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PubMed1982

Intake of phosphatase-active plasma membrane into the cytoplasm of oocytes from sexually immature hamsters.

When thiamine pyrophosphate is used as substrate, heavily stained complexly branching cytoplasmic structures are seen in developing oocytes of the hamster between 8 and 12 days after birth. This coincides with the onset of the dictyate stage of first meiotic prophase. The structures appear to arise from the oocyte plasma membrane in two ways: (1) by proliferation and infolding of the membrane, and (2) by membrane being pushed into the cytoplasm by invaginating follicle cell processes. This appears to be followed by proliferation of the invaginated plasma membrane within the oocyte cytoplasm. Incubations with ATP or beta-glycerophosphate, with and without the inhibitor L-p-bromotetramisole, indicate that the staining is not due to the action of either ATPase or alkaline phosphatases. The origin and possible developmental significance of the reactive structures are discussed.

Adenosine Triphosphatases↗
PubMed1989

Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells.

Kinesin, a microtubule-activated ATPase and putative motor protein for the transport of membrane-bounded organelles along microtubules, was purified from bovine brain and used as an immunogen for the production of murine monoclonal antibodies. Hybridoma lines that secreted five distinct antikinesin IgGs were cloned. Three of the antibodies reacted on immunoblots with the 124-kD heavy chain of kinesin, while the other two antibodies recognized the 64-kD light chain. When used for immunofluorescence microscopy, the antibodies stained punctate, cytoplasmic structures in a variety of cultured mammalian cell types. Consistent with the identification of these structures as membrane-bounded organelles was the observation that cells which had been extracted with Triton X-100 before fixation contained little or no immunoreactive material. Staining of microtubules in the interphase cytoplasm or mitotic spindle was never observed, nor were associated structures, such as centrosomes and primary cilia, labeled by any of the antibodies. Nevertheless, in double-labeling experiments using antibodies to kinesin and tubulin, kinesin-containing particles were most abundant in regions where microtubules were most highly concentrated and the particles often appeared to be aligned on microtubules. These results constitute the first direct evidence for the association of kinesin with membrane-bounded organelles, and suggest a molecular mechanism for organelle motility based on transient interactions of organelle-bound kinesin with the microtubule surface.

Adenosine Triphosphatases↗
PubMed1976

[Electron microscopic investigation on the evolution stages of the trophozoite of Didymophyes gigantea (Sporozoa, Gregarinida). I. The fine structure of the proto- and epimerite and the relationship between host and parasite (author's transl)].

The fine structure of the epimerite and the protomerite of D. gigantea was investigated following the different stages of the evolution of the trophozoite. The first stage is mononucleate and very poor of cytoplasmic structures (Fig. 1). All following stages are polynucleate (Fig. 3). The septum between protomerite and deutomerite appears at the third stage (Fig. 22). The body of the gregarine is in all stages surrounded by a thick cell-wall constituted of three membranes. The limit between epimerite and protomerite is indicated by the existence of an osmiophilic basal ring just under the parasite's cell-wall. This basal ring has a transverse substructure with a periodical distance of 450 A (Fig. 12). The two inner membranes join together just beneath the basal ring, whereas the outer membrane continues and forms the single cell membrane of the epimerite (Fig.9). The epimerite displays a large number of microvillosities and evaginations of the membrane which increase considerably its surface (Figs. 11-14). The epimerite essentially contains ribosomes and mitochondria (Fig.6). The protomerite contains in addition to the usual cell organites cytoplasmic agglomerations consisting of endoplasmic reticulum, ribonucleoprotein and peripheric mitochondria. During evolution from stage IV to V, these agglomerations produce osmiophilic granula of different form and size, most of which are surrounded by an elementary membrane (Fig. 18). Beside these granula one can observe sometimes small spherical or lamellar structures (Fig. 21). Large bundles of microtubules run from the protomerite into the epimerite where they generally branch off and penetrate into the mitochondrial layer (Figs. 6, 19, 20). Between the parasite and the host-cell exists a space, the periparasitic space, without any cytoplasmic inclusions. The cell membrane of the host-cell has in the periparasitic space an outer cell-coat with a ripped pattern (Fig. 13). The microvillosities of the cell membrane disappear at this place. The host-cell cytoplasm displays a large number of microtubules and a fibrillar network (Figs. 13, 14). The importance of these structures for the relationship between parasite and host-cell is discussed.

Animals↗
PubMed1992

Intracellular distribution of a nuclear localization signal binding protein.

The transport of proteins into the nucleus requires the recognition of a nuclear localization signal sequence. Several proteins that interact with these sequences have been identified, including one of about 66 kDa. We have prepared antibodies that recognize the 66-kDa nuclear localization signal binding protein (NLSBP) and inhibit nuclear localization in vitro. By immunofluorescence, it is seen that the NLSBP is predominantly cytoplasmic and is distributed peripherally around the nucleus and the microtubule organizing center. There is also a weak punctate staining of the surface of the nucleus. Methanol-fixed cells can also be stained directly with fluorescently labeled karyophilic proteins. These stains reveal the same cytoplasmic structures as anti-NLSBP. The expression of the NLSBP is growth dependent. When cells grown to confluence are examined, the cytoplasmic staining is greatly reduced, leaving the punctate nuclear staining as the predominant feature. In serum-starved cells, very little staining of either the cytoplasm or the nucleus can be seen. Upon simulation by the addition of serum, the original cytoplasmic and nuclear envelope staining is restored. Cells grown in the presence of colchicine or taxol have an altered NLSBP distribution but apparently normal cytoplasmic nuclear transport.

Amino Acid Sequence↗
PubMed1980

Intracellular pH in single motile cells.

Cytoplasmic pH in single living specimens of Chaos carolinensis is determined microfluorometrically by measuring the ratio of fluorescence intensity of microinjected fluorescein-thiocarbamyl (FTC)-ovalbumin at two different excitation wavelengths. The probe is evenly distributed throughout, and confined to, the cytoplasm, and the fluorescence intensity ratio depends only upon pH. It is independent of pathlength, concentration of probe, divalent cations, and ionic strength. Ratios are calibrated with a standard curve generated in situ by adjusting internal pH of FTC-ovalbumin-containing amebae with weak acid and weak base or by injection of strong buffers. With this technique, the average cytoplasmic pH of freely moving ameba is found to be 6.75 (SD +/- 0.3). The pH of a given spot relative to the morphology of a moving ameba remains fairly constant (+/- 0.05 U), whereas the pH of two different spots in the same cell may differ by as much as 0.4 U, and average pH in different amebae ranges from 6.3 to 7.4, with a suggestion of clustering about pH 6.5 and 6.8. During wound healing, there is a local, transient drop in pH (as great as 0.35 U) at the wound site upon puncture, proportional in extent to the degree of damage. Comparison of tails and advancing pseudopod tips reveals no significant difference in cytoplasmic pH at this level of spatial (50 microns diameter spot) and temporal (1.3 s) resolution. Fluctuations in intracellular pH and/or intracellular free Ca++ may be involved in regulation of cytoplasmic structure and contractility.

Amoeba↗
PubMed2005

Real-time dynamics of the F-actin cytoskeleton during secretion from chromaffin cells.

Transmitted light images showed an intricate and dynamic cytoplasmic structural network in cultured bovine chromaffin cells observed under high magnification. These structures were sensitive to chemicals altering F-actin-myosin and colocalised with peripheral F-actin, beta-actin and myosin II. Interestingly, secretagogues induced a Ca2+-dependent, rapid (>10 second) and transitory (60-second cycle) disassembling of these cortical structures. The simultaneous formation of channel-like structures perpendicular to the plasmalemma conducting vesicles to the cell limits and open spaces devoid of F-actin in the cytoplasm were also observed. Vesicles moved using F-actin pathways and avoided diffusion in open, empty zones. These reorganisations representing F-actin transfer from the cortical barrier to the adjacent cytoplasmic area have been also confirmed by studying fluorescence changes in cells expressing GFP-beta-actin. Thus, these data support the function of F-actin-myosin II network acting simultaneously as a barrier and carrier system during secretion, and that transmitted light images could be used as an alternative to fluorescence in the study of cytoskeleton dynamics in neuroendocrine cells.

Actins↗
PubMed2000

pUL25 immunolocalization in human cytomegalovirus-infected and gene-transfected cells.

By means of confocal and electron microscope immunocytochemistry we have studied the localization of a recently described structural protein (pUL25) of human cytomegalovirus, in both infected cells and in cells transiently transfected with UL25. pUL25 localization in infected cells was observed in typical cytoplasmic structures characterized by a very electrondense texture previously reported to accumulate other tegument proteins. At the virion level pUL25 seems to localize at the interface between the tegument and the capsid of both intracytoplasmic and extracellular virions. In UL-25-transfected cells, pUL25 has been found in characteristic para-crystalline cytoplasmic aggregates, suggesting its intrinsic ability to aggregate in a regular subunit pattern.

Animals↗
PubMed1981

[Ultrastructure of the gastric endocrine cells of hungry and fed sexually immature rats].

Six types of endocrine cells (G, D, D1, EC, ECL and A-like) were identified in gastric mucosa of immature rats by electron microscopy. They differ in the structure, way of formation, maturation and release of their secretory granules. They are also distinguished by the degree of the development of other cytoplasmic structures. Feeding after a long-term (48 h) starvation causes changes in te size and density of activation of the synthetic processes. These facts indicate the role of the above cell and their products (gastrin, histamine) in the stimulation of gastric secretion in the early stages of digestion.

Animals↗
PubMed1995

Membrane potential and input resistance are ambiguous measures of sealing of transected cable-like structures.

For many years, membrane potential (Vm) and input resistance have been used to characterize the electrophysiological nature of a seal (barrier) that forms at the cut end of a transected axon or other extended cytoplasmic structure. Data from a mathematical and an analog model of a transected axon and other theoretical considerations show that steady-state values of Vm and input resistance measured from any cable-like structure provide a very equivocal assessment of the electrical barrier (seal) at the cut end. Extracellular assessments of injury currents almost certainly provide a better electrophysiological measure of the status of plasma membrane sealing because measurements of these currents do not depend on the cable properties of extended cytoplasmic processes after transection.

Animals↗
PubMed1976

Accumulation and decay of messenger ribonucleic acid in mouse kidney.

The stability of polyadenylated messenger ribonucleic acid(mRNA) from cytoplasmic structures sedimenting faster than 40S was analyzed in normal mouse kidney. Incorporation of radioactivity into poly(A)-containing and poly(A)-lacking cytoplasmic RNAs separated by oligo(dT)-cellulose chromatography was determined after sedimentation of RNA IN SODIUM DODECYL SULFATE CONTAINING SUCROSE DENSITY GRADIENTS. Radioactivity accumulated in poly(A)-containing RNA during the first 6 h and then decayed exponentially. Beginning 8-12h after administering label, two components were evident in the decay curve of poly(A)-containing RNA; the short-lived component (approximately 57% of newly synthesized molecules) had an apparent half-life of 6h, and the second class (approximately 43% of new mRNA) was more stable, decaying with a 24-h half-life. These studies provide the basis for examining the regulation of mRNA stability during compensatory renal hypertrophy.

Animals↗
PubMed1980

Morphometric ultrastructural analysis of mouse embryo during early development.

During preimplantation development of the mouse embryos a number of qualitative morphological changes is observed. The aim of the present paper was to perform the stereological analysis of some cytoplasmic structures which play an important role during development. The experiments were performed with embryos of Swiss mouse strain. Material for qualitative and quantitative evaluation at the ultrastructural level was prepared according to the method developed in our laboratory. Stereological investigations were performed after Weibel. The results were statistically elaborated. Volume fraction of the nucleoli, mitochondria and Golgi apparatus related to cytoplasm or total cells were evaluated. Additionally, the shape of the mitochondria was determined as a ratio long to short arm of this structure. Beginning with the 1-cell stage up to the morula the volume fraction of the nucleoli does not change. It is only in the blastocyst that a statistically significant increase in the fraction of these structures was noted both in the inner cell mass and in the trophoblast. After each cleavage of mouse embryos cell, mitochondria change their shape. They became round with transvere cristae in the morula stage and elongated in the blastocyst. Volume fraction of the mitochondria markedly increased after the 1sst and 4th embryos division. In the course of cleavage in the mouse a morphological evaluation of Golgi apparatus occurs from the form of swollen dictyosomes scattered in the whole cytoplasm in 1-cell embryos to the typical structure in the blastocyst. Volume fraction of the Golgi apparatus of the total cell is markedly decreased after the 1st cleavage division and up to the morula stage decreases slightly. In the blastocyst both in the inner cell mass and trophoblast Golgi apparatus markedly increases.

Animals↗
PubMed1986

Curvilinear, three-dimensional motion of chromatin domains and nucleoli in neuronal interphase nuclei.

The term "nuclear rotation" refers to a motion of nucleoli within interphase nuclei of several cell types. No mechanism or function has been ascribed to this phenomenon, and it was unknown whether nuclear structures in addition to nucleoli participate in this motion. Moreover, it was unclear whether nuclear rotation occurs independent of concurrent motion of juxtanuclear cytoplasm. The work reported here presents quantitative evidence, for three-dimensional intranuclear, tandem motion of fluorescently labeled chromatin domains associated with nucleoli and those remote from nucleoli. The results show that such motion is curvilinear, that it is not restricted to nucleoli, and, moreover, that it occurs independently of motion of juxtanuclear, cytoplasmic structures. These results suggest that this motion represents karyoplasmic streaming and its function is to transpose to nuclear pores those chromatin domains actively transcribed.

Cell Nucleolus↗
PubMed1995

Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure.

Peptides representing the N-terminal domain (Ia) of the cardiac sarcoplasmic reticulum protein phospholamban (residues 1-25 [PLB(1-25)] and a phosphorylated form [pPLB(1-25)]) were synthesized and their conformations examined using circular dichroism and nuclear magnetic resonance spectroscopy. In aqueous solution, both PLB(1-25) and pPLB(1-25) adopt a primarily disordered conformation. In 30% trifluoroethanol/10 mM phosphate, PLB(1-25) exhibits a CD spectrum consistent with 60% helical structure. This value decreases to 27% for the phosphorylated peptide. CD spectra in 2% SDS indicate 40% alpha-helix for PLB(1-25) and 20% for pPLB(1-25). Full chemical shift assignments were obtained by conventional homonuclear NMR methodologies for both PLB(1-25) and pPLB(1-25) in 30% trifluoroethanol/water and 300 mM SDS. The solution structure of PLB(1-25) in 30% TFE/water was determined from distance geometry calculations using 54 NOE distance constraints and 17 torsion angle constraints. In the family of 20 calculated conformers, the root mean square deviation from the mean structure is 0.79 A for backbone heavy atoms of residues 1-17. The structure comprises a regular alpha-helix extending from M1 to S16 with the remaining C-terminal residues disordered. The calculated structure is supported by analysis of C alpha H secondary shifts which are significantly negative for residues 1-16. Chemical shift degeneracy is substantially more extensive in the phospho form and precludes a direct comparison of calculated structures. However, the magnitudes of upfield secondary shifts are decreased by 20% in residues 1-11 and are not significantly helical for residues 12-16 according to the criteria of Wishart et al. [(1992) Biochemistry 31, 1647-1651]. 3JHN alpha coupling constants measured for I12, R13, A15, and S16 also suggest that residues 12-16 undergo a local unwinding of the helix upon phosphorylation. Similar results are obtained for PLB(1-25) and pPLB(1-25) in 300 mM perdeuterated sodium dodecyl sulfate except that differences in backbone dynamics for the helical and nonhelical regions of the peptide are evident in the DQF-COSY line shapes for fingerprint cross-peaks. This disruption of structure at the C-terminus of the helix suggests a model for phosphorylation-induced dissociation of the PLB/Ca(2+)-ATPase complex.

Amino Acid Sequence↗
PubMed2000

The functional organization of the nucleolus in proliferating plant cells.

The nucleolus is a prominent nuclear organelle which morphologically expresses all functional steps necessary for the synthesis of ribosomes, from transcription of rRNA genes to the assembly and maturation of preribosomal particles and their transport to the cytoplasm. Structurally, the nucleolus contains some basic components common to practically all cell types, namely fibrillar centers (FCs), the dense fibrillar component (DFC), and the granular component (GC); however, the organization and distribution of these components is highly variable, depending on cell identity and functional status. The different steps of ribosome biogenesis are not strictly correlated with the structural components of the nucleolus. Thus, FCs are most likely the anchoring sites for the accumulation of rDNA, and the sites where the assembly of transcription complexes takes place, but transcription of rRNA genes actually occurs at discrete points in the transition zone between FCs and the DFC. The DFC is a structurally homogeneous, but functionally heterogeneous component in which transcription and some early and advanced steps of pre-rRNA processing develop successively in a gradual fashion, from transition with FCs to transition with the GC. Finally, the GC is the site of the later steps of preribosomal processing, including the final assembly of ribosomal proteins for the export of mature particles to the cytoplasm. The rate of ribosome biogenesis, as well as the structure of the nucleolus, are highly influenced by the proliferation status of the cell, and by factors regulating cell cycle progression. These factors are nucleolar proteins, such as nucleolin, which are targets of signal transduction mechanisms, being at the same time regulators of key steps in preribosome synthesis and processing. Thus, many features of the nucleolus, such as the structural organization of its components, the level and distribution of certain nucleolar proteins and, in general, the rate of ribosome biogenesis, show profound variations throughout cell cycle periods. Particularly interesting is the behavior of the nucleolus during mitosis, in which its structure is disorganized and its activity is stopped, even though the individual transcription and processing complexes are not disassembled, but carried from one cell generation to the next one in such a way that the daughter-cell nucleoli are built with materials coming from the parent-cell nucleolus. Transcription complexes remain assembled at the chromosomal nucleolar organizer in which the rRNA genes are clustered, and processing complexes are carried at the chromosome periphery, and then they are organized into discrete entities called prenucleolar bodies, whose fusion, together with the resumption of transcription and processing, originates the new nucleolus.

Animals↗
PubMed2000

Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene.

UEV proteins are enzymatically inactive variants of the E2 ubiquitin-conjugating enzymes that regulate noncanonical elongation of ubiquitin chains. In Saccharomyces cerevisiae, UEV is part of the RAD6-mediated error-free DNA repair pathway. In mammalian cells, UEV proteins can modulate c-FOS transcription and the G2-M transition of the cell cycle. Here we show that the UEV genes from phylogenetically distant organisms present a remarkable conservation in their exon-intron structure. We also show that the human UEV1 gene is fused with the previously unknown gene Kua. In Caenorhabditis elegans and Drosophila melanogaster, Kua and UEV are in separated loci, and are expressed as independent transcripts and proteins. In humans, Kua and UEV1 are adjacent genes, expressed either as separate transcripts encoding independent Kua and UEV1 proteins, or as a hybrid Kua-UEV transcript, encoding a two-domain protein. Kua proteins represent a novel class of conserved proteins with juxtamembrane histidine-rich motifs. Experiments with epitope-tagged proteins show that UEV1A is a nuclear protein, whereas both Kua and Kua-UEV localize to cytoplasmic structures, indicating that the Kua domain determines the cytoplasmic localization of Kua-UEV. Therefore, the addition of a Kua domain to UEV in the fused Kua-UEV protein confers new biological properties to this regulator of variant polyubiquitination.

Amino Acid Sequence↗
PubMed1996

Cytoplasmically sequestered wild-type p53 protein in neuroblastoma is relocated to the nucleus by a C-terminal peptide.

Cytoplasmic sequestration of wild-type p53 protein occurs in a subset of primary human tumors including breast cancer, colon cancer, and neuroblastoma (NB). The sequestered p53 localizes to punctate cytoplasmic structures that represent large protein aggregates. One functional consequence of this blocked nuclear access is impairment of the p53-mediated G1 checkpoint after DNA damage. Here we show that cytoplasmic p53 from NB cells is incompetent for specific DNA binding, probably due to its sequestration. Importantly, the C-terminal domain of sequestered p53 is masked, as indicated by the failure of a C-terminally directed antibody to detect p53 in these structures. To determine (i) which domain of p53 is involved in the aggregation and (ii) whether this phenotype is potentially reversible, we generated stable NB sublines that coexpress the soluble C-terminal mouse p53 peptide DD1 (amino acids 302-390). A dramatic phenotypic reversion occurred in five of five lines. The presence of DD1 blocked the sequestration of wild-type p53 and relocated it to the nucleus, where it accumulated. The nuclear translocation is due to shuttling of wild-type p53 by heteroligomerization to DD1, as shown by coimmunoprecipitation. As expected, the nuclear heterocomplexes were functionally inactive, since DD1 is a dominant negative inhibitor of wild-type p53. In summary, we show that nuclear access of p53 can be restored in NB cells.

Animals↗
PubMed1990

Electron microscopy of hybridoma cells with special regard to monoclonal antibody production.

Electron microscopy of mouse hybridoma cell lines shows that the major difference between non, low and high producer cell lines is the amount of endoplasmic reticulum. Vesicular-tubular or cavernous structures of endoplasmic reticulum, which can survive long after cell death, are particularly abundant in producer cell lines. Immunogold labelling with anti-mouse IgG reveals that antibodies are predominantly located in these structures. The cell membrane undergoes structural changes during the late stages of batch culture with the disappearance of microvilli and the appearance of blebs and deep indentations. Necrosis disrupts the cytoplasmic structures and the nucleus is last to degrade.

Animals↗
PubMed1998

Architectural features of the Salmonella typhimurium flagellar motor switch revealed by disrupted C-rings.

The three-dimensional surface topology of rapid-frozen Salmonella typhimurium flagellar hook basal body complexes was studied by stereo-examination of thin-film metal replicas. The complexes contained the extended cytoplasmic structure, composed of the switch complex proteins; FliG, FliM, and FliN. Distinct nanometer-scale element arrays, separated by grooves, defined the outer surface of the cytoplasmic (C-) ring. The number of array elements was comparable to previously determined FliG and FliM copy numbers in the basal body. In addition to basal body complexes lacking C-rings, complexes containing incomplete C-rings were identified. The incomplete C-rings had lost segments of the proximal array. Basal bodies with the distal C-ring array alone were not found. These findings are compatible with the spatial organization of the flagellar switch suggested by previous biochemical data.

Bacterial Proteins↗