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 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.

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 Inhibition by colchicine of fibrinogen translocation in hepatocytes.

1975 ◽  
Vol 67 (1) ◽  
pp. 237-243 ◽  
Author(s):  
G Feldmann ◽  
M Maurice ◽  
C Sapin ◽  
J P Benhamou
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Direct Action ◽  
Intraperitoneal Administration ◽  
Cytoplasmic Translocation

In the rat, 8 h after intraperitoneal administration of colchicine, fibrinogen (detected by antirat fibrinogen antibodies labeled with peroxidase) accumulated in the lumina of the rough endoplasmic reticulum of the hepatocytes; 16 and 24 h after colchicine administration, fibrinogen was detected, respectively, in the lumina of the smooth endoplasmic reticulum and in the Golgi apparatus. The effect of colchicine on the cytoplasmic translocation of fibrinogen could be due to a direct action of the drug on the membranes of the endoplasmic reticulum or could be the indirect result of the disruptive action of the drug on the microtubules.

Fine structure of the spores of Minchinia chitonis (Lankester, 1885) Labbé, 1896 (Sporozoa: Haplosporida), a parasite of the chiton, Lepidochitona cinereus

Parasitology ◽  
1980 ◽  
Vol 81 (1) ◽  
pp. 169-176 ◽  
Author(s):  
S. J. Ball
Keyword(s):  
Endoplasmic Reticulum ◽  
Fine Structure ◽  
Golgi Apparatus ◽  
Morphological Study ◽  
Smooth Endoplasmic Reticulum ◽  
Spore Wall ◽  
Single Nucleus

SUMMARYA morphological study of the fine structure of the spores of Minchinia chitonis, a haplosporidian parasite of the chiton, Lepidochitona cinereus, is described. The spores contained a single nucleus, mitochondria, haplosporosomes, smooth endoplasmic reticulum, ribosomes and a large spherule (presumed Golgi apparatus). The spore wall was discontinuous at the spherule end, forming an opening covered by a lid which rested on a circumscribed flange. The flange of the spore wall and the lid were continuous in only one area which served as a hinge. The entire spore was encapsulated by epispore cytoplasm bounded by a strengthened membrane and extended to form 2 long projections, one at either end.

Localization of various phosphatase activities within the golgi apparatus and lysosomes of rat leydig cells

1986 ◽  
Vol 44 ◽  
pp. 294-295
Author(s):  
M. F. Lalli ◽  
V. Lacroix ◽  
L. Hermo ◽  
Y. Clermont ◽  
C. E. Smith
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Leydig Cells ◽  
Smooth Endoplasmic Reticulum ◽  
Fluid Phase ◽  
Multivesicular Bodies ◽  
Golgi Stack ◽  
Dense Membrane ◽  
Membrane Bound ◽  
Adsorptive Endocytosis

The testosterone-secreting Leydig cells contain an abundance of smooth endoplasmic reticulum, peroxisomes, mitochondria as well as a large, spheroidal, juxtanuclear Golgi apparatus composed of interconnected stacks of saccules (Figs. 1,2). Each Golgi stack appears to be composed of between 5 to 7 saccules or sacculo-tubular elements (Figs.1,2). These cells also possess pale and dense multivesicular bodies and dense membrane-bound bodies identified assecondary lysosomes, all of which have been shown to be involved in fluid phase and adsorptive endocytosis as well as in receptor mediated endocytosis. The purpose of the present study was to characterize the reactivity of Golgi saccules, multivesicular bodies and lysosomes of Leydig cells for different phosphatases.

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