells and briefly in paraformaldehyde-fixed cells but not in the cells with prolonged paraformaldehyde fixation. Nuclear localization of lamin A/C was revealed by immunogold electron microscopy also in the quickly frozen and freeze-substituted cells, but not in the paraformaldehyde-fixed cells. Lamin A/C was localized mainly in the peripheral nucleoplasm within 60 nm from the inner nuclear membrane, which corresponded to the nuclear lamina. These results suggest that the nuclear lamina can be preserved both ultrastructurally and immunocytochemically by quick-freezing fixation, rather than by conventional chemical fixation.

scholarly journals Immunocytochemical localization of cathepsin B in rat anterior pituitary endocrine cells, with special reference to its co-localization with renin and prorenin in gonadotrophs.

1991 ◽  
Vol 39 (9) ◽  
pp. 1199-1205 ◽  
Author(s):  
Y Uchiyama ◽  
M Nakajima ◽  
T Watanabe ◽  
S Waguri ◽  
N Sato ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Luteinizing Hormone ◽  
Light Microscopy ◽  
Cathepsin B ◽  
Anterior Pituitary ◽  
Endocrine Cells ◽  
Secretory Granules ◽  
Juxtaglomerular Cells ◽  
Immunocytochemical Localization ◽  
Double Immunostaining

We examined by immunocytochemistry the localization of cathepsin B in endocrine cells of rat anterior pituitary lobe, using a monospecific antibody to cathepsin B. By light microscopy, granular immunodeposits for cathepsin B were detected in most endocrine cells of anterior pituitary lobe. Cells immunoreactive for luteinizing hormone (LH) were diffusely immunostained by anti-cathepsin B. By electron microscopy, immunogold particles for cathepsin B were localized in lysosomes of thyrotrophs, somatotrophs, and mammotrophs. In mammotrophs, immunogold particles for cathepsin B were also detected in crinophagic bodies. Double immunostaining co-localized immunogold particles for LH and cathepsin B in secretory granules of gonadotrophs. Immunocytochemistry was also applied to demonstrate localization of renin and prorenin in LH-producing gonadotrophs; immunogold particles for renin were co-localized with those for LH, cathepsin B, or prorenin in their secretory granules. Immunogold particles for prorenin were also co-localized with those for LH or cathepsin B in secretory granules, but prorenin-positive granules appeared less frequently than renin-positive granules. These results suggest that cathepsin B not only plays a role in the protein degradation in lysosomes of anterior pituitary endocrine cells but also participates in the activation of renin in gonadotrophs, as has been demonstrated in secretory granules of juxtaglomerular cells.

Surface morphology and secretory activity of rat anterior pituitary cells in primary culture

1978 ◽  
Vol 36 (2) ◽  
pp. 584-585
Author(s):  
T. Antakly ◽  
F. Zeytinoglu ◽  
G. Pelletier ◽  
F. Labrie
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Surface Morphology ◽  
Primary Culture ◽  
Anterior Pituitary ◽  
Secretory Activity ◽  
Secretory Cells ◽  
Pituitary Cells ◽  
Anterior Pituitary Cells ◽  
Scanning Electron

So far, there has been no report concerning the surface morphology of cultured secretory cells in different states of activity, as observed by scanning electron microscopy. The anterior pituitary cells in monolayer culture offer an unique system to study the modifications of cell conformation in relation with changes of activity since these cells can be specifically modulated by stimulating or inhibiting factors. Scanning electron microscopy of anterior pituitary cells in primary culture was thus performed in different states of secretory activity. Adult female Sprague-Dawley rats at random stage of the estrous cycle, were used for the preparation of the primary cultures of anterior pituitary cells as previously described (Endocrinology 98: 1528, 1976). The cells 7. 5 x 105 in 1. 5 ml of Dulbecco's modified Eagle's medium containing 10% horse serum and 0. 25% foetal calf serum were plated in 3. 5 x 10 mm Petri dishes and were used six days after plating.

scholarly journals A study of acid phosphatase and dipeptidyl aminopeptidase II in monodispersed anterior pituitary cells using flow cytometry and electron microscopy.

1979 ◽  
Vol 27 (11) ◽  
pp. 1499-1504 ◽  
Author(s):  
R E Smith ◽  
P N Dean
Keyword(s):  
Electron Microscopy ◽  
Flow Cytometry ◽  
Acid Phosphatase ◽  
Anterior Pituitary ◽  
Single Cells ◽  
Fluorescent Microscopy ◽  
Historical Review ◽  
Pituitary Cells ◽  
Anterior Pituitary Cells ◽  
Dipeptidyl Aminopeptidase

A brief historical review of cytoenzymology is presented from the time of introduction into electron microscopy to the present, where the direction for quantification of an enzyme in single cells appears most promising by fluorescent staining. First attempts are reported to quantitate acid phosphatase (AcPase) and dipeptidyl aminopeptidase II (DAP-II) in monodispersed anterior pituitary cells from lactating and postlactating rats by flow cytometry, fluorescent, and electron microscopy. 3-Hydroxy-flavone is introduced as a new fluorescent cytochemical stain for AcPase, useful in flow cytometry but of only limited use in fluorescent microscopy. Histograms for AcPase indicate a single peak of cells staining more intensely in cell preparations from postlactating over lactating animals. Histograms for DAP-II staining indicate two distinct populations of cells present in the lactating and only one in the postlactating rat anterior pituitary gland. The application of dual laser staining indicates that not all cells stain for both enzymes. Electron microscopy shows the subcellular localization of DAP-II to be limited to lytic bodies and in mammotrophic cells to some secretion granules.

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