Demonstration of acid phosphatase activity in the golgi apparatus of the jejunal epithelium cell in patients with idiopathic steatorrhea

1965 ◽  
Vol 5 (2) ◽  
pp. 182-184 ◽  
Author(s):  
E. O. Riecken ◽  
A. G. E. Pearse
1962 ◽  
Vol 15 (2) ◽  
pp. 289-312 ◽  
Author(s):  
Edward Essner ◽  
Alex B. Novikoff

The Reuber hepatoma H-35 and Morris hepatoma 5123 have been studied by electron microscopy and by cytochemical staining methods for a number of phosphatases. These studies emphasize the resemblances of the two tumors to rat liver, but they also indicate distinctive features in each of the three tissues. Secretory product accumulates within the cisternae of the Golgi apparatus that dilate to form the Golgi vacuoles. The vacuoles apparently separate, and secretory material undergoes further condensation within them. These "secretory vacuoles" possess acid phosphatase activity and may thus be considered lysosomes. The membranes of the Golgi apparatus are without acid phosphatase activity but show high levels of thiaminepyrophosphatase activity. The endoplasmic reticulum also hydrolyzes thiaminepyrophosphate but at a lower rate; it hydrolyzes the diphosphates of uridine, guanosine, and inosine rapidly. These observations and the electron microscopic images are consistent with the view that the cytomembranes are in a dynamic state of flux, movement, and transformation in the living cell, and that smooth surfaced derivatives of the endoplasmic reticulum become refashioned into the Golgi membranes as the Golgi membranes are being refashioned into those that delimit secretory vacuoles. The variations encountered in the two hepatomas are described. The electron microscope literature dealing with the relations of the Golgi apparatus to secretory granules, on the one hand, and the endoplasmic reticulum, on the other, is reviewed briefly.


1969 ◽  
Vol 17 (1) ◽  
pp. 23-29 ◽  
Author(s):  
JOHAN F. JONGKIND

The activities of nucleoside diphosphatases and thiamine pyrophosphatase (TPPase) that are associated with the Golgi apparatus and acid phosphatase were measured by quantitative histochemical methods both in histologically pure nucleus supraopticus and in an adjacent area of the anterior hypothalamus of the rat. In the nucleus supraopticus UDP-phosphohydrolase (UDPase), GDP-phosphohydrolase (GDPase) and TPPase activities increased 40% after a thirsting period of 3 days, while IDP-phosphohydrolase activity increased 18% and acid phosphatase activity decreased 25% after the same osmostic stress. The adjacent, nonsupraoptic anterior hypothalamic area did not show significant changes in activity of any of the enzymes studied. The activities of the Golgi-associated TPPase, UDPase and GDPase are likely to be reliable parameters for neurosecretory activity.


Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent

Hemolytic anemias were produced in rats by administering phenylhydrazine or anti-erythrocytic (rooster) serum, the latter having agglutinin and hemolysin titers exceeding 1:1000.Following administration of phenylhydrazine, the erythrocytes undergo oxidative damage and are removed from the circulation by the cells of the reticulo-endothelial system, predominantly by the spleen. With increasing dosage or if animals are splenectomized, the Kupffer cells become an important site of sequestration and are greatly hypertrophied. Whole red cells are the most common type engulfed; they are broken down in digestive vacuoles, as shown by the presence of acid phosphatase activity (Fig. 1). Heinz body material and membranes persist longer than native hemoglobin. With larger doses of phenylhydrazine, erythrocytes undergo intravascular fragmentation, and the particles phagocytized are now mainly red cell fragments of varying sizes (Fig. 2).


1979 ◽  
Vol 88 (5) ◽  
pp. 363-365 ◽  
Author(s):  
P Aruna ◽  
C Sreeramulu Chetty ◽  
R Chandramohan Naidu ◽  
K S Swami

2008 ◽  
Vol 39 (6) ◽  
pp. 627-634 ◽  
Author(s):  
Tatiana Salles de Souza Malaspina ◽  
Célio Xavier dos Santos ◽  
Ana Paula Campanelli ◽  
Francisco Rafael Martins Laurindo ◽  
Mari Cleide Sogayar ◽  
...  

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