scholarly journals THE APPEARANCE OF ACETYLCHOLINESTERASE IN THE DORSAL ROOT NEUROBLAST OF THE RABBIT EMBRYO

1970 ◽  
Vol 46 (1) ◽  
pp. 64-80 ◽  
Author(s):  
Virginia M. Tennyson ◽  
Miro Brzin
Keyword(s):  
Endoplasmic Reticulum ◽  
Enzymatic Activity ◽  
Neural Tube ◽  
Growth Cone ◽  
Golgi Complex ◽  
Dorsal Root ◽  
Ache Activity ◽  
Nerve Roots ◽  
Dual Distribution ◽  
Rabbit Embryo

In the nine day old embryo, acetylcholinesterase (AChE) is found in the reticulum, i.e. the nuclear envelope, endoplasmic reticulum, and Golgi complex, of a few cells in the neural crest. When the neurite first enters the neural tube, reticulum-bound enzyme is present also in the varicosity of the growth cone of the bipolar neuroblast. At later stages, AChE in the neuroblast has a dual distribution; in addition to the reticulum, activity also appears at the axolemmal surface. The axolemmal activity is found initially on the distal portions of axons in the posterior fasciculus and then progressively appears along the nerve roots in a distal to proximal direction. Very little reticulum-bound enzyme is present within the axon proper. After the 13th day the levels of AChE activity in the posterior fasciculus greatly exceed those in the dorsal root or in the ganglion. Enzymatic activity in the dorsal root equals or exceeds that in the posterior fasciculus by day 16, and both areas are considerably more active than the ganglion.

scholarly journals THE FINE STRUCTURE OF THE AXON AND GROWTH CONE OF THE DORSAL ROOT NEUROBLAST OF THE RABBIT EMBRYO

1970 ◽  
Vol 44 (1) ◽  
pp. 62-79 ◽  
Author(s):  
Virginia M. Tennyson
Keyword(s):  
Tissue Culture ◽  
Neural Tube ◽  
Growth Cone ◽  
Dorsal Root ◽  
Matrix Material ◽  
Basal Surface ◽  
Dense Bodies ◽  
Dense Membrane ◽  
Large Numbers ◽  
Rabbit Embryo

The centrally directed neurite of the dorsal root neuroblast has been described from the period of its initial entrance into the neural tube until a well-defined dorsal root is formed. Large numbers of microtubules, channels of agranular reticulum, and clusters of ribosomes are found throughout the length of the early axons. The filopodia of the growth cone appear as long thin processes or as broad flanges of cytoplasm having a finely filamentous matrix material and occasionally small ovoid or elongate vesicles. At first the varicosity is a small expansion of cytoplasm, usually containing channels of agranular reticulum and a few other organelles. The widely dilated cisternae of agranular reticulum frequently found within the growth cone probably correspond to the pinocytotic vacuoles seen in neurites in tissue culture. The varicosities enlarge to form bulbous masses of cytoplasm, which may measure up to 5 µ in width and 13 µ in length. They contain channels of agranular reticulum, microtubules, neurofilaments, mitochondria, heterogeneous dense bodies, and a few clusters of ribosomes. Large ovoid mitochondria having ribonucleoprotein particles in their matrix are common. Dense membrane specializations are found at the basal surface of the neuro-epithelial cell close to the area where the early neurites first enter the neural tube.

Organisation in the Structure of the Cytoplasmic Ground Substance

1978 ◽  
Vol 36 (3) ◽  
pp. 627-639
Author(s):  
K.R. Porter
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Random Distribution ◽  
Ground Substance ◽  
The Matrix ◽  
Cell Processes ◽  
Cytoplasmic Ground Substance

Most types of cells are known from their structure and overall form to possess a characteristic organization. In some instances this is evident in the non-random disposition of organelles and such system subunits as cisternae of the endoplasmic reticulum or the Golgi complex. In others it appears in the distribution and orientation of cytoplasmic fibrils. And in yet others the organization finds expression in the non-random distribution and orientation of microtubules, especially as found in highly anisometric cells and cell processes. The impression is unavoidable that in none of these cases is the organization achieved without the involvement of the cytoplasmic ground substance (CGS) or matrix. This impression is based on the fact that a matrix is present and that in all instances these formed structures, whether membranelimited or filamentous, are suspended in it. In some well-known instances, as in arrays of microtubules which make up axonemes and axostyles, the matrix resolves itself into bridges (and spokes) between the microtubules, bridges which are in some cases very regularly disposed and uniform in size (Mcintosh, 1973; Bloodgood and Miller, 1974; Warner and Satir, 1974).

Membrane-associated microtubular areays induced in proximal myelinated processes of dorsal root ganglia by large doses of vitamin B6

1986 ◽  
Vol 44 ◽  
pp. 368-369
Author(s):  
V.J. Montpetit ◽  
S. Dancea ◽  
L. Tryphonas ◽  
D.F. Clapin
Keyword(s):  
Animal Model ◽  
Endoplasmic Reticulum ◽  
Dorsal Root Ganglia ◽  
Rough Endoplasmic Reticulum ◽  
Dorsal Root ◽  
Vitamin B6 ◽  
Morphological Changes ◽  
Model System ◽  
Sensory Nerves ◽  
Peripheral Sensory

Very large doses of pyridoxine (vitamin B6) are neurotoxic in humans, selectively affecting the peripheral sensory nerves. We have undertaken a study of the morphological and biochemical aspects of pyridoxine neurotoxicity in an animal model system. Early morphological changes in dorsal root ganglia (DRG) associated with pyridoxine megadoses include proliferation of neurofilaments, ribosomes, rough endoplasmic reticulum, and Golgi complexes. We present in this report evidence of the formation of unique aggregates of microtubules and membranes in the proximal processes of DRG which are induced by high levels of pyridoxine.

scholarly journals Prohibitin: A Novel Molecular Player in KDEL Receptor Signalling

2015 ◽  
Vol 2015 ◽  
pp. 1-13 ◽  
Author(s):  
Monica Giannotta ◽  
Giorgia Fragassi ◽  
Antonio Tamburro ◽  
Capone Vanessa ◽  
Alberto Luini ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Membrane Trafficking ◽  
Transmembrane Domain ◽  
Cell Cycle Control ◽  
Retrograde Transport ◽  
Multifunctional Protein ◽  
G Protein Coupled ◽  
Kdel Receptor ◽  
Prohibitin 1

The KDEL receptor (KDELR) is a seven-transmembrane-domain protein involved in retrograde transport of protein chaperones from the Golgi complex to the endoplasmic reticulum. Our recent findings have shown that the Golgi-localised KDELR acts as a functional G-protein-coupled receptor by binding to and activating Gs and Gq. These G proteins induce activation of PKA and Src and regulate retrograde and anterograde Golgi trafficking. Here we used an integrated coimmunoprecipitation and mass spectrometry approach to identify prohibitin-1 (PHB) as a KDELR interactor. PHB is a multifunctional protein that is involved in signal transduction, cell-cycle control, and stabilisation of mitochondrial proteins. We provide evidence that depletion of PHB induces intense membrane-trafficking activity at the ER–Golgi interface, as revealed by formation of GM130-positive Golgi tubules, and recruitment of p115,β-COP, and GBF1 to the Golgi complex. There is also massive recruitment of SEC31 to endoplasmic-reticulum exit sites. Furthermore, absence of PHB decreases the levels of the Golgi-localised KDELR, thus preventing KDELR-dependent activation of Golgi-Src and inhibiting Golgi-to-plasma-membrane transport of VSVG. We propose a model whereby in analogy to previous findings (e.g., the RAS-RAF signalling pathway), PHB can act as a signalling scaffold protein to assist in KDELR-dependent Src activation.

scholarly journals The Lamellar Systems of Cytoplasmic Membranes in Dividing Spermatogenic Cells of Drosophila virilis

1960 ◽  
Vol 7 (3) ◽  
pp. 433-441 ◽  
Author(s):  
Susumu Ito
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Light And Electron Microscopy ◽  
Primary Spermatocyte ◽  
Drosophila Virilis ◽  
Spermatogenic Cells ◽  
Membrane Systems ◽  
Cytoplasmic Membranes ◽  
Pas Reaction ◽  
Staining Methods

Spermatogenic cells of Drosophila virilis were studied by light and electron microscopy. The persistence of a "nuclear wall" during the meiotic divisions has been reported by a number of early cytologists, but this interpretation has been a subject of debate. Electron micrographs of dividing spermatocytes reveal the presence of multiple layers of paired membranes surrounding the nuclear region. These lamellar membrane systems are not typical of the nuclear envelope, but were interpreted as such by light microscopists. The membranes constituting a pair are separated by an interspace of ∼ 100 A and successive pairs are 200 to 400 A apart. These spacings are similar but not identical to those found in the lamellar systems of the Golgi complex. The cisternae of the endoplasmic reticulum in this material are devoid of attached ribonucleoprotein particles, are more precisely ordered than in vertebrate cells, and show a uniform, narrow intracisternal space of ∼ 100 A. The conspicuous asters appear to be made up of similar paired membranes radiating from the centriolar region. The primary spermatocyte has numerous dictyosomes and a well developed endoplasmic reticulum in cisternal form, but no typical Golgi complex or endoplasmic reticulum is found during the meiotic division stages of metaphase to telophase. Evidence is presented that these cytoplasmic organelles contribute to the formation of the extensive lamellar systems that appear during meiosis. The results of the Golgi silver staining methods and staining tests for phospholipids, basophilia, and the PAS reaction, indicate that the lamellar arrays of membranes present during meiosis are indistinguishable from the Golgi complex in their tinctorial properties.

scholarly journals Biosynthesis of the insulin receptor in rat adipose cells. Intracellular processing of the Mr-190 000 pro-receptor

1985 ◽  
Vol 232 (1) ◽  
pp. 71-78 ◽  
Author(s):  
J A Hedo ◽  
I A Simpson
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Insulin Receptor ◽  
Golgi Complex ◽  
Microsomal Fraction ◽  
Primary Cultures ◽  
Sodium Dodecyl ◽  
High Density ◽  
Low Density ◽  
Adipose Cells

We investigated the biosynthesis of the insulin receptor in primary cultures of isolated rat adipose cells. Cells were pulse-chase-labelled with [3H]mannose, and at intervals samples were homogenized. Three subcellular membrane fractions were prepared by differential centrifugation: high-density microsomal (endoplasmic-reticulum-enriched), low-density microsomal (Golgi-enriched), and plasma membranes. After detergent solubilization, the insulin receptors were immunoprecipitated with anti-receptor antibodies and analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and autoradiography. After a 30 min pulse-label [3H]mannose first appeared in a band of Mr 190 000. More than 80% of the Mr-190 000 component was recovered in the microsomal fractions. Its intensity reached a maximum at 1 h in the high-density microsomal fraction and at 2 h in the low-density microsomal fraction, and thereafter declined rapidly (t 1/2 approx. 3 h) in both fractions. In the plasma-membrane fraction, the radioactivity in the major receptor subunits, of Mr 135 000 (alpha) and 95 000 (beta), rose steadily during the chase and reached a maximum at 6 h. The Mr-190 000 precursor could also be detected in the high-density microsomal fraction by affinity cross-linking to 125I-insulin. In the presence of monensin, a cationic ionophore that interferes with intracellular transport within the Golgi complex, the processing of the Mr-190 000 precursor into the alpha and beta subunits was completely inhibited. Our results suggest that the Mr-190 000 pro-receptor originates in the endoplasmic reticulum and is subsequently transferred to the Golgi complex. Maturation of the pro-receptor does not seem to be necessary for the expression of the insulin-binding site. Processing of the precursor into the mature receptor subunits appears to occur during the transfer of the pro-receptor from the Golgi complex to the plasma membrane.

scholarly journals Myosin Motors and Not Actin Comets Are Mediators of the Actin-based Golgi-to-Endoplasmic Reticulum Protein Transport

2003 ◽  
Vol 14 (2) ◽  
pp. 445-459 ◽  
Author(s):  
Juan M. Durán ◽  
Ferran Valderrama ◽  
Susana Castel ◽  
Juana Magdalena ◽  
Mónica Tomás ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Light Chain ◽  
Shiga Toxin ◽  
Actin Filaments ◽  
Protein Transport ◽  
Myosin Ii ◽  
Nonmuscle Myosin ◽  
Nonmuscle Myosin Ii ◽  
Myosin Motors

We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibitors such as 2,3-butanedione monoxime (BDM) and 1-[5-isoquinoline sulfonyl]-2-methyl piperazine (ML7), which inhibit myosin and the phosphorylation of myosin II by the myosin light chain kinase, respectively; and a mutant of the nonmuscle myosin II regulatory light chain, which cannot be phosphorylated (MRLC2AA). On the other hand, actin comet tails were induced by the overexpression of phosphatidylinositol phosphate 5-kinase. Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the brefeldin A (BFA)-induced fusion of Golgi enzymes with the endoplasmic reticulum (ER). This delay was not caused by an alteration in the formation of the BFA-induced tubules from the Golgi complex. In addition, the Shiga toxin fragment B transport from the Golgi complex to the ER was also altered. This impairment in the retrograde protein transport was not due to depletion of intracellular calcium stores or to the activation of Rho kinase. Neither the reassembly of the Golgi complex after BFA removal nor VSV-G transport from ER to the Golgi was altered in cells treated with BDM/ML7 or expressing MRLC2AA. Finally, transport carriers containing Shiga toxin did not move into the cytosol at the tips of comet tails of polymerizing actin. Collectively, the results indicate that 1) myosin motors move to transport carriers from the Golgi complex to the ER along actin filaments; 2) nonmuscle myosin II mediates in this process; and 3) actin comets are not involved in retrograde transport.

scholarly journals Glycosyltransferase activities in Golgi complex and endoplasmic reticulum fractions isolated from African trypanosomes.

1984 ◽  
Vol 99 (2) ◽  
pp. 569-577 ◽  
Author(s):  
D J Grab ◽  
S Ito ◽  
U A Kara ◽  
L Rovis
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Surface Glycoprotein ◽  
Relative Distribution ◽  
African Trypanosomes ◽  
Independent Form ◽  
Variable Surface ◽  
Dependent Form

Highly enriched Golgi complex and endoplasmic reticulum fractions were isolated from total microsomes obtained from Trypanosoma brucei, Trypanosoma congolense, and Trypanosoma vivax, and tested for glycosyltransferase activity. Purity of the fractions was assessed by electron microscopy as well as by biochemical analysis. The relative distribution of all the glycosyltransferases was remarkably similar for the three species of African trypanosomes studied. The Golgi complex fraction contained most of the galactosyltransferase activity followed by the smooth and rough endoplasmic reticulum fractions. The dolichol-dependent mannosyltransferase activities were highest for the rough endoplasmic reticulum, lower for the smooth endoplasmic reticulum, and lowest for the Golgi complex. Although the dolichol-independent form of N-acetylglucosaminyltransferase was essentially similar in all the fractions, the dolichol-dependent form of this enzyme was much higher in the endoplasmic reticulum fractions than in the Golgi complex fraction. Inhibition of this latter activity in the smooth endoplasmic reticulum fraction by tunicamycin A1 suggests that core glycosylation of the variable surface glycoprotein may occur in this organelle and not in the rough endoplasmic reticulum as previously assumed.

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