Electron histochemistry of thiamine pyrophosphatase activity in the neuronal Golgi apparatus observed after axotomy and transneuronal deprivation

1975 ◽  
Vol 36 (2) ◽  
pp. 123-141 ◽  
Author(s):  
I. L�szl� ◽  
Elizabeth Knyih�r
Keyword(s):  
Golgi Apparatus ◽  
Electron Histochemistry ◽  
Thiamine Pyrophosphatase ◽  
Pyrophosphatase Activity

Intracellular digestion and cellular defecation in a monogenean, Diclidophora merlangi

Parasitology ◽  
1975 ◽  
Vol 70 (3) ◽  
pp. 331-340 ◽  
Author(s):  
D. W. Halton
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Digestive Enzymes ◽  
Host Protein ◽  
Blood Proteins ◽  
Host Fish ◽  
Intracellular Digestion ◽  
Thiamine Pyrophosphatase ◽  
Lysosomal System ◽  
Pyrophosphatase Activity

The ultrastructural and cytochemical changes accompanying intracellular digestion and cellular defecation in the haematin cell of Diclidophora merlangi have been described. Blood proteins of the host-fish are sequestered by endocytosis and degraded within an interconnecting network of channels that form an integral, but changing, part of the cell. The digestive enzymes involved originate in the granular endoplasmic reticulum and are packaged in the Golgi apparatus and transferred to the channels in Golgi vesicles. The rate of haemoglobin absorption and the activity of the Golgi, as judged by vesicle counts and staining intensities for thiamine pyrophosphatase activity, are stimulated by the introduction of host protein into the gut lumen. The haematin residues of digestion are extruded periodically into the lumen by exocytosis involving membrane fusion. The process is a continuous one and, in worms starved of food, can result in the complete evacuation of pigment from the cell. It is suggested that a lysosomal system operates in the digestive cycle of the haematin cell.

scholarly journals AN ULTRACYTOCHEMICAL AND ULTRASTRUCTURAL STUDY OF EPITHELIAL CELLS IN DUCTULI EFFERENTES OF CHINESE HAMSTER

1971 ◽  
Vol 19 (12) ◽  
pp. 766-774 ◽  
Author(s):  
MASAO YOKOYAMA ◽  
JEFFREY P. CHANG
Keyword(s):  
Epithelial Cells ◽  
Golgi Apparatus ◽  
Phosphatase Activity ◽  
Plasma Membranes ◽  
Chinese Hamster ◽  
Fluid Composition ◽  
Ciliated Cells ◽  
Efferent Duct ◽  
Thiamine Pyrophosphatase ◽  
Pyrophosphatase Activity

Ultrastructural and ultracytochemical features of the efferent duct of Chinese hamster have been studied. The ducts are composed of two main types of epithelial cells, ciliated and nonciliated. Distinct structural and cytochemical characteristics of these cells are apparent. Presence of fibrogranular complex which is supposedly related to basal body replication was demonstrated in ciliated cells for the first time in this tissue. Thiamine pyrophosphatase activity in Golgi apparatus, acid phosphatase activity in Golgi apparatus and lysosomes and alkaline phosphatase activity on basal plasma membranes of both ciliated and nonciliated cells have been localized. However, thiamine pyrophosphatase activity was seen only on the luminal surface, apical vacuole and apical tubular structure of nonciliated cells but not on the surface of ciliated cells. Similarly, horseradish peroxidase was absorbed only by nonciliated cells. The cytochemical and ultrastructural differences between the two types of cells indicate a functional specialization. The results indicate that the ciliated cells are concerned with the transportation of the sperms and that the nonciliated cells are concerned with the regulation of fluid composition in the duct since the latter are capable of both secretion and absorption.

Phosphatases in the Neurones of Locusta Migratoria

1963 ◽  
Vol s3-104 (68) ◽  
pp. 475-481
Author(s):  
ROSEMARY S. LEE
Keyword(s):  
Electron Microscope ◽  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Acid Phosphatase Activity ◽  
Locusta Migratoria ◽  
Frozen Sections ◽  
Thiamine Pyrophosphatase ◽  
Motor Neurones ◽  
Membrane Bound ◽  
Pyrophosphatase Activity

Frozen sections of motor neurones in the thoracic ganglia of Locusta migratoria were treated for thiamine pyrophosphatase activity and for acid phosphatase activity. The TPPase-positive bodies range from 0.5 to 1.25 µ diameter and appear to be the small, membrane-bound inclusions described by Ashhurst and Chapman (1962) in their electron-microscope work; these are the smaller lipochondria of Shafiq (1953). The acid-phosphatase-positive bodies range from 1 to 2.5 µ, diameter and seem to be the lamellar aggregates described by Ashhurst and Chapman that are very similar to γ-cytomembranes, and which are the larger lipochondria of Shafiq. It is concluded that the enzyme content of the γ-cytomembranes is very different in this cell from their content in the vertebrate neurone, and doubt is thrown on the usefulness of TPPase activity as a marker for the Golgi apparatus in invertebrate tissue.

scholarly journals ISOLATION OF A GOLGI APPARATUS-RICH FRACTION FROM RAT LIVER

1970 ◽  
Vol 44 (3) ◽  
pp. 492-500 ◽  
Author(s):  
R. D. Cheetham ◽  
D. James Morré ◽  
Wayne N. Yunghans
Keyword(s):  
Endoplasmic Reticulum ◽  
Uric Acid ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Rat Liver ◽  
Succinic Dehydrogenase ◽  
Acid Oxidase ◽  
Enzyme Substrate ◽  
Thiamine Pyrophosphatase ◽  
Cell Fractions

Enzymatic activities associated with Golgi apparatus-, endoplasmic reticulum-, plasma membrane-, mitochondria-, and microbody-rich cell fractions isolated from rat liver were determined and used as a basis for estimating fraction purity. Succinic dehydrogenase and cytochrome oxidase (mitochondria) activities were low in the Golgi apparatus-rich fraction. On the basis of glucose-6-phosphatase (endoplasmic reticulum) and 5'-nucleotidase (plasma membrane) activities, the Golgi apparatus-rich fraction obtained directly from sucrose gradients was estimated to contain no more than 10% endoplasmic reticulum- and 11% plasma membrane-derived material. Total protein contribution of endoplasmic reticulum, mitochondria, plasma membrane, microbodies (uric acid oxidase), and lysosomes (acid phosphatase) to the Golgi apparatus-rich fraction was estimated to be no more than 20–30% and decreased to less than 10% with further washing. The results show that purified Golgi apparatus fractions isolated routinely may exceed 80% Golgi apparatus-derived material. Nucleoside di- and triphosphatase activities were enriched 2–3-fold in the Golgi apparatus fraction relative to the total homogenate, and of a total of more than 25 enzyme-substrate combinations reported, only thiamine pyrophosphatase showed a significantly greater enrichment.

scholarly journals A mitotic form of the Golgi apparatus in HeLa cells

1987 ◽  
Vol 104 (4) ◽  
pp. 865-874 ◽  
Author(s):  
JM Lucocq ◽  
JG Pryde ◽  
EG Berger ◽  
G Warren
Keyword(s):  
Golgi Apparatus ◽  
Hela Cells ◽  
Dense Matrix ◽  
Tubular Structures ◽  
Serial Sectioning ◽  
Interphase Cells ◽  
Thiamine Pyrophosphatase ◽  
Multiple Copies ◽  
Lowicryl K4m ◽  
Electron Lucent

Galactosyltransferase, a marker for trans-Golgi cisternae in interphase cells, was localized in mitotic HeLa cells embedded in Lowicryl K4M by immunoelectron microscopy. Specific labeling was found only over multivesicular structures that we term Golgi clusters. Unlike Golgi stacks in interphase cells, these clusters lacked elongated cisternae and ordered stacking of their components but did comprise two distinct regions, one containing electron-lucent vesicles and the other, smaller, vesiculo-tubular structures. Labeling for galactosyltransferase was found predominantly over the latter region. Both structures were embedded in a dense matrix that excluded ribosomes and the cluster was often bounded by cisternae of the rough endoplasmic reticulum, sometimes on all sides. Clusters were present at all stages of mitosis examined, which included prometaphase, metaphase, and telophase. They were also identified in conventionally processed mitotic cells and shown to contain another trans-Golgi marker, thiamine pyrophosphatase. Serial sectioning showed that clusters were discrete and globular and multiple copies appeared to be dispersed in the cytoplasm. Their possible role in the division of the Golgi apparatus is discussed.

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