scholarly journals The neuronal endoplasmic reticulum: its cytochemistry and contribution to the endomembrane system. I. Cell bodies and dendrites.

1983 ◽  
Vol 31 (9) ◽  
pp. 1077-1088 ◽  
Author(s):  
R D Broadwell ◽  
A M Cataldo
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Cell Types ◽  
Endomembrane System ◽  
Cell Organelles ◽  
Electron Microscopic ◽  
Enzyme Cytochemistry ◽  
G6pase Activity ◽  
Numerous Cell ◽  
Intracellular Compartments

The endoplasmic reticulum (ER) and its contribution to the endomembrane system (i.e., membranes of cell organelles) in the neuron have been investigated in brains of mice by applying electron microscopic enzyme cytochemistry for demonstration of glucose-6-phosphatase (G6Pase) activity. The phosphohydrolytic activity of G6Pase is a well-known cytochemical marker for the ER in numerous cell types. Of the different substrates employed, glucose-6-phosphate and mannose-6-phosphate were the only two with which G6Pase reaction product was seen in the neuronal ER and organelles related morphologically to the ER. G6Pase activity in cell bodies and dendrites was localized consistently within the lumen of the nuclear envelope, rough and smooth ER, lamellar bodies, hypolemmal and subsurface cisternae, and frequently in the cis saccules of the Golgi apparatus. The G6Pase reactive ER appeared as a network of saccules and tubules pervading the cell body and its dendrites. Possible membrane continuities were identified between the ER and the other reactive structures, including the cis half of the Golgi apparatus. Neither G6Pase activity nor reactive ER was associated with the trans Golgi saccules or GERL. G6Pase activity thus serves as a reliable marker for the perikaryal and dendritic ER and related structures. These observations support the theory that the ER is an integral component of the neuronal endomembrane system associated with the transfer of membrane or membrane molecules among intracellular compartments, the packaging and transport of exportable protein, and energy metabolism. G6Pase activity in the ER of axons and terminals is considered in detail in part two of this study.

Spermatogenesis in the Dragonfly with Particular Reference to the Cytoplasmic Organelles

1972 ◽  
Vol 30 ◽  
pp. 110-111
Author(s):  
Sant S. Sekhon
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Mature Sperm ◽  
Electron Microscopic ◽  
Cytoplasmic Organelles ◽  
Microscopic Studies ◽  
Insect Sperm ◽  
Large Round

Although there have been numerous studies concerning the morphogenetic changes accompanying the maturation of insect sperm, only a few deal with the sperm differentiation in the dragonflies. In two recent electron microscopic studies Kessel, has comprehensively treated the erlationship of microtubules to the nucleus and mid-piece structures during spermiogenesis in the dragonfly. The purpose of this study is to follow the sequential nuclear and cytoplasmic changes which accompany the differentiation of spermatogonium into a mature sperm during spermatogenesis in the dragonfly (Aeschna sp.).The dragonfly spermatogonia are characterized by large round nuclei. Loosely organized chromatin is usually unevenly distributed within the spermatogonial nuclei. The scant cytoplasm surrounding the nucleus contains mitochondria, the Golgi apparatus, elements of endoplasmic reticulum and numerous ribosomes (Fig. 1).

Altered labelling of the cell surface and intracellular organelles with [3H]mannose in enucleated amoebae

1984 ◽  
Vol 68 (1) ◽  
pp. 83-94
Author(s):  
C.J. Flickinger
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Cell Surface ◽  
Rough Endoplasmic Reticulum ◽  
Intracellular Transport ◽  
Cell Organelles ◽  
Intracellular Organelles ◽  
And Control ◽  
Kinetics Of ◽  
Heavy Labelling

The production, transport, and disposition of material labelled with [3H]mannose were studied in microsurgically enucleated and control amoebae. Cells were injected with the precursor and samples were prepared for electron-microscope radioautography at intervals, up to 24 h later. Control cells showed heavy labelling of the rough endoplasmic reticulum and the Golgi apparatus at early intervals after injection. Later, labelling of groups of small vesicles increased, and the percentage of grains over the cell surface peaked 12 h after administration of the precursor. Two major changes were detected in enucleate amoebae. First, the kinetics of labelling of cell organelles with [3H]mannose were altered in the absence of the nucleus. The Golgi apparatus and cell surface both displayed maximal labelling at later intervals in enucleates, and the percentage of grains over the rough endoplasmic reticulum varied less with time in enucleated than in control cells. Second, the distribution of radioactivity was altered. A greater percentage of grains was associated with lysosomes in enucleates than in control cells. The change in the kinetics of labelling of the endoplasmic reticulum, Golgi apparatus and cell surface indicates that intracellular transport of surface material was slower in the absence of the nucleus. It is suggested that this is related to the decreased motility of enucleate cells.

scholarly journals Cytochemical staining of the endoplasmic reticulum and glycogen in mouse anterior pituitary cells.

1984 ◽  
Vol 32 (12) ◽  
pp. 1285-1294 ◽  
Author(s):  
A M Cataldo ◽  
R D Broadwell
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Anterior Pituitary ◽  
Cell Types ◽  
Pituitary Cells ◽  
Cytochemical Staining ◽  
Anterior Pituitary Cells ◽  
G6pase Activity ◽  
Pituitary Glands ◽  
Glycogen Particles

The endoplasmic reticulum (ER) and glycogen in secretory cells of anterior pituitary glands from control and fasted mice were investigated ultrastructurally using cytochemical staining techniques. Potential enzyme cytochemical markers for the ER included glucose-6-phosphatase (G6Pase) and nucleoside diphosphatase (NDPase) activities. Presumptive glycogen particles were identified in tissue postfixed in 1% osmium tetroxide-1.5% potassium ferrocyanide or in ultrathin sections poststained with periodic acid-thiocarbohydrazide-silver proteinate. The ER appeared to be related structurally and cytochemically to the nuclear envelope and cis Golgi saccules. Similar relationships between the ER and the trans Golgi saccules or GERL were not observed. In anterior pituitary glands from control mice, G6Pase activity was prominent within the lumen of the ER, nuclear envelope, and cis Golgi saccules of all cells; reaction product was absent in the trans Golgi saccules and in GERL. G6Pase activity was sparse to non-existent in anterior pituitary cells from fasted mice. The cytochemical reaction utilizing the Gomori lead capture method indicated that G6Pase in anterior pituitary cells may function as a phosphohydrolase for converting glucose-6-phosphate to glucose. Cytochemical localization of NDPase activity was not evident in the ER; reaction product was localized consistently in one or two trans Golgi saccules and occasionally in GERL and nascent secretory granules. Presumptive glycogen particles in each of the different secretory cell types from control mice appeared as 20-30 nm wide, electron-dense particles scattered as single entities throughout the cytoplasm. Anterior pituitary glands from fasted mice exhibited conspicuous and numerous clumps of glycogen particles in addition to scattered particles in all cell types except corticotrophs, which appeared to be devoid of glycogen. Glycogen particles were absent in anterior pituitary cells incubated in a medium containing diastase. Our results suggest that in anterior pituitary cells of the mouse: 1) the phosphohydrolytic activity of G6Pase is a reliable cytochemical marker for the ER; 2) the ER is associated morphologically and cytochemically with the cis face but not with the trans face of the Golgi apparatus or with GERL; 3) some glucose-6-phosphate, a possible substrate for G6Pase in vivo, may be derived indirectly from glycogen stores; and 4) modulations in G6Pase activity and glycogen storage during fasting may reflect an alteration in energy metabolism.

scholarly journals Cytochemical localization of glucose-6-phosphatase activity in cerebral endothelial cells.

1983 ◽  
Vol 31 (6) ◽  
pp. 818-822 ◽  
Author(s):  
R D Broadwell ◽  
A M Cataldo ◽  
M Salcman
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Glucose Metabolism ◽  
Cell Types ◽  
Brain Parenchyma ◽  
Free Medium ◽  
Cytochemical Localization ◽  
Cerebral Endothelial Cells ◽  
G6pase Activity ◽  
Cerebral Microvasculature

Glucose-6-phosphatase (G6Pase) activity, with glucose-6-phosphate and mannose-6-phosphate as substrates, was examined by cytochemistry in capillary and arteriole endothelial cells of the mouse brain. G6Pase activity was observed ultrastructurally in the lumen of the nuclear envelope and endoplasmic reticulum (ER) of these cells. The reactive ER and nuclear membrane appeared to be in continuity. Nucleoside diphosphatase activity, also a marker for the ER in some cell types, was not seen within the ER of the cerebral microvasculature. The ER of arterioles and capillaries did not bind lead nonspecifically when incubated in a substrate-free medium. Speculation is raised concerning the involvement of G6Pase in glucose metabolism of cerebral endothelial cells and in making blood-borne glucose available to brain parenchyma.

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.

scholarly journals Controlled Signaling—Insulin-Like Growth Factor Receptor Endocytosis and Presence at Intracellular Compartments

2021 ◽  
Vol 11 ◽  
Author(s):  
Leonie Rieger ◽  
Rosemary O’Connor
Keyword(s):  
Golgi Apparatus ◽  
Cancer Cells ◽  
Growth Factor Receptor ◽  
Cell Types ◽  
Specific Cell ◽  
Receptor Endocytosis ◽  
Intracellular Compartments ◽  
Associated Proteins ◽  
Membrane Compartments ◽  
And Function

Ligand-induced activation of the IGF-1 receptor triggers plasma-membrane-derived signal transduction but also triggers receptor endocytosis, which was previously thought to limit signaling. However, it is becoming ever more clear that IGF-1R endocytosis and trafficking to specific subcellular locations can define specific signaling responses that are important for key biological processes in normal cells and cancer cells. In different cell types, specific cell adhesion receptors and associated proteins can regulate IGF-1R endocytosis and trafficking. Once internalized, the IGF-1R may be recycled, degraded or translocated to the intracellular membrane compartments of the Golgi apparatus or the nucleus. The IGF-1R is present in the Golgi apparatus of migratory cancer cells where its signaling contributes to aggressive cancer behaviors including cell migration. The IGF-1R is also found in the nucleus of certain cancer cells where it can regulate gene expression. Nuclear IGF-1R is associated with poor clinical outcomes. IGF-1R signaling has also been shown to support mitochondrial biogenesis and function, and IGF-1R inhibition causes mitochondrial dysfunction. How IGF-1R intracellular trafficking and compartmentalized signaling is controlled is still unknown. This is an important area for further study, particularly in cancer.

Effect of different colchicine concentrations on microtubules and membranes in tomato root tip cells

1988 ◽  
Vol 46 ◽  
pp. 306-307
Author(s):  
T.E. Jensen
Keyword(s):  
Plasma Membrane ◽  
Phosphate Buffer ◽  
Cell Types ◽  
Root Tip ◽  
Distilled Water ◽  
Root Tips ◽  
Cell Organelles ◽  
Tomato Root ◽  
Thin Sections ◽  
Numerous Cell

The effect of colchicine on microtubules has been investigated in numerous cell types. In this present study we have used different concentrations of colchicine to determine if the two major groups of microtubules in plant cells, plasma membrane associated and mitotic, are differentially sensitive to this drug.Tomato seeds “Michigan forcing” were germinated on filter paper saturated with distilled water. Radicles 1.5 to 2.0cm were selected and placed into either distilled water or colchicine, 0.001, 0.01, 0.03, 0.04, 0.05, 0.1%, for 20 hrs. During this time they were kept at 20°C in dim light. Root tips were fixed in 3% glutaraldehyde in phosphate buffer at pH7.2 for lh at 4°C. After 5 rinses in buffer they were placed in 1% OsO4 in phosphate buffer at pH7.2 for 1h at 4°C. Root tips were then dehydrated in ethanol, treated with propylene and embedded in Epon.No growth occurred in any of the colchicine treated radicles. Observation of thin sections of control cells revealed many plasma membrane associated microtubules, many cells in division stages and the usual arrangement of cell organelles.

Phosphatases and Differentiation of the Golgi Apparatus

1969 ◽  
Vol 4 (2) ◽  
pp. 455-497
Author(s):  
MARIANNE DAUWALDER ◽  
W. G. WHALEY ◽  
JOYCE E. KEPHART
Keyword(s):  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Smooth Endoplasmic Reticulum ◽  
Cell Types ◽  
Root Tip ◽  
Morphological Development ◽  
Electron Microscopic ◽  
Reaction Specificity ◽  
The Face ◽  
Inosine Diphosphatase

Cytochemical techniques for the electron microscopic localization of inosine diphosphatase, thiamine pyrophosphatase, and acid phosphatase have been applied to the developing root tip of Zea mays. Following formaldehyde fixation the Golgi apparatus of most of the cells showed reaction specificity for IDPase and TPPase. Following glutaraldehyde fixation marked localization of IDPase reactivity in the Golgi apparatus was limited to the root cap, the epidermis, and the phloem. A parallelism was apparent between the sequential morphological development of the apparatus for the secretion of a polysaccharide product, the fairly direct incorporation of tritiated glucose into the apparatus to become a component of this product and the development of the enzyme reactivity. Acid phosphatase, generally accepted as a lysosomal marker, was found in association with the Golgi apparatus in only a few cell types near the apex of the root. The localization was usually in a single cisterna at the face of the apparatus toward which the production of secretory vesicles builds up and associated regions of what may be smooth endoplasmic reticulum. Since the cell types involved were limited regions of the cap and epidermis and some initial cells, no functional correlates of the reactivity were apparent. Despite the presence of this lysosomal marker, no structures clearly identifiable as ‘lysosomes’ were found and the lack of reaction specificity in the vacuoles did not allow them to be so defined.

scholarly journals Large granular lymphocytes in human peripheral blood: ultrastructural and cytochemical characterization of the granules

Blood ◽  
1982 ◽  
Vol 59 (2) ◽  
pp. 277-283 ◽  
Author(s):  
CE Grossi ◽  
A Cadoni ◽  
A Zicca ◽  
A Leprini ◽  
M Ferrarini
Keyword(s):  
Golgi Apparatus ◽  
Peripheral Blood ◽  
Mononuclear Cells ◽  
Human Peripheral Blood ◽  
Single Cells ◽  
Cell Types ◽  
Large Granular Lymphocytes ◽  
Enzyme Cytochemistry ◽  
Acetate Esterase ◽  
Granular Lymphocytes

Abstract Large granular lymphocytes (LGL) are defined as nonadherent mononuclear cells with cytoplasmic azurophilic granules, avid receptors for the Fc portion of IgG, and cytotoxic functions (NK or ADCC activities). In the present study, the granules of LGL isolated from human peripheral blood have been analyzed by enzyme cytochemistry and electron microscopy. It had been found that: (1) in the single cells, granules at different stages of maturation could be detected: in addition, packaging of the granules took place in the proximity of the Golgi apparatus, which is similar to that seen in secretory cell types. (2) Acid phosphatase (AP) was observed within the granules and the vesicles located in the Golgi area: the Golgi apparatus identified through its thiamine pyrophosphatase-positivity was consistently negative for AP. (3) Alpha naphthyl-acetate esterase (ANAE) activity was localized in the granules as well as on the membrane of LGL and monocytes. (4) The ANAE activity of LGL was of the monocytic and not of the lymphocytic type, as shown by NaF inhibition. (5) The LGL granules, although identifiable as primary lysosomes, were not involved in the process of phagocytosis, since LGL failed consistently to ingest latex particles or opsonized red cells.

Sign in / Sign up

Export Citation Format

Share Document