Effect of desympathization on development of adaptive and compensatory reactions of the thyroid C-cells apparatus and adrenal chromaffin cells in young rats

1991 ◽  
Vol 111 (6) ◽  
pp. 880-883 ◽  
Author(s):  
S. N. Ryashchikov ◽  
V. N. Markov ◽  
V. A. Glumova ◽  
M. Yu. Murashova ◽  
A. S. Elkin ◽  
...  
1985 ◽  
Vol 33 (8) ◽  
pp. 791-798 ◽  
Author(s):  
J A Nolan ◽  
J Q Trojanowski ◽  
R Hogue-Angeletti

Gel-eluted bovine chromogranin (CG), the 75,000 dalton acidic protein abundantly present in adrenal chromaffin granules, was used as immunogen to prepare anti-CG serum. The specificity of the antiserum was demonstrated in immunoblots of electrophoresed bovine CG and in immunohistochemical studies of bovine adrenal medulla. In the immunoblots, the predominant immunoreactive band had a molecular weight of 75,000 daltons. Bands with a higher or lower molecular weight were also immunoreactive and may represent CG precursors or breakdown products. In the adrenal gland, only adrenal chromaffin cells contained CG immunoreactivity. Immunoblots and immunohistochemistry were also used to characterize the distribution of CG in bovine tissues. CG was expressed by cells of the diffuse neuroendocrine system (DNS) including: adrenal chromaffin cells, enterochromaffin cells, pancreatic islet cells, cells of the adenohypophysis, thyroid C cells, parathyroid cells, and submandibular gland. CG was also seen in four locations not previously recognized to express this antigen: thymic epithelial cells, neurons, the inner segment of rods and cones, and the submandibular gland. We demonstrate a wider distribution of CG than previously recognized and that the molecule detected in tissue by immunohistochemistry is indeed CG. We conclude that CG is expressed by neurons, cells of the DNS, and by a few other cells that may or may not be related to the DNS. The antiserum described here should prove valuable in developing an understanding of the function(s) of CG.


Author(s):  
Joe A. Mascorro ◽  
Robert D. Yates

Extra-adrenal chromaffin organs (abdominal paraganglia) constitute rich sources of catecholamines. It is believed that these bodies contain norepinephrine exclusively. However, the present workers recently observed epinephrine type granules in para- ganglion cells. This report investigates catecholamine containing granules in rabbit paraganglia at the ultrastructural level.New Zealand white rabbits (150-170 grams) were anesthetized with 50 mg/kg Nembutal (IP) and perfused with 3% glutaraldehyde buffered with 0.2M sodium phosphate, pH 7.3. The retroperitoneal tissue blocks were removed and placed in perfusion fluid for 4 hours. The abdominal paraganglia were dissected from the blocks, diced, washed in phosphate buffer and fixed in 1% osmic acid buffered with phosphate. In other animals, the glutaraldehyde perfused tissue blocks were immersed for 1 hour in 3% glutaraldehyde/2.5% potassium iodate buffered as before. The paraganglia were then diced, separated into two vials and washed in the buffer. A portion of this tissue received osmic acid fixation.


1997 ◽  
Vol 73 ◽  
pp. 226
Author(s):  
Kazuo Minakuchi ◽  
Hitoshi Houchi ◽  
Masanori Yoshizumi ◽  
Yasuko Ishimura ◽  
Kyoji Morita ◽  
...  

1992 ◽  
Vol 284 (2) ◽  
pp. 321-326 ◽  
Author(s):  
G Ahnert-Hilger ◽  
U Wegenhorst ◽  
B Stecher ◽  
K Spicher ◽  
W Rosenthal ◽  
...  

1. In bovine adrenal chromaffin cells made permeable either to molecules less than or equal to 3 kDa with alphatoxin or to proteins less than or equal to 150 kDa with streptolysin O, the GTP analogues guanosine 5′-[beta gamma-imido]triphosphate (p[NH]ppG) and guanosine 5′-[gamma-thio]triphosphate (GTP[S]) differently modulated Ca(2+)-stimulated exocytosis. 2. In alphatoxin-permeabilized cells, p[NH]ppG up to 20 microM activated Ca(2+)-stimulated exocytosis. Higher concentrations had little or no effect. At a free Ca2+ concentration of 5 microM, 7 microM-p[NH]ppG stimulated exocytosis 6-fold. Increasing the free Ca2+ concentration reduced the effect of p[NH]ppG. Pretreatment of the cells with pertussis toxin prevented the activation of the Ca(2+)-stimulated exocytosis by p[NH]ppG. 3. In streptolysin O-permeabilized cells, p[NH]ppG did not activate, but rather inhibited Ca(2+)-dependent catecholamine release under all conditions studied. In the soluble cytoplasmic material that escaped during permeabilization with streptolysin O, different G-protein alpha-subunits were detected using an appropriate antibody. Around 15% of the cellular alpha-subunits were detected in the supernatant of permeabilized control cells. p[NH]ppG or GTP[S] stimulated the release of alpha-subunits 2-fold, causing a loss of about 30% of the cellular G-protein alpha-subunits under these conditions. Two of the alpha-subunits in the supernatant belonged to the G(o) type, as revealed by an antibody specific for G(o) alpha. 4. GTP[S], when present alone during stimulation with Ca2+, activated exocytosis in a similar manner to p[NH]ppG. Upon prolonged incubation, GTP[S], in contrast to p[NH]ppG, inhibited Ca(2+)-induced exocytosis from cells permeabilized by either of the pore-forming toxins. This effect was resistant to pertussin toxin. 5. The p[NH]ppG-induced activation of Ca(2+)-stimulated release from alphatoxin-permeabilized chromaffin cells may be attributed to one of the heterotrimeric G-proteins lost during permeabilization with streptolysin O. The inhibitory effect of GTP[S] on exocytosis is apparently not mediated by G-protein alpha-subunits, but by another GTP-dependent process still occurring after permeabilization with streptolysin O.


2008 ◽  
Vol 107 (3) ◽  
pp. 658-667 ◽  
Author(s):  
Chien-Yuan Pan ◽  
Ling-Ling Tsai ◽  
Jhih-Hang Jiang ◽  
Lih-Woan Chen ◽  
Lung-Sen Kao

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