False localization of acid phosphatase activity in the nuclear envelope and endoplasmic reticulum of peritoneal macrophages

1985 ◽  
Vol 17 (2) ◽  
pp. 235-241 ◽  
Author(s):  
E. C. M. Hoefsmit ◽  
I. L. Eestermans ◽  
C. Korn ◽  
P. Van Duijn
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Nuclear Envelope ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Peritoneal Macrophages

scholarly journals CYTOLOGICAL STUDIES ON TWO FUNCTIONAL HEPATOMAS

1962 ◽  
Vol 15 (2) ◽  
pp. 289-312 ◽  
Author(s):  
Edward Essner ◽  
Alex B. Novikoff
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Secretory Granules ◽  
Dynamic State ◽  
Secretory Product ◽  
Electron Microscopic ◽  
Golgi Membranes

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.

Cellular mechanisms of periostracum formation in Physa spp. (Mollusca: Pulmonata)

1978 ◽  
Vol 56 (11) ◽  
pp. 2299-2311 ◽  
Author(s):  
G. M. Jones ◽  
A. S. M. Saleuddin
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rough Endoplasmic Reticulum ◽  
Acid Phosphatase Activity ◽  
Homogeneous Material ◽  
Cellular Mechanisms ◽  
Phenoloxidase Activity ◽  
Enzyme Substrate ◽  
Mantle Edge

The periostracum comprises an external lamella, 13 nm thick, and one sublamellar layer. Periostracal cells secrete the lamella as preformed periostracal units. The mantle edge gland (meg) produces most of the sublamellar layer. A sequence of formation of periostracal units within the periostracal cells is suggested. Homogeneous inclusions, possibly Golgi derived, fuse into larger, irregular inclusions. Within these inclusions, three-layered membranes, 7 nm thick, arise from the homogeneous material. The membranes fuse in pairs to form the five-layered, 13-nm periostracal units. Acid phosphatase activity has been localised al the surfaces of the periostracal units and might be involved in modifying the units prior to their discharge. Phenoloxidase and polyphenols have been localised in the meg, suggesting that this region is responsible for periostracal sclerotisation. Phenoloxidase activity is present in Golgi, rough endoplasmic reticulum, and apical secretory inclusions in cells in the anterior two-thirds of the meg. Polyphenols are present in apical secretory inclusions, particulary in three or four cells in the posterior meg. This distribution may suggest that phenoloxidase is incorporated into all levels of the sublamellar layer and that sclerotisation occurs subsequently when the enzyme substrate is presented.

Ébauches intracytoplasmiques de grains protéiques dans des cotylédons de Raphanus en développement

1986 ◽  
Vol 64 (12) ◽  
pp. 2887-2895
Author(s):  
Louis Genevès ◽  
Jacques Rutin
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rough Endoplasmic Reticulum ◽  
Early Phase ◽  
Acid Phosphatase Activity ◽  
Early Stage ◽  
Protein Bodies ◽  
Meristematic Cells ◽  
Size And Structure

Protein bodies were characterized at an early stage of their maturation in thin green cotyledons of developing radish embryos. They appeared as granules in the cytoplasm of meristematic cells. Their diameter (0.5 to 1 μm) was in the range of that of mitochondria. They were distinguished from vacuoles by their morphology, size, and structure. Some appeared to be associated with cisternae of endoplasmic reticulum or dictyosomes (permanganic fixations). Their evolution was synchronous in the cell and also in the cotyledonary tissue. Compact in appearance, they were constituted of thin packed fibrillar structures, limited by a denser peripheral layer. It is difficult to know whether or not they had a limiting membrane. Some possessed thin dense crystals or globoids (aldehydic fixations). During this early phase, several types of organelles seemed to contribute to the development of protein bodies, including saccules of rough endoplasmic reticulum and dictyosomes. Polyribosomes constituted a network around their surface. They did not exhibit any acid phosphatase activity. In this respect, they differed from the vacuoles, saccules of endoplasmic reticulum, and several neighbouring vesicles.

scholarly journals ELECTRON MICROSCOPIC LOCALIZATION OF GLYCOPROTEINS IN PITUITARY CELLS OF DUCK AND QUAIL

1971 ◽  
Vol 19 (12) ◽  
pp. 775-797 ◽  
Author(s):  
ANDRÉE TIXIER-VIDAL ◽  
RENÉE PICART
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Secretory Granules ◽  
Periodic Acid ◽  
Pituitary Cells ◽  
Electron Microscopic ◽  
Gonadotropic Cells ◽  
Dense Bodies

Structures demonstrating the presence of glycoproteins, acid phosphatase activity and OsO4 impregnation were localized by means of the electron microscope in duck and in quail pituitary cells. Two methods for the electron microscopic demonstration of glycoproteins were used: a chromic acid-phosphotungstic acid mixture on glycol-methacrylate-embedded tissues, and the periodic acid-thiocarbohydrazide-silver proteinate technique. Both methods showed glycoproteins in the following sites: ( a) the secretory granules in three types of cells (A, B, C) which are part of the seven different cells of the avian pituitary; ( b) the several kinds of dense bodies which are richer in reaction product than the secretory granules. A correlation with previous studies on similar species of birds is helpful in identifying each of the three positive types of cells as thyrotropic cell (A), prolactin cell (B) and gonadotropic cell (C). The presence of glycoproteins within the Golgi saccules (on condensing granules) was found with the periodic acid-thiocarbohydrazide-silver proteinate method in these gonadotropic cells only. In gonadotropic and thyrotropic cells, acid phosphatase activity is weak in the inner Golgi saccules and strong in the "Golgi Endoplasmic Reticulum Lysosomes" system, in the lysosomes, in the dense bodies and in the vacuolated dense bodies. The structures which are richest in glycoproteins are also those which have the most acid phosphatase activity. On the contrary, OsO4-stained structures in duck gonadotropic cells (nuclear pericisterna, rough endoplasmic reticulum, cisternae and outer Golgi saccules) have no glycoproteins or acid phosphatase activity.

Ultrastructure de I'érythrocyte du triton Pleurodeles waltlii Michah

1980 ◽  
Vol 58 (6) ◽  
pp. 1193-1199 ◽  
Author(s):  
K. E. Sean ◽  
B. Lassalle ◽  
B. Boilly
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Rough Endoplasmic Reticulum ◽  
Acid Phosphatase Activity ◽  
Condensed Chromatin ◽  
Pleurodeles Waltlii ◽  
Altered Form

The erythrocytes of the newt Pleurodeles wultlii Michah are characterized by the presence of DAB negative cytoplasmic autophagic-type vacuoles; these vacuoles have an intense acid phosphatase activity and are expelled by exocytosis. Golgi, rough endoplasmic reticulum, and mitochondria ate not well developed and generally present an altered form; the nucleus is characterized by condensed chromatin without pseudoperoxidase activity. These results suggest that the erythrocyte of Pleurodeles seems to have a low metabolism and to partly mature in the circulating blood.

Erythrophagocytosis in the Liver in Hemolytic Anemias

1968 ◽  
Vol 26 ◽  
pp. 184-185
Author(s):  
O. T. Minick ◽  
E. Orfei ◽  
F. Volini ◽  
G. Kent
Keyword(s):  
Acid Phosphatase ◽  
Oxidative Damage ◽  
Phosphatase Activity ◽  
Kupffer Cells ◽  
Acid Phosphatase Activity ◽  
Common Type ◽  
Red Cell ◽  
Cell Fragments ◽  
Reticulo Endothelial System ◽  
Important Site

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).

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