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PubMed1981

[Effect of phalloidin on the contractile structures in cytoplasmic preparations of Amoeba proteus].

The effect of phalloidin on ultrastructural components involved in movement have been studied in spread cytoplasmic preparations of Amoeba proteus. In absence of phalloidin, actin filaments are usually rare and only myosin rods are observed. With concentrations of phalloidin between 2 X 10(-6) M and 5 X 10(-6) M, numerous F-actin filaments are present in the preparations. Most of these actin filaments are straight, however some appeared branched and interconnected. Higher concentrations of phalloidin inhibit the movement of naked cytoplasm. Fibrils composed by aggregation of F-actin filaments are present in these preparations. Myosin rods are unaffected by phalloidin.

Actins↗
PubMed2002

GIT1 functions in a motile, multi-molecular signaling complex that regulates protrusive activity and cell migration.

GIT1 is a multidomain protein that is thought to function as an integrator of signaling pathways controlling vesicle trafficking, adhesion and cytoskeletal organization. It regulates ARF GTPases and has binding domains for paxillin and PIX, which is a PAK-binding protein and an exchange factor for Rac. We show that GIT1 cycles between at least three distinct subcellular compartments, including adhesion-like structures, the leading edge and cytoplasmic complexes. The cytoplasmic structures, which also contain paxillin, PAK and PIX, do not detectably co-localize with endosomal Golgi or membrane markers, suggesting that they represent a novel supramolecular complex. The GIT1 cytoplasmic complexes are motile and tended to move toward the cell periphery where they joined existing adhesions. In retracting regions of the cells, the GIT1 complexes moved away from the disassembling adhesions toward the cell body. Using deletion mutants, we have identified domains that target GIT1 to each of the compartments. Localization to adhesions and the leading edge requires the paxillin-binding domain, which comprises the C-terminal 140 residues (cGIT1), whereas targeting to the cytoplasmic complexes requires the central region that contains ankyrin repeats and the PIX-binding domain. Expression of GIT1 or cGIT, but not nGIT1 in which the paxillin-binding domain is deleted, increases the rate of migration and the size and number of protrusions. The latter are inhibited when GIT1 is co-expressed with a kinase-dead PAK, suggesting that the GIT1 interaction with PAK is required for enhanced migration and protrusive activity. Furthermore, GIT1 targets constitutively activated PAK to adhesions and the leading edge via its interaction with paxillin. Since expression of cGIT targets endogenous GIT1 to the leading edge, it appears that the leading edge is the location of GIT1 responsible for these activities. Thus, GIT1 is a component of a motile, multimolecular complex that traffics a set of signaling components to specific locations in the cell where they regulate localized activities.

Animals↗
PubMed1986

A post-embedding avidin-biotin peroxidase system to demonstrate the light and electron microscopic localization of lectin binding sites in rat kidney tubules.

A post-embedding method for the light and electron microscopic demonstration of lectin binding sites in rat kidney tubules is described. The use of biotinylated lectins, followed by treatment with avidin peroxidase and the DAB-H2O2 sequence, produced intense staining of acrylic sections at the electron microscope level: brush borders and associated structures, cytoplasmic granules, basal infoldings and basement membrane-plasmalemmal interfaces of proximal tubules bound erythrophytohaemagglutinin, while distal tubules were mainly unstained. At the light microscope level, epoxy resin sections showed a similar staining pattern after etching, as did acrylic resin sections after intensification of the final reaction product. The binding of wheatgerm agglutinin to cytoplasmic granules and brush border structures in the proximal tubules was abolished, at both the light and electron microscope levels, by the competing sugar tri-N-acetylchitotriose. Epoxy resin ultrathin sections required etching before staining was achieved in the electron microscope, and results were far inferior to those obtained with acrylic resin. This method allows rapid and inexpensive screening of large numbers of lectins, if required, at both the light and electron microscope levels, using reagents that are stable for long periods of time.

Animals↗
PubMed1959

Electron microscope studies of the human epidermis; the cell boundaries and topography of the stratum malpighii.

The thin skin of the left upper quadrant of the human abdomen has been studied by electron microscopy. Tissue removed with a high speed rotary punch was fixed in osmium tetroxide or potassium permanganate. The latter fixative in our preparations is superior to osmium for the demonstration of epidermal cell membranes and certain other membranous structures of the epidermis. The cytoplasmic membranes of basal cells and cells of the stratum granulosum have been found to be relatively straight, while those of most spinous cells are sharply scalloped. The deep cells of the stratum spinosum in the rete ridge area show cell membranes and cytoplasmic structure intermediate between true basal cells and most cells of the stratum spinosum. The extracellular material of the desmosome has been found to consist of alternate dark and light laminae similar to those described by Odland (13) and Horstmann and Knoop (7).

Cell Membrane↗
PubMed1980

[Postmortem changes in the ultrastructure, cytoplasmic proteins and nuclear chromatin of rabbit nerve cells].

Changes in the set of water soluble cytoplasmic and chromatin proteins have been studied in the rabbit neocortex, cerebral trunk, liver and muscles by means of electrophoresis in polyacryl gel with sodium dodecisulfate, 12 and 24 h after the animals are decapitated, when the material is kept in cold and at room temperature. Ultrastructure of pyramidal neurons in layer V of the rabbit sensomotor cortex has also been studied immediately after death and after 24 hours' preservation of the material at 4 degrees C and at room temperature. It has been stated that the ultrastructural changes in the nucleus and in the set of chromatin proteins in the cerebral cells are rather small even 24 h after death. Cytoplasmic structure and spectrum of the cytoplasmic proteins undergo much greater changes. Chromatin proteins of the cerebral cell nuclei, especially those of the neocortex, much better withstand the postmortem proteolysis than the cells in the liver and muscles, and cytoplasmic proteins of the cerebral cells are less stable than in other tissues. A possibility to perform analogous investigations in section material of the human brain and possible mechanisms of adaptive character on unequal stability of proteins in various tissue cells are discussed.

Animals↗
PubMed2001

Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.

A dark state tertiary structure in the cytoplasmic domain of rhodopsin is presumed to be the key to the restriction of binding of transducin and rhodopsin kinase to rhodopsin. Upon light-activation, this tertiary structure undergoes a conformational change to form a new structure, which is recognized by the above proteins and signal transduction is initiated. In this and the following paper in this issue [Cai, K., Klein-Seetharaman, J., Altenbach, C., Hubbell, W. L., and Khorana, H. G. (2001) Biochemistry 40, 12479-12485], we probe the dark state cytoplasmic domain structure in rhodopsin by investigating proximity between amino acids in different regions of the cytoplasmic face. The approach uses engineered pairs of cysteines at predetermined positions, which are tested for spontaneous formation of disulfide bonds between them, indicative of proximity between the original amino acids. Focusing here on proximity between the native cysteine at position 316 and engineered cysteines at amino acid positions 55-75 in the cytoplasmic sequence connecting helices I-II, disulfide bond formation was studied under strictly defined conditions and plotted as a function of the position of the variable cysteines. An absolute maximum was observed for position 65 with two additional relative maxima for cysteines at positions 61 and 68. The observed disulfide bond formation rates correlate well with proximity of these residues found in the crystal structure of rhodopsin in the dark. Modeling of the engineered cysteines in the crystal structure indicates that small but significant motions are required for productive disulfide bond formation. During these motions, secondary structure elements are retained as indicated by the lack of disulfide bond formation in cysteines that do not face toward Cys316 in the crystal structure model. Such motions may be important in light-induced conformational changes.

Amino Acid Sequence↗
PubMed1991

Phosphorylation-dependent down-modulation of CD4 requires a specific structure within the cytoplasmic domain of CD4.

Several structural features of the cytoplasmic domain of CD4 including phosphorylation of Ser-408 have been shown to be important in its endocytosis (Shin, J., Doyle, C., Yang, Z., Kappes, D., and Strominger, J.L. (1990) EMBO J. 9, 425-434). A series of cytoplasmic domain truncations have now indicated that the membrane proximal region of the cytoplasmic domain from Arg-396 to Lys-417 is sufficient for phorbol ester-induced internalization; this segment is predicted to be an alpha-helix. The severe impairment of endocytosis resulting from the mutation Ser-408 to Ala-408 is largely restored by a compensating mutation Ala-404 to Ser-404; phosphorylation of Ser-404 has been directly demonstrated. Furthermore, mutation of Met-407, Ile-410, Leu-413, or Leu-414 to a hydrophilic residue eliminated CD4 endocytosis as did domain truncation at Arg-412. Ser-408 was normally phosphorylated in all of these mutants, suggesting that other residues in this region, including the four hydrophobic amino acids, are also required for CD4 endocytosis. Immunofluorescence microscopy following staining of intact and permeabilized cells showed that all endocytosis defective mutants indeed remained on the cell surface even after phorbol ester treatment, while wild type CD4 was endocytosed and degraded in lysosomes. These data indicate that endocytosis requiring residues 397-417 and binding of lymphocyte tyrosine kinase at residues 417-429 are functions of independent segments of the cytoplasmic region and lead to a hypothesis regarding some features of the endocytic process.

Amino Acid Sequence↗
PubMed1967

Structure and development of rabies virus in tissue culture.

Structure and development of two fixed rabies virus strains in baby hamster kidney cells (BHK/21) were investigated by electron microscopy. The morphological development was correlated with fluorescent-antibody staining and infectivity titration. The uptake of virus was enhanced by addition of diethylaminoethyl dextran, and structural changes became apparent in the cytoplasm 8 to 9 hr after infection, when fluorescent-antibody staining was first discernible. These changes consisted of matrices containing fibers replacing normal cytoplasmic structures. Virus particles appeared at the edges of these matrices and inside them at 24 to 48 hr. This corresponded to significant rises in intracellular infectious virus. Formation of virus particles by budding from cell membranes was seen at 72 hr. Further incubation of the infected cells resulted in synthesis of bizarre structural elements. The complete virus particle was bullet-shaped with an average size of 180 by 75 mmu. It consisted of an inner core of filamentous material surrounded by two membranes of different densities. The surface showed a honeycomb arrangement with surface protrusions 60 to 70 A long having a knoblike structure at their distal end. These surface protrusions were absent at the flat end of the virus particle.

Animals↗
PubMed1978

[Morphologic and histochemical characteristics of mammalian embryos during the pre-implantation period of development].

Submicroscopic embryo organization during preimplantation development was analyzed and its carbohydrate metabolism at these stages was studied. In the process of investigation the following regularities were revealed: progressive rearrangement of the nucleus (from compact to reticular); alterations in cytoplasmic structures (in multivesicular bodies, in autophagal vacuoles, in mitochondria, in granular cytoplasmic network, in lamellar structures); complication of intracellular interrelations (by means of microvilli and median bodies at early stages and during subsequent formation of cellular processes, contacts after "thorn--net" pattern, dense, fissure-like contacts and desmosomes). By means of cytochemical and electron histochemical methods, glycogen distribution in embryos at different stages of development was elucidated, and tendency to its decrease with the progress of the development was noted, with its least contents being at the stage of blastocyst.

Animals↗
PubMed2000

An ultrastructural study of the liver in erythropoietic protoporphyria.

An ultrastructural investigation of the liver was performed in two patients with erythropoietic protoporphyria. There were many protoporphyrin crystals in the hepatocytes, Kupffer cells, bile canaliculi, epithelia of bile ducts, and sinusoidal endothelial cells and also free within sinusoids. In hepatocytes, these deposits were composed of granular amorphous materials and numerous slender, straight, or slightly curved needle-like crystals aligned in radial orientation. They were randomly distributed in the cytoplasm and completely replaced other cytoplasmic structures. Some crystals lay free in the cytoplasm and others were surrounded by a single membrane. In the bile canaliculi, severe alterations could be observed. Some of the bile canaliculi were filled with amorphous, noncrystalline pigments, and lumina were enlarged with loss of micro-villi. In addition, despite the absence of protoporphyrin deposits, there were many dilated bile canaliculi. The microfilamentous network around such dilated bile canaliculi was no longer evident, suggesting the depolymerization of actin filaments, which could lead to bile excretory disturbances. The bile duct epithelia showed focal apical membrane bleb formation. The functional or structural alterations of the sinusoidal endothelial cells by the protoporphyrin crystals might lead to the hepatic disturbances. These ultrastructural findings of the liver might contribute to the understanding of the pathogenesis of complicated liver disease in erythropoietic protoporphyria.

Adult↗
PubMedDate not supplied

[Analysis of possible mechanisms of orthonectid emergence from their hosts].

In the present study authors claim that the adult orthonectids can not move through host tissues by themselves. In various species of these enigmatic parasites there are at least two different mechanisms of emission of males and females from the host body. Intoshia linei, the orthonectid from Lineus ruber (Heteronemertini), and Intoshia variabili, the parasite of a flatworm Macrorhynchus crocea, realize the first way of emission. The plasmodium of these species forms tube-like outgrowths, which pierce the host tissues reaching the host body surface. The cytoplasm structure of these outgrowths differs from the cytoplasm of the central mass of plasmodium. Small mitochondria with electron dense matrix, lipid granules and vesicular bodies being common in the central part are absent in these outgrowths. Plasmodial outgrowths reach the host body surface and adult orthonectids move inside them using their cilia and stopping from time to time. The plasmodial outgrowths penetrate the ciliated epithelium, then males and females leave the host. Duration of emission may vary in different species from 6 to 13 days. The second mechanisms of emission is common for the orthonectid parasites of mollusks. Our observations of Rhopalura philinae from the gastropod Philine scabra lead to the conclusion that males and females leave their host practically simultaneously. When the plasmodium attains the terminal stage of its development most of the host entrails are already displaced by plasmodial mass. It causes breaks in host body walls and hence to emission of sexual individuals. During this process, which lasts about 24 hours, the mollusk dies. The same mechanism was observed in Rhopalura littoralis--parasite of the gastropod Onoba aculeus. Our investigations of emission ways reveal that the plasmodium of orthonectids has a potency of directing growth and can form certain structures. The process of forming the plasmodial outgrowths is coordinated in time and space. These outgrowths have certain directions inside the host body and the maturation of sexual individuals is clear related with the development of plasmodium outgrowth system. Our results suggest that forming of plasmodial outgrowths is an element of development of the united and highly integrated system. It is necessary to emphasize the capability of plasmodium to accomplish such morphogenetic transformations. This fact argues that plasmodium is a part of parasite organism and not host cells modified, like some experts supposed.

Animals↗
PubMed1992

Effects of extracellular matrix components and dihydrotestosterone on the structure and function of human prostate cancer cells.

The extracellular matrix (ECM) has been shown to play a major role in cell structure and function. Several studies have demonstrated that the ECM can alter cell morphology and effect DNA synthesis and gene expression. The ECM also interacts with growth hormones which have been shown to be located in or near the ECM where they are believed to effect cell structure and function. In the nontransformed cell, these ECM and hormone-mediated effects appear to be tightly regulated and this is believed to be accomplished through cell receptor-tissue matrix interactions. We, therefore, undertook a study to determine the effects of a variety of ECM components and the adrogenic hormone dihydrotestosterone (DHT) on the structure and function of the human prostate cancer cell line, LNCaP. The effects of individual matrix components in the presence and absence of 1 nM DHT on the static and dynamic morphology, growth rate, and PSA production of the LNCaP cell line were studied. We determine that the ECM and DHT interact in complex ways to effect cell structure and function. DHT produced alterations in cytoplasmic structure that increased cell size and decreased the nuclear area/cytoplasmic area ratio. Dynamic cell structure as measured by cell motility was very sensitive to the ECM components and the presence of DHT. PSA and growth could be regulated by substratum and DHT and there was an inverse relationship between PSA production and growth rate. These data exemplify the complex interactions which occur between prostate cancer cells, ECM components, and exogenous DHT that are reflected in cell structure and function.

Antigens, Neoplasm↗
PubMed2006

Intracellular accumulation of hepatitis C virus proteins in a human hepatoma cell line.

BACKGROUND/AIMS: The establishment of HCV replicon systems strongly improved the research on the replication processes but poorly advanced our knowledge on the subcellular localization of the structural glycoproteins, mainly due to their low expression. We sought to verify whether reinforcing E1E2 expression in the context of both HCV genomic and subgenomic replicon from either homologous or heterologous strains leads to formation of supramolecular structures including structural and nonstructural proteins. METHODS: Robust expression of HCV glycoproteins was achieved by stable expression of E1E2p7 from genotype 1a and 1b. RESULTS: In these cells, E1 and E2 triggered the formation of dot-like structures in which they co-localized with core and the nonstructural proteins NS3 and NS5A. Confocal microscopy analyses suggested that accumulation of HCV proteins occurs in an ER-derived subcompartment. Moreover, by labeling de novo-synthesized HCV RNA, we showed that these structures constitute a site of viral RNA synthesis. CONCLUSIONS: Expression in trans of HCV glycoproteins in the context of replicative viral genome or subgenome generates accumulation of structural and nonstructural viral proteins in peculiar cytoplasmic structures. The simultaneous presence of viral RNA, structural and nonstructural protein suggests that these complexes represent not only sites of HCV replication but also potential places of viral pre-budding.

Base Sequence↗