Continuities between outer nuclear membrane and the rough endoplasmic reticulum increase in hippocampal neurons during seizure-induced protein synthesis

1989 ◽  
Vol 497 (2) ◽  
pp. 387-392 ◽  
Author(s):  
Richard M. Pico ◽  
Christine Gall
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Hippocampal Neurons ◽  
Outer Nuclear Membrane

scholarly journals The eta isoform of protein kinase C is localized on rough endoplasmic reticulum.

1994 ◽  
Vol 14 (6) ◽  
pp. 3782-3790 ◽  
Author(s):  
K Chida ◽  
H Sagara ◽  
Y Suzuki ◽  
A Murakami ◽  
S Osada ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Mouse Skin ◽  
Endoplasmic Reticulum Membrane ◽  
Present Observation ◽  
Outer Nuclear Membrane ◽  
Kinase C

The eta isoform of protein kinase C, isolated from a cDNA library of mouse skin, has unique tissue and cellular distributions. It is predominantly expressed in epithelia of the skin, digestive tract, and respiratory tract in close association with epithelial differentiation. We report here that this isoform is localized on the rough endoplasmic reticulum in transiently expressing COS1 cells and constitutively expressing keratinocytes. By the use of polyclonal antibodies raised against peptides of the diverse D1 and D2/D3 regions, we found that immunofluorescent signals were strongest in the cytoplasm around the nucleus and became weaker toward the peripheral cytoplasm. Under immunoelectron microscopic examination, electron-dense signals were located on the rough endoplasmic reticulum and on the outer nuclear membrane which is continuous with the endoplasmic reticulum membrane. However, no signals were detected in the nucleus, inner nuclear membrane, smooth endoplasmic reticulum, Golgi apparatus, mitochondria, or plasma membrane. Treatment of the cells in situ with detergents suggested association of the isoform of protein kinase C with intracellular structures. By immunoblotting, a distinct single band with an M(r) of 80,000 was detected in whole-cell lysate and in rough microsomal and crude nuclear fractions, all of which contain outer nuclear membrane and/or rough endoplasmic reticulum. We further demonstrated the absence of a nuclear localization signal in the pseudosubstrate sequence. The present observation is not consistent with the report of Greif et al. (H. Greif, J. Ben-Chaim, T. Shimon, E. Bechor, H. Eldar, and E. Livneh, Mol. Cell. Biol. 12:1304-1311, 1992).

The eta isoform of protein kinase C is localized on rough endoplasmic reticulum

1994 ◽  
Vol 14 (6) ◽  
pp. 3782-3790
Author(s):  
K Chida ◽  
H Sagara ◽  
Y Suzuki ◽  
A Murakami ◽  
S Osada ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Mouse Skin ◽  
Endoplasmic Reticulum Membrane ◽  
Present Observation ◽  
Outer Nuclear Membrane ◽  
Kinase C

The eta isoform of protein kinase C, isolated from a cDNA library of mouse skin, has unique tissue and cellular distributions. It is predominantly expressed in epithelia of the skin, digestive tract, and respiratory tract in close association with epithelial differentiation. We report here that this isoform is localized on the rough endoplasmic reticulum in transiently expressing COS1 cells and constitutively expressing keratinocytes. By the use of polyclonal antibodies raised against peptides of the diverse D1 and D2/D3 regions, we found that immunofluorescent signals were strongest in the cytoplasm around the nucleus and became weaker toward the peripheral cytoplasm. Under immunoelectron microscopic examination, electron-dense signals were located on the rough endoplasmic reticulum and on the outer nuclear membrane which is continuous with the endoplasmic reticulum membrane. However, no signals were detected in the nucleus, inner nuclear membrane, smooth endoplasmic reticulum, Golgi apparatus, mitochondria, or plasma membrane. Treatment of the cells in situ with detergents suggested association of the isoform of protein kinase C with intracellular structures. By immunoblotting, a distinct single band with an M(r) of 80,000 was detected in whole-cell lysate and in rough microsomal and crude nuclear fractions, all of which contain outer nuclear membrane and/or rough endoplasmic reticulum. We further demonstrated the absence of a nuclear localization signal in the pseudosubstrate sequence. The present observation is not consistent with the report of Greif et al. (H. Greif, J. Ben-Chaim, T. Shimon, E. Bechor, H. Eldar, and E. Livneh, Mol. Cell. Biol. 12:1304-1311, 1992).

scholarly journals A Cellular Reaction to Antibody in Tissue Culture Studied with Electron Microscopy

1959 ◽  
Vol 5 (3) ◽  
pp. 405-410 ◽  
Author(s):  
Harrison Latta
Keyword(s):  
Electron Microscopy ◽  
Tissue Culture ◽  
Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Normal Serum ◽  
Butyl Methacrylate ◽  
Heart Cells ◽  
Plasma Clot ◽  
Outer Nuclear Membrane ◽  
Cell Components

The reaction of embryonic chick heart cells grown in tissue culture to specific guinea pig antiserum has been studied with electron microscopy. Heart fragments from chick embryos were cultured with a plasma clot. After being tested with antiserum or normal serum, they were fixed with buffered osmium tetroxide and embedded in butyl methacrylate before removal from the glass culture chamber. Thin cells found by phase microscopy to have reacted were sectioned in a plane parallel to the glass surface on which they had grown. The results confirm and extend observations made previously while the reactions were occurring. The plasma membrane, like that of the red cell, becomes disrupted or less resistant to trauma following the action of antiserum. The membranes of mitochondria and endoplasmic reticulum vesiculate and swell. Before nuclear shrinkage becomes prominent, the outer nuclear membrane separates over a large portion of the nuclear envelope and forms one or more large swollen blebs. Thus, the outer nuclear membrane shows a reactivity similar to endoplasmic reticulum. It is suggested that the various physical and chemical changes observed to follow the action of antibody and complement on fibroblasts may be explained by osmotic pressure differences between various cell components. Some basic similarities to the action of hemolytic agents on red cells are noted.

scholarly journals Endoplasmic reticulum-to-Golgi transitions upon herpes virus infection

F1000Research ◽  
2018 ◽  
Vol 6 ◽  
pp. 1804 ◽  
Author(s):  
Peter Wild ◽  
Andres Kaech ◽  
Elisabeth M. Schraner ◽  
Ladina Walser ◽  
Mathias Ackermann
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Golgi Complex ◽  
Nuclear Membrane ◽  
Progeny Virus ◽  
Cytoplasmic Matrix ◽  
Outer Nuclear Membrane ◽  
Nuclear Membranes ◽  
Perinuclear Space ◽  
Hsv 1

Background: Herpesvirus capsids are assembled in the nucleus, translocated to the perinuclear space by budding, acquiring tegument and envelope, or released to the cytoplasm via impaired nuclear envelope. One model proposes that envelopment, “de-envelopment” and “re-envelopment” is essential for production of infectious virus. Glycoproteins gB/gH were reported to be essential for de-envelopment, by fusion of the “primary” envelope with the outer nuclear membrane. Yet, a high proportion of enveloped virions generated from genomes with deleted gB/gH were found in the cytoplasm and extracellular space, suggesting the existence of alternative exit routes.Methods: We investigated the relatedness between the nuclear envelope and membranes of the endoplasmic reticulum and Golgi complex, in cells infected with either herpes simplex virus 1 (HSV-1) or a Us3 deletion mutant thereof, or with bovine herpesvirus 1 (BoHV-1) by transmission and scanning electron microscopy, employing freezing technique protocols.Results:  The Golgi complex is a compact entity in a juxtanuclear position covered by a membrane on thecisface. Golgi membranes merge with membranes of the endoplasmic reticulum forming an entity with the perinuclear space. All compartments contained enveloped virions. After treatment with brefeldin A, HSV-1 virions aggregated in the perinuclear space and endoplasmic reticulum, while infectious progeny virus was still produced.Conclusions: The data suggest that virions derived by budding at nuclear membranes are intraluminally transported from the perinuclear space via Golgi -endoplasmic reticulum transitions into Golgi cisternae for packaging. Virions derived by budding at nuclear membranes are infective like Us3 deletion mutants, which  accumulate in the perinuclear space. Therefore, i) de-envelopment followed by re-envelopment is not essential for production of infective progeny virus, ii) the process taking place at the outer nuclear membrane is budding not fusion, and iii) naked capsids gain access to the cytoplasmic matrix via impaired nuclear envelope as reported earlier.

The polypeptides of rat liver nuclear envelope. II. Comparison of rat liver nuclear membrane polypeptides with those of the rough endoplasmic reticulum

1980 ◽  
Vol 43 (1) ◽  
pp. 269-277
Author(s):  
J.C. Richardson ◽  
A.H. Maddy
Keyword(s):  
Endoplasmic Reticulum ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Relative Proportion ◽  
Membrane System ◽  
Membrane Systems ◽  
Nuclear Membranes ◽  
Cytoplasmic Surface ◽  
Triton X

Nuclear envelopes are separated into pore-lamina and membrane sub-fractions by extraction in 2.0% Triton X-100 followed by pelleting of the pore-laminae. The polypeptides of these subfractions are then compared with those from isolated rough endoplasmic reticulum. The dispositions of individual polypeptides in the cytoplasmic surface of nuclear envelopes and rought endoplasmic reticulum were studied by lactoperoxidase-catalysed iodination. These studies show that although the nuclear membranes exhibit several homologies with the Triton-soluble polypeptides of the rough endoplasmic reticulum the relative proportion of individual polypeptides within the two systems are very largely different. The cytoplasmic surfaces of the 2 membrane systems show only 2 obvious homologies at 105 000 and 15 000 mol. wt and the overall impression is that, at least in rat liver, the outer nuclear membrane is very substantially differentiated from rough endoplasmic reticulum. It is concluded that the nuclear membranes may not be regarded as a mere continuum of the endoplasmic reticulum, but should be seen as a highly specialized membrane system in their own right.

Ultrastructural Modifications in one Case of Hairy Cell Leukemia during Alpha-Interferon Therapy

1992 ◽  
Vol 78 (3) ◽  
pp. 190-197 ◽  
Author(s):  
Manrico Morroni ◽  
Giordano Ripa ◽  
Guido Bolognesi ◽  
Pietro Leoni ◽  
Saverio Cinti
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Hairy Cell Leukemia ◽  
Interferon Therapy ◽  
Close Contact ◽  
Hairy Cell ◽  
Cell Leukemia ◽  
Ultrastructural Modifications ◽  
Hairy Cells

There are many reports concerning the morphology of hairy cell leukemia (HCL), but, to our knowledge, there are no data on the ultrastructural modifications of HCL during interferon therapy. The ultrastructural modifications of neoplastic cells In peripheral blood in a case of HCL were investigated before and 2 and 4 months after beginning treatment with human lymphoblastoid alpha-interferon. Before therapy, hairy cells displayed the typical cytoplasmic projections, and 4 % contained ribosome-lamellae complexes (RLC) (the cells contained up to 7 RLC). Two months from the beginning of therapy, hairy cells had shorter projections, RLC had disappeared, and tubuloreticular structures (TRS) had appeared in 2.2 % of the elements. Four months from the beginning of therapy, TRS persisted in 2.3 % of hairy cells, cylindrical confronting cisternae (CCC) appeared in 6.8 % of the cells, and uncommon RLC, in close contact with the rough endoplasmic reticulum and nuclear membrane, were found in 1.5 % of the elements. The cells contained up to 3 RLC. Our data confirm that interferon stimulates the synthesis of TRS and CCC, whereas the reappearance of uncommon forms of RLC could reflect their neosynthesis, possibly related to the interferon therapy. The frequent findings of a close contact between RLC and nuclear membrane support the view that RLC are derived not only from rough endoplasmic reticulum, but also from the nuclear membrane.

Mechanism regulating nuclear calcium signalingThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

2006 ◽  
Vol 84 (3-4) ◽  
pp. 403-422 ◽  
Author(s):  
Anant N. Malviya ◽  
Christian Klein
Keyword(s):  
Endoplasmic Reticulum ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Calcium Signaling ◽  
Nuclear Membrane ◽  
Protein Fragment ◽  
Outer Nuclear Membrane ◽  
Nuclear Calcium ◽  
A Cell ◽  
Epidermal Growth

Although the outer nuclear membrane is continuous with the endoplasmic reticulum, it is possible to isolate nuclei both intact and free from endoplasmic reticulum contaminants. The outer and the inner nuclear membranes can be purified free from cross-contamination. Evidence in support of autonomous regulation of nuclear calcium signaling relies upon the investigations with isolated nuclei. Mechanisms for generating calcium signaling in the nucleus have been identified. Two calcium transporting systems, an ATP-dependant nuclear Ca2+-ATPase and an IP4-mediated inositol 1,3,4,5-tetrakisphosphate receptor, are located on the outer nuclear membrane. Thus, ATP and IP4, depending on external free calcium concentrations, are responsible for filling the nuclear envelope calcium pool. The inositol 1,4,5-trisphosphate receptor is located on the inner nuclear membrane with its ligand binding domain facing toward the nucleoplasm. Likewise, the ryanodine receptor is located on the inner nuclear membrane and its ligand cADP-ribose is generated within the nucleus. A 120 kDa protein fragment of nuclear PLC-γ1 is stimulated in vivo by epidermal growth factor nuclear signaling coincident with the time course of nuclear membrane epidermal growth factor receptor activation. Stimulated 120 kDa protein fragment interacts with PIKE, a nuclear GTPase, and together they form a complex with PI[3]kinase serving as a module for nuclear PI[3]K stimulation. Thus, the nucleus has its own IP3 generating system.

Particles Seen in Fefeze-Fracture Preparattoks

1969 ◽  
Vol 27 ◽  
pp. 206-207
Author(s):  
Stanley Bullivant
Keyword(s):  
Endoplasmic Reticulum ◽  
Cardiac Muscle ◽  
Nuclear Membrane ◽  
Actin Filaments ◽  
Carbon Coating ◽  
Freeze Fracture ◽  
Animal Tissues ◽  
Outer Nuclear Membrane ◽  
First Category ◽  
Electron Microscopical

A variety of animal tissues were examined by the simple freeze-fracture technique. An apparatus was used in which the Pt shadowing and carbon coating was carried out through aligned tunnels or apertures. Tn this way the previously fractured cold specimen is protected from contamination.Some particles seen in freeze-fracture replicas can be correlated with structures seen by other electron microscopical techniques. Into this first category fall the broken-off ends of myosin and actin filaments, (Figure 1), the broken-off ends of nucleohistone fibrils the particles seen between membranes in the close junction in cardiac muscle (Figure 2) and quantasomes in chloroplasts. The second group of particles are those found on membranes. An example of these is provided by the membrane faces seen in a fracture through the endoplasmic reticulum (Figure 3). The topology of the situation can be worked out using the outer nuclear membrane as a reference and counting off alternate cytoplasmic and cisternal spaces.

Freeze-Fracture Replication of Rough Endoplasmic Reticulum of Mouse Liver Cells

1972 ◽  
Vol 11 (2) ◽  
pp. 477-489
Author(s):  
A. S. BREATHNACH ◽  
C. STOLINSKI ◽  
M. GROSS
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Mouse Liver ◽  
Freeze Fracture ◽  
The Other ◽  
Fracture Face ◽  
Mitochondrial Membranes ◽  
En Face

Fresh, chemically unfixed, glycerinated specimens of mouse liver were examined by the technique of freeze-fracture replication without sublimation (i.e. they were not ‘etched’). Where extensive areas of fractured lamellar membranes of the rough endoplasmic reticulum are revealed en face, 2 types of fracture face are distinguishable. One of these fracture faces (A) is directed towards the cytoplasm, and the other (B) towards the cisternal cavity. A characteristic mosaic, or patchwork pattern of flat areas circumscribed by particles, is evident on both faces, and more clearly so on face B, due to a greater number of more prominent particles. Similar mosaic patterns are revealed on convex faces of the nuclear membrane, and on concave fracture faces of mitochondrial membranes, but are not evident on fracture faces of the plasma membrane. Uncertainty in establishing the exact plane of fracture of membranes in this material, since glycerol is virtually non-sublimable, makes it difficult to assess the significance of these mosaic patterns. The fact that ribosomes are not identifiable on either face of fractured endoplasmic reticulum membranes, gives no certain indication of the plane of fracture.

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