[Ontogenetic changes in the metabolism of phosphorus compounds in plant cytoplasmic structures].
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Chloroplasts↗
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Studies on the localization of oxidative phosphorylation in cytoplasmic structures of rat liver.
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Animals↗
Poly(ADP-ribose) synthetase associated to cytoplasmic structures of meiotic cells.
An active poly(ADP-ribose) synthetase has been found to be associated to mitochondria of frog oocytes and of testis from various species. The enzyme was also found in association with the microsomal-ribosomes fraction of the testis. Both enzymes are strongly inhibited by nicotinamide, thymidine, and theophylline, and they synthesize oligomers of ADP-ribose of an average chain length of 2-6 residues. The apparent km for NAD+ of the mitochondrial enzyme is 22 micro M which contrasts with the corresponding value of the chromatin-bound enzyme, 210 micro M NAD+. Treatment of the isolated mitochondria with Triton X-100 revealed that the enzyme is associated to a polydisperse structure. The higher specific activity of the enzyme associated to mitochondria was found in testis of 20 to 30 days old rats. This development study suggest that the maximal activity of the enzyme is associated to mitochondria belonging to primary spermatocytes. Poly(ADP-ribose) synthetase was also found in association of the microsome-ribosome fraction of rat, mouse, carp, and bull testis. This activity is 20 to 30 times higher than in the same fraction of the liver. Contrary to the chromatin-bound enzyme, the microsome-ribosome enzyme activity is stimulated 3 to 4 times by DNA, but it is slightly inhibited by histone H1. The enzyme seems to be associated to ribonucleoproteins of a very polydisperse nature. The possible relationship of poly(ADP-ribose) synthetase with the intermitochondrial cement and with the chromatoid body will be discussed. These are very unique structures only present in germinal cells.
Animals↗
The structure of cytoplasm in directly frozen cultured cells. II. Cytoplasmic domains associated with organelle movements.
The relationship between organelle movement and cytoplasmic structure in cultured fibroblasts or epithelial cells was studied using video-enhanced differential interference contrast microscopy and electron microscopy of directly frozen whole mounts. Two functional cytoplasmic domains are characterized by these techniques. A central domain rich in microtubules is associated with directed as well as Brownian movements of organelles, while a surrounding domain rich in f-actin supports directed but often intermittent organelle movements more distally along small but distinct individual microtubule tracks. Differences in the organization of the cytoplasm near microtubules may explain why organelle movements are typically continuous in central regions but usually intermittent along the small tracks through the periphery. The central type of cytoplasm has a looser cytoskeletal meshwork than the peripheral cytoplasm which might, therefore, interfere less frequently with organelles moving along microtubules there.
Actins↗
Cytoplasmic tubular structures in liver of HBsAg carrier chimpanzees infected with delta agent and comparison with cytoplasmic structures in non-A, non-B hepatitis.
Electron microscopic observations were carried out on five HBsAg carrier chimpanzees infected with delta (delta) agent and two chimpanzees infected with human non-A, non-B hepatitis. The cytoplasmic tubular structures, which have been recognized in the liver of chimpanzees infected with human non-A, non-B hepatitis, were found also in the liver of HBsAg carrier chimpanzees infected with delta agent. The quantity of the cytoplasmic structures in serial studies was associated with SGPT elevation rather than with expression of delta antigen in sera and liver tissues. This indicates that the cytoplasmic structures reflect a pathologic change of the hepatocytes in chimpanzees infected with delta agent or human non-A, non-B hepatitis. These and other similarities between the two agents suggest a similar nature.
Animals↗
Dual effect of procaine in sea urchin eggs. Inducer and inhibitor of microtubule assembly.
An increase in the amount of cytoplasmic filamentous structures (cytoplasmic matrix and aster) which were recovered after hexylene glycol/Triton X-100 treatment of sea urchin eggs (Paracentrotus lividus) activated by 0.2-2.5 mM procaine was observed. At higher activator concentrations, an opposite effect was observed and formation of these cytoplasmic structures was inhibited in the presence of 10 mM procaine. This inhibitory effect was reversed by diluting the drug in the incubation medium. DNase I inhibition assays on egg homogenates which were performed at different time points of the activation process, show that the same amount of actin was induced to polymerize in eggs activated either by 2.5 or 10 mM procaine. However, colchicine-binding assays on the 100 000 g particulate fractions of these homogenates show that in eggs activated by 10 mM procaine, in contrast to those activated by 2.5 mM, tubulin polymerization was inhibited and microtubules were disassembled. These results show that the dual effect of procaine in the organization of the egg cytoskeleton appears to be related to its effect on the state of tubulin.
Animals↗
Ultrastructural and histological effects of exposure to CEES or heat in a human epidermal model.
Ultrastructural and terminal deoxynucleotidyl transferase nick end labeling (TUNEL) studies were conducted to compare mechanisms of 2-chloroethyl ethyl sulfide (CEES) and heat-induced injury to EpiDerm. Twenty-two hours after 2-h exposure to the monofunctional alkylating agent CEES, budding of cytoplasm, clumping of nuclear chromatin, disintegration of nuclear membranes and cytoplasmic structures, and cytoplasmic vacuolization were detected, especially in the basal cells near the pseudobasement membrane. TUNEL techniques revealed DNA fragmentation distinct from that normally associated with terminal keratinocyte differentiation. Similar evaluations 22.5 h after 90 min exposure of EpiDerm to elevated temperature (45 degrees C) produced a different pattern of cell damage. Swelling of intercellular spaces, extensive cytoplasmic vacuolization, disruption of normal nuclear shape, reduced cell membrane integrity, and release of cellular material in the basal region characterized heat injury. Heat did not alter the DNA fragmentation normally associated with keratinocyte maturation. These data suggest that CEES elicited an apoptotic mechanism of cell death with features of terminal differentiation such as nuclear membrane disintegration and loss of cytoplasmic structures. Heat, alternatively, produced changes more typical of oncotic necrosis.
Apoptosis↗
Repeating structure of cytoplasmic poly(A)-ribonucleoprotein.
A repeating structure of cytoplasmic poly(A)-ribonucleoprotein is revealed by digestion with T2 RNase. A pattern of fragments that are multiples of about 27 residues is obtained. The repeating structure is readily reconstituted from purified poly(A) and cytoplasmic factors. Reconstitution is specific for poly(A), as shown by the lack of competition by poly(G), poly(C), poly(dA), and tRNA. The repeating structure is absent from the nucleus, and so appears to be formed upon transport to the cytoplasm.
Animals↗
Characterization of cytoplasmic fibril structures found in gliding cells of Saprospira sp.
The cytoplasmic fibril structures of Saprospira sp. strain SS98-5 grown on a low-nutrient agar medium were purified from cell lysates treated with Triton X-100 and were observed by electron microscopy to be about 7 nm in width and 200-300 nm in length. SDS-PAGE of the fibril structures exhibited a single protein band with a molecular mass of 61 kDa. A Saprospira cytoplasmic fibril protein (SCFP), which is a subunit of the fibril structures, was digested with trypsin to oligopeptides and analyzed for amino acid sequences. A partial nucleotide sequence of the SCFP gene was determined after PCR using primers designated from the amino acid sequences of the oligopeptides. SCFP gene including DNA fragments were detected by Southern hybridization using the PCR product for an SCFP gene as a probe and were cloned to determine whole nucleotide sequences. The SCFP gene indicated relatively higher similarity to conserved hypothetical phage tail sheath proteins. A Western immunoblotting analysis showed that SCFP was significantly expressed in gliding cells as compared with nongliding cells. The above findings with the previously reported results suggest that the cytoplasmic fibril structures are possibly related to the gliding motility of Saprospira sp. strain SS98-5.
Bacterial Proteins↗
Gap junction endocytosis and lysosomal degradation of connexin43-P2 in WB-F344 rat liver epithelial cells treated with DDT and lindane.
Treatment of WB-F344 rat liver epithelial cells with DDT (1,1-bis(p-chlorophenyl)-2,2,2-trichloroethane) or lindane induces a loss of gap junction plaques and a decrease in the phosphorylated gap junction protein connexin43-P2 (Cx43-P2), which is associated with the plaques. In this study we have considered several mechanisms. The loss of junctional plaques could be due to disaggregation of junctional particles or to endocytosis of the plaques, while the loss of Cx43-P2 could be due to dephosphorylation or degradation. Immunohistochemical analyses of DDT- or lindane-treated cells revealed a reduction in plasma membranous Cx43-positive gap junction plaques coincident with the appearance of Cx43-positive punctate cytoplasmic structures. The cytoplasmic Cx43-positive structures eventually disappeared after 4 h treatment. Diffuse Cx43-positive plasma membranous staining was not seen following DDT or lindane treatment. Western blot analyses of these cells indicated that Cx43-P2 decreased in a time-dependent manner that paralleled the disappearance of gap junction plaques from the plasma membrane. The loss of Cx43-P2 was not due to dephosphorylation, since no increase in non-phosphorylated (Cx43-NP) or other phosphorylated (Cx43-P1) forms of the protein were evident. The decrease in Cx43-P2 and the disappearance of cytoplasmic Cx43-positive structures were prevented by colchicine and chloroquine, which suggests that Cx43-P2-containing plaques were internalized and degraded in lysosomes. In addition, two small (approximately 18 and approximately 22 kDa) bands appeared in Western blots coincident with the loss of Cx43-P2 and may be degradation products of the protein. These immunohistochemical and biochemical data strongly suggest that the loss of gap junction plaques and of Cx43-P2 in WB-F344 cells treated with DDT and lindane were due to endocytosis of the plaques and degradation of Cx43-P2 in lysosomes.
Animals↗
Stigmoid bodies contain type I receptor proteins SorLA/LR11 and sortilin: new perspectives on their function.
Stigmoid bodies (SBs) are structures in the cytoplasm of neurons. SBs are mostly found in the hypothalamic region of the rat and contain a protein called huntingtin-associated protein 1 (HAP1). In a recent publication, large cytoplasmic structures were shown to be immunoreactive for a type I receptor called SorLA/LR11. By light microscopic analysis, these structures appeared similar to SBs in size and in brain regional and subcellular localization. To determine whether these large puncta correspond to HAP1-containing SBs, we used antibodies specific to various domains of the apolipoprotein receptor LR11 to perform immunocytochemistry in rat and mouse brain tissue. Transfection studies using HeLa cells were conducted to demonstrate the specificity of the antibodies. We found that, in both species, antibodies to the domain II (or VSP10 for vacuolar sorting protein 10 domain) of LR11 immunoreact with large cytoplasmic structures. Co-localization immunolabeling experiments in rat brain tissue sections and in neuron cultures showed that these LR11-immunoreactive structures correspond to HAP1-positive SBs. Electron microscopy was performed in rat hypothalamus and further demonstrated the presence of LR11 in SBs and its co-localization with HAP1. LR11-containing SBs were most abundant in the hypothalamus but were also found in many brainstem nuclei, thalamus, and hippocampus. Our data also show that sortilin, another transmembrane protein containing a VPS10 domain, localizes to large cytoplasmic puncta and is found in LR11-positive and Hap1-positive SBs in hypothalamic neuron cultures.
Adaptor Proteins, Vesicular Transport↗
THE CYTOPLASMIC FINE STRUCTURE OF THE DIATOM, NITZSCHIA PALEA.
The cytoplasmic fine structure of the motile, pennate diatom, Nitzschia palea was studied in thin sections viewed in the electron microscope. The cells were fixed in OsO(4), embedded in methacrylate, and immersed in 10 per cent hydrofluoric acid (HF) for 36 to 40 hours to remove the siliceous cell wall prior to sectioning. The HF treatment did not cause any obvious cytoplasmic damage. The dictyosome complex is perinuclear, and located only in the central cytoplasm. Mitochondria are sparse in the central cytoplasm, but abundant in the peripheral cytoplasm, and fill many of the transvacuolar cytoplasmic strands. Characteristic, amorphous oil bodies fill certain cytoplasmic strands and probably are not leucosin. The pyrenoid appears to be membrane limited, and oil droplets are found adjacent to the pyrenoid. The pyrenoid of another diatom, Cymbella affinis, is also membrane-limited. The membrane limiting the pyrenoid may be a composite of the terminal portions of chloroplast discs, facilitating rapid movement of photosynthate into the pyrenoid matrix, where the characteristic oil droplets may be formed. Carinal fibrils are found singly in each carinal pore, and may be involved in the locomotion of Nitzschia palea.
Cell Biology↗
Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution.
The molecular structure of cytoplasmic malate dehydrogenase from pig heart has been refined by alternating rounds of restrained least-squares methods and model readjustment on an interactive graphics system. The resulting structure contains 333 amino acids in each of the two subunits, 2 NAD molecules, 471 solvent molecules, and 2 large noncovalently bound molecules that are assumed to be sulfate ions. The crystallographic study was done on one entire dimer without symmetry restraints. Analysis of the relative position of the two subunits shows that the dimer does not obey exact 2-fold rotational symmetry; instead, the subunits are related by a 173 degrees rotation. The structure results in a R factor of 16.7% for diffraction data between 6.0 and 2.5 A, and the rms deviations from ideal bond lengths and angles are 0.017 A and 2.57 degrees, respectively. The bound coenzyme in addition to hydrophobic interactions makes numerous hydrogen bonds that either are directly between NAD and the enzyme or are with solvent molecules, some of which in turn are hydrogen bonded to the enzyme. The carboxamide group of NAD is hydrogen bonded to the side chain of Asn-130 and via a water molecule to the backbone nitrogens of Leu-157 and Asp-158 and to the carbonyl oxygen of Leu-154. Asn-130 is one of the corner residues in a beta-turn that contains the lone cis peptide bond in cytoplasmic malate dehydrogenase, situated between Asn-130 and Pro-131. The active site histidine, His-186, is hydrogen bonded from nitrogen ND1 to the carboxylate of Asp-158 and from its nitrogen NE2 to the sulfate ion bound in the putative substrate binding site. In addition to interacting with the active site histidine, this sulfate ion is also hydrogen bonded to the guanidinium group of Arg-161, to the carboxamide group of Asn-140, and to the hydroxyl group of Ser-241. It is speculated that the substrate, malate or oxaloacetate, is bound in the sulfate binding site with the substrate 1-carboxyl hydrogen bonded to the guanidinium group of Arg-161.
Amino Acid Sequence↗
[Visualization of the cytoplasmic segregation structure by using computed microscopy].
Cytoplasm organella segregation accompanies virtually all the changes occuring in embryonic and differentiated cells. The general scheme of mapping spatial distribution of cytoplasm texture parameters, realized using computed microscope LEITZ-T.A.S., allowed the imaging of geometrical relationship between yolk granules in the Rana Temporaria fertilized egg. The development of dorsoventral polarity in amphibian embryos was shown to be related to shape and location asymmetry of cytoplasm area containing clusters of yolk granules.
Animals↗
The cytoplasmic surface structures of uncoated vesicles in various tissues of rat as revealed by quick-freeze, deep-etching replicas.
We examined the cytoplasmic surface structures of the plasmalemmal vesicles in various tissues using quick-freeze, deep-etching replicas, and identified three types of cytoplasmic surface specializations. In addition to the baskets of clathrin-coated vesicles, stripe-surfaced and bumpy-surfaced vesicles could be identified. The striped patterns were clearly observed on the vesicles in endothelial cells and fibroblasts of various tissues, while in epithelial cells such as hepatocytes, renal proximal tubule cells, and superficial cells of the urinary bladder, instead of the striped patterns, rough-surfaced vesicles could be identified. These differences in 'uncoated' vesicles may suggest that there is the tissue specificity of the cytoplasmic surface structures of plasmalemmal vesicles.
Animals↗
Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification.
N- and C-terminal cytoplasmic domains of inwardly rectifying K (Kir) channels control the ion-permeation pathway through diverse interactions with small molecules and protein ligands in the cytoplasm. Two new crystal structures of the cytoplasmic domains of Kir2.1 (Kir2.1(L)) and the G protein-sensitive Kir3.1 (Kir3.1(S)) channels in the absence of PIP(2) show the cytoplasmic ion-permeation pathways occluded by four cytoplasmic loops that form a girdle around the central pore (G-loop). Significant flexibility of the pore-facing G-loop of Kir2.1(L) and Kir3.1(S) suggests a possible role as a diffusion barrier between cytoplasmic and transmembrane pores. Consistent with this, mutations of the G-loop disrupted gating or inward rectification. Structural comparison shows a di-aspartate cluster on the distal end of the cytoplasmic pore of Kir2.1(L) that is important for modulating inward rectification. Taken together, these results suggest the cytoplasmic domains of Kir channels undergo structural changes to modulate gating and inward rectification.
Amino Acid Sequence↗
Plasmodium vivax: malarial proteins associated with the membrane-bound caveola-vesicle complexes and cytoplasmic cleft structures of infected erythrocytes.
The identification of antigens of parasite origin associated with the altered membrane of Plasmodium vivax-infected erythrocytes was undertaken in this study. The 125I-lactoperoxidase catalyzed surface radiolabeling of trophozoite-infected erythrocytes revealed new bands of 95 and 70 kDa not labeled in normal erythrocytes. Erythrocyte membrane-enriched preparations from [35S]methionine biosynthetically labeled-infected erythrocytes also indicated that in addition to bands at 95 and 70 kDa, several other parasite proteins were possibly membrane associated. Five monoclonal antibodies (Mabs) reactive with P. vivax produced an immunofluorescent pattern of numerous small dots scattered over the entire infected erythrocyte. This pattern mimics that of Schuffner's stippling; small red dots seen in Giemsa-stained P. vivax-infected erythrocytes, which represent accumulations of dye in caveola-vesicle complexes (CVC). Four of the monoclonal antibodies immunoprecipitated a Triton X-100 detergent-insoluble 95-kDa parasite protein which was localized by immunofluorescent assay and immunoelectron microscopy exclusively to the CVC. Two of these Mabs were immunofluorescence reactive with the surface of intact infected erythrocytes in suspension. The fifth Mab, which also localized exclusively to the CVC structures, immunoprecipitated a Triton X-100 extractable protein of 70 kDa. Two other monoclonal antibodies reacted exclusively with the numerous membranous cleft structures found in the cytoplasm of infected erythrocytes. This cleft-associated parasite antigen was 28 kDa in size. Some of these Mabs recognize epitopes and produce similar IFA patterns on erythrocytes infected with P. cynomolgi, P. knowlesi, and P. ovale parasites, but not with P. falciparum- or P. brasilianum-infected erythrocytes.
Animals↗
Structural basis of motility in the microtubular axostyle: implications for cytoplasmic microtubule structure and function.
The gross morphology of the protozoan microtubule axostyle of Saccinobaculus ambloaxostylus can now be described in macromolecular detail. The left-handed coil of the axostyle is seen to be dependent upon the asymmetry inherent in the constituent microtubules as expressed by the specific array of linkages between microtubules and by a possible tendency for microtubules to coil into left-handed helices. The laminated sheets of microtubules are not aligned parallel to the long axis of the organelle, but become increasingly tilted off-axis as one descends through the sheets of microtubules from the convex to the concave surface of the axostyle. Fine-structural analysis of the axostyle indicates similarities of the linkages to dynein. The potential loci of the force-generating protein(s) are discussed as well as implications of the axostyle's structure on general microtubule function.
Animals↗