Aids: Tubuloreticular Structures (Trs), Cylindrical Confronting Cisternae (Ccc), and Related Alterations

1999 ◽  
Vol 5 (S2) ◽  
pp. 1092-1093
Author(s):  
Gurdip S. Sidhu ◽  
Nicholas D. Cassai
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Matrix Material ◽  
Cell Types ◽  
Test Tube ◽  
Endoplasmic Reticulum Membrane ◽  
Annulate Lamellae ◽  
Electron Dense Material ◽  
Tubuloreticular Inclusions ◽  
Tubuloreticular Structures

TRS and CCC are endoplasmic reticulum membrane-derived structures seen in HIV-infected individuals in a variety of cell types. TRS (synonym: tubuloreticular inclusions) are 24-25 nm in diameter, branching tubules which are short or long and associated with the granular or smooth endoplasmic reticulum, the Golgi complex, the perinuclear cistern, and annulate lamellae (Fig. 1-3, 8). The tubules are noticeably more stretched out in Kaposi's sarcoma endothelial cells, presumably by an increase of matrix material within the reticulum sac (Fig. 3). TRS consist of membranous components, including polypeptides, but lack nucleic acid.CCC (test tube and ring-shaped forms; curvilinear membranes) are formed by a concentric stacking of two or three cisterns of endoplasmic reticulum resembling nuclear membrane in mitosis (Fig. 7), but with the interposition between the opposing membranes of a layer of electron-dense material that is resistant to lipid solvents (Fig. 4,5,8).

scholarly journals Syntaxin 17 Is Abundant in Steroidogenic Cells and Implicated in Smooth Endoplasmic Reticulum Membrane Dynamics

2000 ◽  
Vol 11 (8) ◽  
pp. 2719-2731 ◽  
Author(s):  
Martin Steegmaier ◽  
Viola Oorschot ◽  
Judith Klumperman ◽  
Richard H. Scheller
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Regulatory Protein ◽  
Cell Types ◽  
Membrane Dynamics ◽  
Endoplasmic Reticulum Membrane ◽  
Steroidogenic Cell ◽  
Molecular Machinery ◽  
Intermediate Compartment ◽  
Steroidogenic Cells

The endoplasmic reticulum (ER) consists of subcompartments that have distinct protein constituents, morphological appearances, and functions. To understand the mechanisms that regulate the intricate and dynamic organization of the endoplasmic reticulum, it is important to identify and characterize the molecular machinery involved in the assembly and maintenance of the different subcompartments. Here we report that syntaxin 17 is abundantly expressed in steroidogenic cell types and specifically localizes to smooth membranes of the ER. By immunoprecipitation analyses, syntaxin 17 exists in complexes with a syntaxin regulatory protein, rsly1, and/or two intermediate compartment SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin 17 is anchored to the smooth endoplasmic reticulum through an unusual mechanism, requiring two adjacent hydrophobic domains near its carboxyl terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular ER membranes that are abundant in steroidogenic cells.

NSP-encoded reticulons, neuroendocrine proteins of a novel gene family associated with membranes of the endoplasmic reticulum

1994 ◽  
Vol 107 (9) ◽  
pp. 2403-2416 ◽  
Author(s):  
H.J. van de Velde ◽  
A.J. Roebroek ◽  
N.H. Senden ◽  
F.C. Ramaekers ◽  
W.J. Van de Ven
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Gene Family ◽  
Biochemical Characterization ◽  
Smooth Endoplasmic Reticulum ◽  
Dendritic Tree ◽  
Cell Types ◽  
In Vitro Translation ◽  
Amino Terminal

The novel NSP gene was previously shown to encode, among a variety of neuroendocrine cell types, two 3′-overlapping transcripts, a 3.4 kb one for NSP-A (776 amino acids) and a 1.8 kb one for NSP-C (208 amino acids). The deduced proteins, which were predicted to possess distinct amino-terminal regions, appeared to exhibit some architectural resemblance to known neuroendocrine proteins. In this paper the biochemical characterization and subcellular localization of the two proteins is addressed. In vitro translation of NSP-A and -C RNA produced proteins of about 135 and 23 kDa, respectively. Proteins of similar molecular mass were also detected in immunoprecipitation and western blot analyses of neural and endocrine cells using specific anti-NSP-A or -C antisera; some heterogeneity of NSP-A was observed. NSP-A, but not NSP-C, appeared to be highly phosphorylated and preferentially on serine residues. In immunocytochemical studies, we demonstrated that NSP-A and -C are associated with the endoplasmic reticulum; NSP-A was found to co-localize with SERCA2b, a membrane-associated Ca(2+)-ATPase of the endoplasmic reticulum. In Purkinje cells, we found NSP-immunostaining in the perikaryon, the extensive dendritic tree and the axon, also suggesting association with the smooth endoplasmic reticulum. Biochemical studies of NSP-A provided evidence that NSP-A is strongly associated with microsomal membranes and analysis of deletion mutants of NSP-A revealed that the hydrophobic carboxy-terminal portion of the protein, which is also present in NSP-C, is critical for membrane binding. Through database searches, finally, we found two different NSP-related sequences, one in a sequenced region of human chromosome 19, and the second in a human, pancreatic islet-derived partial cDNA, suggesting that the NSP gene is the prototype of a larger gene family. The results of our studies seem to indicate that the NSP-encoded proteins are novel, membrane-anchored components of the endoplasmic reticulum for which we propose the name reticulons.

scholarly journals THE RABBIT ZYGOTE

1972 ◽  
Vol 55 (3) ◽  
pp. 533-541 ◽  
Author(s):  
Bela J. Gulyas
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Nuclear Envelope ◽  
Smooth Endoplasmic Reticulum ◽  
Annulate Lamellae ◽  
Nuclear Pores ◽  
Late Anaphase ◽  
Dense Nucleus

The formation of the blastomere nucleus was examined in the rabbit zygote with the electron microscope. In late anaphase the chromosomes are bare and vesicles of the smooth endoplasmic reticulum are numerous in the vicinity of the chromosomes. In early telophase individual chromosomes attain their own nuclear envelope and they are called karyomeres. The envelope of the karyomeres contains small gaps within it at several places where the chromatin is exposed to the cytoplasm. Nuclear pores are also observed. In the cytoplasm short annulate lamellae appear adjacent to the karyomeres, and clusters of punctate substance are also present. From early telophase onward the karyomeres extend pseudopod-like structures, called karyopods, which extend toward other karyomeres or karyopods, and consequently fuse together and serve as chromosomal bridges. Eventually all of the karyomeres fuse into a dense nucleus and decondensation of the chromosomes occurs.

The ultrastructure of the R.S. zoospore of the Chytridiomycete Physoderma gerhardti

1978 ◽  
Vol 56 (12) ◽  
pp. 1387-1393 ◽  
Author(s):  
Robert J. Lowry ◽  
Frederick K. Sparrow
Keyword(s):  
Endoplasmic Reticulum ◽  
Fine Structure ◽  
Inclusion Bodies ◽  
Smooth Endoplasmic Reticulum ◽  
Lipid Body ◽  
Dense Material ◽  
Electron Dense Material ◽  
General Internal ◽  
Deep Groove ◽  
Posterior Flagellum

The fine structure of the zoospore of Physoderma gerhardti Schroeter is described. It possesses a single very large lipid body (sometimes accompanied by several smaller ones) situated laterally to the nuclear cap – nucleus complex and is associated with electron-dense material (the microbody) and the single large posteriorly located mitochondrion. The single posterior flagellum proximally terminates in a kinetosome just short of the posterior cone-shaped end of the nucleus. The kinetosome lies in a deep groove in the mitochondrion and is associated with this organelle by striated rootlets. The kinetosome terminates in electron-dense material from which an array of microtubules arises. These microtubules run along the sides of the cone-shaped nucleus and nuclear cap. There is an accessory centriole lying close to and more or less parallel with the kinetosome. The cytoplasm contains a small amount of smooth endoplasmic reticulum and several inclusion bodies in the anterior region and several small vacuoles in the posterior region of the cell. The general internal organization of the zoospore of Physoderma gerhardti more nearly resembles that of a blastocladiaceous fungus than of any chytrid thus far investigated.

Ultrastructural features of ovarian interstitial tissue in a wild mouse, Apodemus flavicollis, at various reproductive stages, with a note on its histochemistry at the onset of the breeding period

1983 ◽  
Vol 61 (7) ◽  
pp. 1560-1567 ◽  
Author(s):  
Margareta Eriksson ◽  
Erik Nyholm
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Droplets ◽  
Smooth Endoplasmic Reticulum ◽  
Wild Mouse ◽  
Hydroxysteroid Dehydrogenase ◽  
Breeding Period ◽  
Interstitial Tissue ◽  
Apodemus Flavicollis ◽  
Electron Dense Material ◽  
Glucose 6 Phosphate Dehydrogenase

In Apodemus flavicollis caught at the onset of the breeding season, interstitial tissue of the ovaries showed weak to moderate 3β-hydroxysteroid dehydrogenase and glucose-6-phosphate dehydrogenase activity. Interstitial cells were found to be actively secretory among females with open vaginas. The active cells were characterized by round nuclei and well-developed cytoplasmic organelles. The mitochondria were sometimes associated with smooth endoplasmic reticulum and had mainly tubular cristae. Lipid droplets were few and contained electron-dense material. A Golgi complex with associated vesicles was conspicuous, as were endo- or exo-cytotic vesicles. It is concluded that in A. flavicollis interstitial tissue is actively secretory in connection with ovulation or early pregnancy.

scholarly journals Targeting of Rough Endoplasmic Reticulum Membrane Proteins and Ribosomes in Invertebrate Neurons

2002 ◽  
Vol 13 (5) ◽  
pp. 1778-1791 ◽  
Author(s):  
Melissa M. Rolls ◽  
David H. Hall ◽  
Martin Victor ◽  
Ernst H. K. Stelzer ◽  
Tom A. Rapoport
Keyword(s):  
Endoplasmic Reticulum ◽  
Caenorhabditis Elegans ◽  
Membrane Proteins ◽  
Cell Body ◽  
Rough Endoplasmic Reticulum ◽  
Protein Targeting ◽  
Fluorescent Protein ◽  
Cell Types ◽  
Endoplasmic Reticulum Membrane ◽  
Unknown Mechanism

The endoplasmic reticulum (ER) is divided into rough and smooth domains (RER and SER). The two domains share most proteins, but RER is enriched in some membrane proteins by an unknown mechanism. We studied RER protein targeting by expressing fluorescent protein fusions to ER membrane proteins in Caenorhabditis elegans. In several cell types RER and general ER proteins colocalized, but in neurons RER proteins were concentrated in the cell body, whereas general ER proteins were also found in neurites. Surprisingly RER membrane proteins diffused rapidly within the cell body, indicating they are not localized by immobilization. Ribosomes were also concentrated in the cell body, suggesting they may be in part responsible for targeting RER membrane proteins.

A role for smooth endoplasmic reticulum membrane cholesterol ester in determining the intracellular location and regulation of sterol-regulatory-element-binding protein-2

2001 ◽  
Vol 358 (2) ◽  
pp. 415-422 ◽  
Author(s):  
Christopher R. IDDON ◽  
Jane WILKINSON ◽  
Andrew J. BENNETT ◽  
Julie BENNETT ◽  
Andrew M. SALTER ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cholesterol Ester ◽  
Smooth Endoplasmic Reticulum ◽  
Regulatory Element ◽  
Membrane Cholesterol ◽  
Endoplasmic Reticulum Membrane ◽  
Cellular Cholesterol ◽  
Element Binding Protein ◽  
Sterol Regulatory Element ◽  
Coa Reductase

Cellular cholesterol homoeostasis is regulated through proteolysis of the membrane-bound precursor sterol-regulatory-element-binding protein (SREBP) that releases the mature transcription factor form, which regulates gene expression. Our aim was to identify the nature and intracellular site of the putative sterol-regulatory pool which regulates SREBP proteolysis in hamster liver. Cholesterol metabolism was modulated by feeding hamsters control chow, or a cholesterol-enriched diet, or by treatment with simvastatin or with the oral acyl-CoA:cholesterol acyltransferase inhibitor C1-1011 plus cholesterol. The effects of the different treatments on SREBP activation were confirmed by determination of the mRNAs for the low-density lipoprotein receptor and hydroxymethylglutaryl-CoA (HMG-CoA) reductase and by measurement of HMG-CoA reductase activity. The endoplasmic reticulum was isolated from livers and separated into subfractions by centrifugation in self-generating iodixanol gradients. Immunodetectable SREBP-2 accumulated in the smooth endoplasmic reticulum of cholesterol-fed animals. Cholesterol ester levels of the smooth endoplasmic reticulum membrane (but not the cholesterol levels) increased after cholesterol feeding and fell after treatment with simvastatin or C1-1011. The results suggest that an increased cellular cholesterol load causes accumulation of SREBP-2 in the smooth endoplasmic reticulum and, therefore, that membrane cholesterol ester may be one signal allowing exit of the SREBP-2/SREBP-cleavage-regulating protein complex to the Golgi.

In Vitro Induction of Crystals of MT Protein by Vinblastine-Colcemid in Mouse Spermatids

1974 ◽  
Vol 32 ◽  
pp. 132-133
Author(s):  
John J. Wolosewick ◽  
John H. D. Bryan
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Nuclear Ring ◽  
Rough Er ◽  
Distal Direction ◽  
In Vitro Induction

Early in spermiogenesis the manchette is rapidly assembled in a distal direction from the nuclear-ring-densities. The association of vesicles of smooth endoplasmic reticulum (SER) and the manchette microtubules (MTS) has been reported. In the mouse, osmophilic densities at the distal ends of the manchette are the organizing centers (MTOCS), and are associated with the SER. Rapid MT assembly and the lack of rough ER suggests that there is an existing pool of MT protein. Colcemid potentiates the reaction of vinblastine with tubulin and was used in this investigation to detect this protein.

Hepatic Ultrastructure Changes Induced by Lithocholic Acid

1967 ◽  
Vol 25 ◽  
pp. 162-163 ◽  
Author(s):  
F. G. Zaki
Keyword(s):  
Endoplasmic Reticulum ◽  
Lithocholic Acid ◽  
Smooth Endoplasmic Reticulum ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Electron Microscopic ◽  
Hydropic Degeneration ◽  
Hepatic Cells ◽  
Low Protein ◽  
Microscopic Studies

Addition of lithocholic acid (LCA), a naturally occurring bile acid in mammals, to a low protein diet fed to rats induced marked inflammatory reaction in the hepatic cells followed by hydropic degeneration and ductular cell proliferation. These changes were accompanied by dilatation and hyperplasia of the common bile duct and formation of “gallstones”. All these changes were reversible when LCA was withdrawn from the low protein diet except for the hardened gallstones which persisted.Electron microscopic studies revealed marked alterations in the hepatic cells. Early changes included disorganization, fragmentation of the rough endoplasmic reticulum and detachment of its ribosomes. Free ribosomes, either singly or arranged in small clusters were frequently seen in most of the hepatic cells. Vesiculation of the smooth endoplasmic reticulum was often encountered as early as one week after the administration of LCA (Fig. 1).

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