The relationship between synaptic vesicles, Golgi apparatus, and smooth endoplasmic reticulum: a developmental study using the zinc iodide-osmium technique

1971 ◽  
Vol 120 (3) ◽  
pp. 332-345 ◽  
Author(s):  
D. J. Stelzner
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Synaptic Vesicles ◽  
Smooth Endoplasmic Reticulum ◽  
Developmental Study ◽  
The Relationship ◽  
Zinc Iodide

Interaction of the smooth endoplasmic reticulum and mitochondria

2006 ◽  
Vol 34 (3) ◽  
pp. 370-373 ◽  
Author(s):  
J.G. Goetz ◽  
I.R. Nabi
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Close Association ◽  
Cytosolic Calcium ◽  
Functional Roles ◽  
Calcium Dependent ◽  
Motility Factor ◽  
Calcium Sequestration ◽  
Multiple Domains ◽  
The Relationship

The ER (endoplasmic reticulum) is composed of multiple domains including the nuclear envelope, ribosome-studded rough ER and the SER (smooth ER). The SER can also be functionally segregated into domains that regulate ER–Golgi traffic (transitional ER), ERAD (ER-associated degradation), sterol and lipid biosynthesis and calcium sequestration. The last two, as well as apoptosis, are critically regulated by the close association of the SER with mitochondria. Studies with AMFR (autocrine motility factor receptor) have defined an SER domain whose integrity and mitochondrial association can be modulated by ilimaquinone as well as by free cytosolic calcium levels in the normal physiological range. AMFR is an E3 ubiquitin ligase that targets its ligand directly to the SER via a caveolae/raft-dependent pathway. In the present review, we will address the relationship between the calcium-dependent morphology and mitochondrial association of the SER and its various functional roles in the cell.

scholarly journals The G protein of vesicular stomatitis virus has free access into and egress from the smooth endoplasmic reticulum of UT-1 cells.

1990 ◽  
Vol 110 (3) ◽  
pp. 625-635 ◽  
Author(s):  
J E Bergmann ◽  
P J Fusco
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
G Protein ◽  
Vesicular Stomatitis Virus ◽  
Smooth Endoplasmic Reticulum ◽  
Free Access ◽  
First Order ◽  
First Order Kinetics ◽  
Vesicular Stomatitis ◽  
Endoglycosidase H

We have investigated the role of the smooth endoplasmic reticulum (SER) of UT-1 cells in the biogenesis of the glycoprotein (G) of vesicular stomatitis virus (VSV). Using immunofluorescence microscopy, we observed the wild type G protein in the SER of infected cells. When these cells were infected with the mutant VSV strain ts045, the G protein was unable to reach the Golgi apparatus at 40 degrees C, but was able to exit the rough endoplasmic reticulum (RER) and accumulate in the SER. Ribophorin II, a RER marker, remained excluded from the SER during the viral infection, ruling out the possibility that the infection had destroyed the separate identities of these two organelles. Thus, the mechanism that results in the retention of this mutant glycoprotein in the ER at 39.9 degrees C does not limit its lateral mobility within the ER system. We have also localized GRP78/BiP to the SER of UT-1 cells indicating that other mutant proteins may also have access to this organelle. Upon incubation at 32 degrees C, the mutant G protein was able to leave the SER and move to the Golgi apparatus. To measure how rapidly this transfer occurs, we assayed the conversion of the G protein's N-linked oligosaccharides from endoglycosidase H-sensitive to endoglycosidase H-resistant forms. After a 5-min lag, transport of the G protein followed first order kinetics (t1/2 = 15 min). In contrast, no lag was seen in the transport of G protein that had accumulated in the RER of control UT-1 cells lacking extensive SER. In these cells, the transport of G protein also exhibited first order kinetics (t1/2 = 17 min). Possible implications of this lag are discussed.

Spermiogenesis in the Nine-Banded Armadillo

1973 ◽  
Vol 31 ◽  
pp. 632-633
Author(s):  
Frank J. Weaker
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Smooth Endoplasmic Reticulum ◽  
Posterior Pole ◽  
Seminiferous Tubules ◽  
Anterior Pole ◽  
Chromatoid Body ◽  
Acrosome Formation

The testes of mature armadillos were fixed by either perfusion or immersion. The morphology of the seminiferous tubules and the process of spermiogenesis were studied.The developing spermatids are generally oval in shape and contain a centrally placed nucleus. A well-developed Golgi apparatus, scattered mitochondria, centrioles, smooth endoplasmic reticulum, and a chromatoid body are observed within the cytoplasm. Granules formed within the Golgi appear to coalesce to form the acrosomal granule, which is enclosed within a vesicle (Fi,g. 1). The acrosome adheres to the nucleus at the anterior pole of the developing spermatid. The acrosome vesicle collapses and extends over the anterior two-thirds of the nucleus (Fig. 2). As this vesicle expands, the Golgi continues to release granules into the vesicle. Concomitant with acrosome formation, the centrioles and chromatoid body migrate to the posterior pole of the developing cell.

scholarly journals LYSOSOMES AND GERL IN NORMAL AND CHROMATOLYTIC NEURONS OF THE RAT GANGLION NODOSUM

1967 ◽  
Vol 33 (2) ◽  
pp. 419-435 ◽  
Author(s):  
Eric Holtzman ◽  
Alex B. Novikoff ◽  
Humberto Villaverde
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Smooth Endoplasmic Reticulum ◽  
Cell Periphery ◽  
Electron Microscopic ◽  
Ganglion Nodosum ◽  
Autophagic Vacuoles ◽  
Inosine Diphosphatase ◽  
Nissl Substance ◽  
Membranous Material

The rat ganglion nodosum was used to study chromatolysis following axon section. After fixation by aldehyde perfusion, frozen sections were incubated for enzyme activities used as markers for cytoplasmic organelles as follows: acid phosphatase for lysosomes and GERL (a Golgi-related region of smooth endoplasmic reticulum from which lysosomes appear to develop) (31–33); inosine diphosphatase for endoplasmic reticulum and Golgi apparatus; thiamine pyrophosphatase for Golgi apparatus; acetycholinesterase for Nissl substance (endoplasmic reticulum); NADH-tetra-Nitro BT reductase for mitochondria. All but the mitochondrial enzyme were studied by electron microscopy as well as light microscopy. In chromatolytic perikarya there occur disruption of the rough endoplasmic reticulum in the center of the cell and segregation of the remainder to the cell periphery. Golgi apparatus, GERL, mitochondria and lysosomes accumulate in the central region of the cell. GERL is prominent in both normal and operated perikarya. Electron microscopic images suggest that its smooth endoplasmic reticulum produces a variety of lysosomes in several ways: (a) coated vesicles that separate from the reticulum; (b) dense bodies that arise from focal areas dilated with granular or membranous material; (c) "multivesicular bodies" in which vesicles and other material are sequestered; (d) autophagic vacuoles containing endoplasmic reticulum and ribosomes, presumably derived from the Nissl material, and mitochondria. The number of autophagic vacuoles increases following operation.

scholarly journals GOLGI APPARATUS, GERL, AND LYSOSOMES OF NEURONS IN RAT DORSAL ROOT GANGLIA, STUDIED BY THICK SECTION AND THIN SECTION CYTOCHEMISTRY

1971 ◽  
Vol 50 (3) ◽  
pp. 859-886 ◽  
Author(s):  
Phyllis M. Novikoff ◽  
Alex B. Novikoff ◽  
Nelson Quintana ◽  
Jean-Jacques Hauw
Keyword(s):  
Endoplasmic Reticulum ◽  
Acid Phosphatase ◽  
Golgi Apparatus ◽  
Dorsal Root Ganglia ◽  
Dorsal Root ◽  
Smooth Endoplasmic Reticulum ◽  
Thin Sections ◽  
Golgi Stack ◽  
Golgi Element ◽  
Thiamine Pyrophosphatase

New insights into the ultrastructure and phosphatase localizations of Golgi apparatus and GERL, and into the probable origin of lysosomes in the neurons of fetal dorsal root ganglia and the small neurons of adult ganglia have come from studying thick (0.5–1.0 µ) as well as thin (up to 500 A) sections by conventional electron microscopy. Tilting the thick specimens, by a goniometer stage, has helped to increase our understanding of the three-dimensional aspects of the Golgi apparatus and GERL. One Golgi element, situated at the inner aspect of the Golgi stack, displays thiamine pyrophosphatase and nucleoside diphosphatase activities. This element exhibits regular geometric arrays (hexagons) of interconnected tubules without evidence of a flattened portion (saccule or cisterna). In contrast, GERL shows acid phosphatase activity and possesses small cisternal portions and anastomosing tubules. Lysosomes appear to bud from GERL. Osmium deposits, following prolonged osmication, are found in the outer Golgi element. Serial 0.5-µ and thin sections of thiamine pyrophosphatase-incubated material demonstrate that, in the neurons studied, the Golgi apparatus is a continuous network coursing through the cytoplasm. Serial thick sections of acid phosphatase-incubated tissue suggest that GERL is also a continuous structure throughout the cytoplasm. Tubules of smooth endoplasmic reticulum, possibly part of GERL, extend into the polygonal compartments of the inner Golgi element. The possible physiological significance of a polygonal arrangement of a phosphatase-rich Golgi element in proximity to smooth ER is considered. A tentative diagram of the Golgi stack and associated endoplasmic reticulum in these neurons has been drawn.

scholarly journals Biosynthesis of high density lipoprotein by chicken liver: conjugation of nascent lipids with apoprotein A1.

1984 ◽  
Vol 99 (6) ◽  
pp. 1917-1926 ◽  
Author(s):  
D Banerjee ◽  
C M Redman
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Smooth Endoplasmic Reticulum ◽  
Lipid Synthesis ◽  
Density Lipoprotein ◽  
Plasma Lipoproteins ◽  
Golgi Cell ◽  
Intracellular Organelles ◽  
Apoprotein A1 ◽  
Cell Fractions

To study the assembly of newly synthesized lipids with apoprotein A1, we administered [2-3H]glycerol to young chickens and determined the hepatic intracellular sites of lipid synthesis and association of nascent lipids with apoprotein A1. [2-3H]glycerol was rapidly incorporated into hepatic lipids, reaching maximal levels at 5 min, and this preceded the appearance of lipid radioactivity in the plasma. The liver was fractionated into rough and smooth endoplasmic reticulum and Golgi cell fractions. The isolated cell fractions were further subfractionated into membrane and soluble (content) fractions by treatment with 0.1 M Na2CO3, pH 11.3. At various times, the lipid radioactivity was measured in each of the intracellular organelles, in immunoprecipitable apoprotein A1, and in materials that floated at buoyant densities similar to those of plasma lipoproteins. Maximal incorporation occurred at 1 min in the rough endoplasmic reticulum, at 3-5 min in the smooth endoplasmic reticulum, and at 5 min in the Golgi cell fractions. The majority (66-93%) of radioactive glycerol was incorporated into triglycerides with smaller (4-27%) amounts into phospholipids. About 80% of the lipid radioactivity in the endoplasmic reticulum and 70% of that in the Golgi cell fractions was in the membranes. The radioactive lipids in the content subfraction were distributed in various density classes with most nascent lipids floating at a density less than or equal to 1.063 g/ml. Apoprotein A1 from the Golgi apparatus, obtained by immunoprecipitation, contained sixfold more nascent lipids than did that from the endoplasmic reticulum. These data indicate that [2-3H]glycerol is quickly incorporated into lipids of the endoplasmic reticulum and the Golgi cell fractions, that most of the nascent lipids are conjugated with apoproteins A1 in the Golgi apparatus, and that very little association of nascent lipid to apoprotein A1 occurs in the endoplasmic reticulum.

scholarly journals Aspects of turnover and biogenesis of synaptic vesicles at locust neuromuscular junctions as revealed by zinc iodide-osmium tetroxide (ZIO) reacting with intravesicular SH-groups.

1978 ◽  
Vol 78 (3) ◽  
pp. 839-855 ◽  
Author(s):  
M Reinecke ◽  
C Walther
Keyword(s):  
Synaptic Vesicles ◽  
Osmium Tetroxide ◽  
Developmental Stages ◽  
Neuromuscular Junctions ◽  
Smooth Endoplasmic Reticulum ◽  
Motor Nerve ◽  
Average Volume ◽  
Experimental Conditions ◽  
Sh Groups ◽  
Zinc Iodide

Retractor unguis nerve muscle preparations from the locust were subjected to the zinc iodide-osmium tetroxide reaction (ZIO) after pre-fixation in glutaraldehyde. Applied for 18 h at 4 degrees C in the dark, ZIO reacts at pH 4.2--4.0 fairly selectively with the matrix of synaptic vesicles. Approximately 53% of the vesicles are completely and 4% partially stained. The percentage of ZIO-positive vesicles is increased to nearly 90% and reduced to 4% or less by pretreatment with SH-protecting (dithiothreitol) or SH-blocking (N-ethylmaleimide, p-chloromercuriphenyl sulfonic acid) and SH-oxidizing (azodicarboxylic acid-bis-dimethylamide) reagents, respectively. Stimulation of the motor nerve at 20 Hz for 7 min, partially fatiguing synaptic transmission, reduces the number of vesicles per square micrometer of terminal area by approximately 52%; 2 min of rest restores this number of its pre-stimulation level. These changes are chiefly accounted for by changes in the number of completely ZIO-positive vesicles. 2 min after the end of stimulation, partially ZIO-positive vesicles are three times more frequent than before. With all experimental conditions, the average volume of vesicles was as follows: ZIO-negative less than partially ZIO-positive less than completely ZIO-positive. The average volume of ZIO-positive vesicles is almost unaffected by stimulation; that of ZIO-negative vesicles is decreased by 25% immediately after stimulation, increasing with subsequent rest to the initial level after 1 h. It is suggested (a) that ZIO demonstrates intravesicular protein(s) containing SH-groups and (b) that the completely ZIO-positive vesicles represent the mature ones ready to be used for transmitter release. How the ZIO reaction differentiates between different developmental stages of vesicles which could arise from the smooth endoplasmic reticulum is discussed.

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