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Quantitation of turnover and export to the cytoplasm of hnRNA transcribed in the Balbiani rings.

Some quantitative parameters of the intranuclear metabolism and export to the cytoplasm of Balbiani ring 1 and 2 RNA molecules in salivary gland cells of Chironomus tentans have been determined. Growing RNA chains in the Balbiani rings attain uniform labeling with RNA precursors after 20 min of incorporation. The specific activity of 75S RNA released from the Balbiani rings into the nuclear sap increases rapidly and reaches a maximum level between 90 and 180 min of labeling. After 20 min, labeled 75S RNA enters the cytoplasm and accumulates at a linear rate. However, only a small proportion of the RNA produced at the Balbiani ring loci can subsequently be recovered in the nuclear sap (14-17%) or cytoplasm (4-7%) as 75S RNA; presumably the remainder is degraded entirely. Experiments using inhibitors of elongation (actinomycin D) or initiation (5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole) revealed that no significant quanity of the 75S RNA transcribed can be chased into the cytoplasm. Both the kinetics of entry of labeled 75S RNA into the cytoplasm-that is, a constant rate of increase after a brief lag-and chase data are incompatible with a precursor-product relationship between the great majority of nuclear 75S RNA and cytoplasmic 75S RNA with messenger characteristics. The results are discussed in relation to the possibility that a post-transcriptional control mechanism is operating in these cells.

Animals↗

The cytoplasmic domain of the cell adhesion molecule L1 is not required for homophilic adhesion.

L1 is a highly conserved cell adhesion molecule with complete homology of the cytoplasmic domain between the known mammalian protein sequences. Since the cytoplasmic domains of other adhesion molecules have been shown to influence adhesion, we have investigated the effects of deletion of the cytoplasmic domain on the ability of L1 to mediate homophilic adhesion. Full length L1 and a truncated L1, lacking 95% of the cytoplasmic domain, were expressed in myeloma cells. Independent stable transfectants were assayed for the ability to form aggregates. Myelomas expressing L1 lacking the cytoplasmic domain were able to form cell aggregates as well as the myelomas expressing full length L1. Cell aggregate formation was correlated with the level of L1 expression, and the aggregation could be blocked by anti-L1 Fabs. Similar results were obtained in adhesion assays of the myeloma cells to substrate-bound L1. These results indicate that the cytoplasmic domain of L1 is not required for homophilic interactions.

Amino Acid Sequence↗

ATP-induced cytoplasmic [Ca2+] increases in isolated cochlear outer hair cells. Involved receptor and channel mechanisms.

Outer hair cells (OHC) of the mammalian cochlea are thought to preprocess the sound signal by active movements, which can be induced by electrical or chemical stimulation, e.g. depolarization evoked by high [K+] or increased cytoplasmic [Ca2+]. Extracellular ATP has been found to induce cytoplasmic [Ca2+] increases in OHC but involved mechanisms have not been elucidated. Cytoplasmic [Ca2+] was measured in non-enzymatically isolated single OHC using Fura-2 microspectrometry. Results, using ATP/derivatives and other P2-purinergic receptor (P2R) ligands, as well as Ca(2+)-channel blockers and pertussis toxin, revealed several signal transduction pathways that increase cytoplasmic [Ca2+] in OHC: a P2-purinergic receptor (P2R)--G-protein--effector (phospholipase C or an ion channel) system and a voltage-dependent Ca2+ channel. Agonist potency studies denote a pattern analogous to that found in skeletal muscle, i.e. ATP-alpha-S > ATP = 2-methyl-S-ATP >> ADP > alpha,beta-methylene-ATP, but no activation by ADP beta F or UTP, leaving a choice of P2y or P2zR subtypes. The latter possibility gained strength from calculations showing that up to 8% of ATP may have formed the P2zR agonist ATP4- in the experimental medium. Experiments in Ca(2+)-free medium and with pertussis toxin revealed that the main Ca2+ source was intracellular. Pertussis toxin did not affect [Ca2+] increase induced by carbachol. Acetylcholine, administered a few seconds before ATP, did not affect total cytoplasmic [Ca2+] increases. Induced cytoplasmic [Ca2+] increases were high enough (> 500 nM at 50 microM ATP/derivatives) to hyperpolarize the OHC membrane by opening K(+)-channels and decreased little with time.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine Triphosphate↗

Prognostic significance of cytoplasmic p53 overexpression in colorectal cancer. An immunohistochemical analysis.

p53 overexpression was studied by immunohistochemistry in 96 consecutive colorectal cancer patients, subdividing positive specimens according to two staining patterns: cytoplasmic or nuclear. Forty-seven per cent of the cases were p53 positive, a significant correlation being found with Dukes' stage (P = 0.0036). A prevalence of nuclear staining was observed in Dukes' B and cytoplasmic in Dukes' D stages. After 36 months, 23% of the patients had a recurrence, and 45% were p53 positive, all Dukes' C-D stage with cytoplasmic staining. The Kaplan-Meier curve showed a significant correlation between p53 cytoplasmic staining and disease-free survival period (P = 0.002). With respect to disease-free survival, the Cox proportional hazard regression test, comparing p53 positivity with Dukes' stage, showed the latter to be the most significant variable. In our series of patients, advanced Dukes' stage tumours were localised in the right colon, where a higher percentage of p53 positivity (67% versus 40% of the left side), as well as a higher frequency of cytoplasmic staining was observed. In conclusion, from the data obtained, a strong correlation between p53 cytoplasmic staining and patient prognosis is clearly indicated.

Adult↗

Loop X/XI, the largest cytoplasmic loop in the membrane-bound melibiose carrier of Escherichia coli, is a functional re-entrant loop.

The melibiose carrier of Escherichia coli is a membrane-bound sugar-cation cotransporter consisting of 12 transmembrane helices connected by cytoplasmic and periplasmic loops, with both N- and C-terminus on the cytoplasmic side. Using a functional cysteine-less carrier, cysteine was substituted individually for residues 347-378 that comprise the largest cytoplasmic loop X/XI. The majority of the cysteine mutants have good protein expression levels. The cysteine mutants were studied for their transport activities, and the inhibitory effects of two sulfhydryl reagents, PCMBS (7-A long) and BM (29-A long). Cysteine substitution resulted in substantial loss of transport in 12 mutants. While PCMBS caused significant inhibition in only two mutants, T373C and V376C, from the periplasmic side (in a substrate-protective manner), more extensive inhibition pattern was observed from the cytoplasmic side, in seven mutants: V353C, Y358C, V371C, Q372C, T373C, V376C and G378C, suggesting that these residues are along the sugar pathway in the aqueous channel, close to the cytoplasmic side. Furthermore, the inhibitory effect of BM on the inside-out vesicles of the above mutants was clearly less than that of PCMBS, suggesting channel space limitation to large molecules, consistent with those residues being inside the channel. Three second-site revertants (A350C/F268L, A350C/I22S, and A350C/I22N) were selected. They may suggest proximities between loop X/XI and helices I and VIII, in agreement with a re-entrant loop structure. Self thiol cross-linkings of the cysteine mutants on loop X/XI failed to form dimers, suggesting that most of the loop is not surface-exposed from cytoplasmic side. Together, these results strongly indicated a functional re-entrant loop mechanistically important in Na+-coupled transporters.

4-Chloromercuribenzenesulfonate↗

Developmentally regulated cytoplasmic retention of the transcription factor XMI-ER1 requires sequence in the acidic activation domain.

Xmi-er1 is a fibroblast growth factor regulated immediate-early gene that is activated during mesoderm induction in Xenopus embryonic explants. This gene encodes a nuclear protein with potent transcriptional regulator activity and overexpression of XMI-ER1 in Xenopus embryos inhibits mesoderm induction and leads to truncations along the anteroposterior axis. We showed previously that XMI-ER1 is retained in the cytoplasm during cleavage stages and only begins to appear in the nucleus at mid-blastula. Such developmentally regulated nuclear translocation may represent an important mechanism for regulating XMI-ER1 activity in the early embryo. Here, we investigate different mechanisms that might control nuclear translocation of XMI-ER1. Using alpha-amanitin to inhibit transcription, we show that nuclear localization is not dependent on zygotic transcription. Nor is it the result of a developmentally regulated import pathway, as the XMI-ER1 nuclear localization signal (NLS) fused to beta-galactosidase (betagal) was able to direct nuclear translocation prior to mid-blastula. Fusion of an additional, heterologous NLS to the N-terminus of XMI-ER1 was not sufficient to overcome cytoplasmic retention, indicating that retention does not involve NLS masking, but rather binding to a cytoplasmic anchor. The anchoring molecule is not an RNA, as microinjection of RNase A did not affect the timing of nuclear translocation. Western blot analysis using antibodies that recognize phosphorylated residues revealed that, while XMI-ER1 is not itself phosphorylated, it is associated with two differentially phosphorylated proteins, suggesting that the anchoring mechanism may involve interaction with a cytoplasmic protein(s). A series of XMI-ER1 deletion mutants was utilized to map the putative retention domain. Our analysis revealed that amino acids 144-175, containing the fourth acidic stretch of the acidic activation domain, are required for retention. These results suggest that XMI-ER1 is retained in the cytoplasm of the early embryo by interaction of the region containing amino acids 144-175 with a cytoplasmic anchor.

Animals↗

Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments.

The nuclear pore complex (NPC) controls transport of macromolecules across the nuclear envelope. It is large and complex but appears to consist of only approximately 30 different proteins despite its mass of > 60MDa. Vertebrate NPC structure has been analyzed by several methods giving a comprehensive architectural model. Despite our knowledge of yeast nucleoporins, structural data is more limited and suggests the basic organization is similar to vertebrates, but may lack some peripheral and other components. Using field emission scanning electron microscopy to probe NPC structure we found that the yeast, like higher eukaryotic, NPCs contain similar peripheral components. We can detect cytoplasmic rings and evidence of nucleoplasmic rings in yeasts. A filamentous basket is present on the nucleoplasmic face and evidence for cytoplasmic filaments is shown. We observed a central structure, possibly the transporter, that which may be linked to the cytoplasmic ring by internal filaments. Immuno-gold labeling suggested that Nup159p may be attached to the cytoplasmic ring, whereas Nup116p may be associated, partly, with the cytoplasmic filaments. Analysis of a Nup57p mutant suggested a role in maintaining the stability of cytoplasmic components of the NPC. We conclude that peripheral NPC components appear similar in yeasts compared to higher organisms and present a revised model for yeast NPC structural composition.

Animals↗

Mammary epithelial cell-cycle progression via the alpha(2)beta(1) integrin: unique and synergistic roles of the alpha(2) cytoplasmic domain.

The alpha(2)beta(1) integrin supports cell-cycle progression of mammary epithelial cells adherent to type I collagen matrices. Integrin collagen receptors containing the alpha(2) cytoplasmic domain stimulated expression of cyclin E and cyclin-dependent kinase (cdk)2, resulting in cyclin E/cdk2 activation in the absence of growth factors other than insulin. Integrin collagen receptors in which the alpha(2) cytoplasmic domain was replaced by the alpha(1) cytoplasmic domain or an alpha(2) subunit cytoplasmic domain truncated after the GFFKR sequence failed to stimulate cyclin E/cdk2 activation or entry into S phase in the absence of growth factors. Although overexpression of cyclins D or E or cdk2 in cells expressing the integrin collagen receptor with the alpha(1)-integrin cytoplasmic domain did not restore G(1) progression when mammary epithelial cells adhered to type I collagen, co-expression of cyclin E and cdk2 did rescue the ability of the transfectants to enter S phase. Activation of cyclin E/cdk2 complex by mammary epithelial cells required synergy between adhesion mediated by an integrin collagen receptor containing the alpha(2)-integrin subunit cytoplasmic domain and the insulin receptor.

Breast↗

Effects of cytoplasmic and luminal pH on Ca(2+) release channels from rabbit skeletal muscle.

Ryanodine receptor (RyR)-Ca(2+) release channels from rabbit skeletal muscle were incorporated into lipid bilayers. The effects of cytoplasmic and luminal pH were studied separately over the pH range 5-8, using half-unit intervals. RyR activity (at constant luminal pH of 7.5) was inhibited at acidic cytoplasmic pH, with a half-inhibitory pH (pH(I)) approximately 6.5, irrespective of bilayer potential and of whether the RyRs were activated by cytoplasmic Ca(2+) (50 microM), ATP (2 or 5 mM), or both. Inhibition occurred within approximately 1 s and could be fully reversed within approximately 1 s after brief inhibition or within approximately 30-60 s after longer exposure to acidic cytosolic pH. There was no evidence of any hysteresis in the cytoplasmic pH effect. Ryanodine-modified channels were less sensitive to pH inhibition, with pH(I) at approximately 5.5, but the inhibition was similarly reversible. Steady-state open and closed dwell times of RyRs during cytoplasmic pH inhibition suggest a mechanism where the binding of one proton inhibits the channel and the binding of two to three additional protons promotes further inhibited states. RyR activity was unaffected by luminal pH in the pH range 7.5 to 6.0. At lower luminal pH (5-5.5) most RyRs were completely inhibited, and raising the pH again produced partial to full recovery in only approximately 50% of cases, with the extent of recovery not detectably different between pH 7.5 and pH 9. The results indicate that isolated skeletal muscle RyRs are not inhibited as strongly by low cytoplasmic and luminal pH, as suggested by previous single-channel studies.

Adenosine Triphosphate↗

Short class I major histocompatibility complex cytoplasmic tails differing in charge detect arbiters of lateral diffusion in the plasma membrane.

Directed and Brownian movement of class I major histocompatibility complex (MHC) molecules on cell membranes is implicated in antigen presentation. Previous studies indicated that the class I MHC cytoplasmic tail imposes constraints on the molecule's diffusion. Here we used single particle tracking to study the mobility of the wild-type mouse H-2L(d) class I MHC molecule and of seven cytoplasmic tail variants. Six of the variants have cytoplasmic tails of four or seven residues (differing in net charge), and one is tailless, yet all are susceptible to confinement in membrane domains. However, truncation of the cytoplasmic tail to 0-4 residues decreases the proportion of particles exhibiting confined diffusion and increases the proportion exhibiting simple diffusion. Particularly for the truncated mutants (tail length of 0-7 residues), many of the particles have complex trajectories and do not move at a constant speed or in the same mode of diffusion throughout the observation period. Several particles of the tailless H-2L(d) mutant display a type of directed diffusion that is rarely observed for other H-2L(d) mutants. Taken together, these data show that even short cytoplasmic tails can influence markedly class I MHC mobility and that cytoplasmic tail length and sequence affect the molecule's diffusion in the membrane.

Animals↗

Reference phase analysis of free and bound intracellular solutes. II. Isothermal and isotopic studies of cytoplasmic sodium, potassium, and water.

The intracellular reference phase (RP) method and ultra-low temperature micro-dissection were used for isothermal and isotopic phase distribution studies of Na(+), K(+), and water in amphibian oocyte cytoplasm. One-third of the cytoplasmic water is available as solvent for [(3)H]sucrose. This fraction, designated c1, quantitatively coincides with the water volume in which Na(+) and K(+) are freely diffusible. Two-thirds of the cytoplasmic water is inaccessible to sucrose and is designated c2. The Na(+) and K(+) associated with c2 are extremely slowly exchanging (bound) and at different concentrations than in c1. The cations in c1 are in mass-action equilibria with those in c2, each described by an equation of the formC(c) (i) = C(c) (1) (i) + C(c) (2) (i) = q(i).C(RP) (i) + (max)C(c) (2) (i).f(C(RP) (i)in which C(c) (i) is the cytoplasmic Na(+) or K(+) concentration, C(c) (1) (i) is the free, and C(c) (2) (i) the bound cation concentration averaged over the cytoplasmic water. q(i) is the fractional free solute space, C(RP) (i) the RP concentration, (max)C(c) (2) (i) the concentration of binding sites, and the function f is satisfied by the Langmuir isotherm. Numerical values for the variables of the isotherm are determined. Activity coefficients are calculated from RP data and provide a basis for generalizing the oocyte results to other cells. The conclusion is drawn that both c1 and c2 are widely distributed in cells, and that cellular ionic activities involve two distinct systems: the cell-membrane system and an adsorbed water ion-exchange-like buffering system. Alternative explanations for the two-component cytoplasm are considered. A model is proposed in which c1 is a normal intracellular aqueous phase controlled by the plasma membrane, whereas c2 consists of water and ions adsorbed in hydrate crystalline structures. In oocytes these structures are identified with yolk platelets.

Animals↗

Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.

The second half of the photocycle of the light-driven proton pump bacteriorhodopsin includes proton transfers between D96 and the retinal Schiff base (the M to N reaction) and between the cytoplasmic surface and D96 (decay of the N intermediate). The inhibitory effects of decreased water activity and increased hydrostatic pressure have suggested that a conformational change resulting in greater hydration of the cytoplasmic region is required for proton transfer from D96 to the Schiff base, and have raised the possibility that the reversal of this process might be required for the subsequent reprotonation of D96 from the cytoplasmic surface. Tilt of the cytoplasmic end of helix F has been suggested by electron diffraction of the M intermediate. Introduction of bulky groups, such as various maleimide labels, to engineered cysteines at the cytoplasmic ends of helices A, B, C, E, and G produce only minor perturbation of the decays of M and N, but major changes in these reactions when the label is linked to helix F. In these samples the reprotonation of the Schiff base is accelerated and the reprotonation of D96 is strongly retarded. Cross-linking with benzophenone introduced at this location, but not at the others, causes the opposite change: the reprotonation of the Schiff base is greatly slowed while the reprotonation of D96 is accelerated. We conclude that, consistent with the structure from diffraction, the proton transfers in the second half of the photocycle are facilitated by motion of the cytoplasmic end of helix F, first away from the center of the protein and then back.

Bacteriorhodopsins↗

Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion.

The green fluorescent protein (GFP) was used as a noninvasive probe to quantify the rheological properties of cell cytoplasm. GFP mutant S65T was purified from recombinant bacteria for solution studies, and expressed in CHO cell cytoplasm. GFP-S65T was brightly fluorescent in solution (lambda ex 492 nm, lambda em 509 nm) with a lifetime of 2.9 ns and a rotational correlation time (tc) of 20 ns. Recovery of GFP fluorescence after photobleaching was complete with a half-time (t1/2) in aqueous saline of 30 +/- 2 ms (5-micron diameter spot), giving a diffusion coefficient of 8.7 x 10(-7) cm2/s. The t1/2 was proportional to solution viscosity and was dependent on spot diameter. In contrast to fluorescein. GFP photobleaching efficiency was not affected by solution O2 content, triplet state quenchers, singlet oxygen scavengers, and general radical quenchers. In solutions of higher viscosity, an additional, rapid GFP recovery process was detected and ascribed to reversible photobleaching. The t1/2 for reversible photobleaching was 1.5-5.5 ms (relative viscosity 5-250), was independent of spot diameter, and was unaffected by O2 or quenchers. In cell cytoplasm, time-resolved microfluorimetry indicated a GFP lifetime of 2.6 ns and a tc of 36 +/- 3 ns, giving a relative viscosity (cytoplasm versus water) of 1.5. Photobleaching recovery of GFP in cytoplasm was 82 +/- 2% complete with a t1/2 of 83 +/- 6 ms, giving a relative viscosity of 3.2. GFP translational diffusion increased 4.7-fold as cells swelled from a relative volume of 0.5 to 2. Taken together with measurements of GFP translation and rotation in aqueous dextran solutions, the data in cytoplasm support the view that the primary barrier to GFP diffusion is collisional interactions between GFP and macromolecular solutes.

Animals↗

Engineering stable cytoplasmic intrabodies with designed specificity.

Many attempts have been made to develop antibody fragments that can be expressed in the cytoplasm ("intrabodies") in a stable and functional form. The recombinant antibody fragment scFv(F8) is characterised by peculiarly high in vitro stability and functional folding in both prokaryotic and eukaryotic cytoplasm. To dissect the relative contribution of different scFv(F8) regions to cytoplasmic stability and specificity we designed and constructed five chimeric molecules (scFv-P1 to P5) in which several groups of residues important for antigen binding in the poorly stable anti-hen egg lysozyme (HEL) scFv(D1.3) were progressively grafted onto the scFv(F8) scaffold. All five chimeric scFvs were expressed in a soluble form in the periplasm and cytoplasm of Escherichia coli. All the periplasmic oxidised forms and the scFv(P3) extracted from the cytoplasm in reducing conditions had HEL binding affinities essentially identical (K(d)=15nM) to that of the cognate scFv(D1.3) fragment (K(d)=16nM). The successful grafting of the antigen binding properties of D1.3 onto the scFv(F8) opens the road to the exploitation of this molecule as a scaffold for the reshaping of intrabodies with desired specificities to be targeted to the cytoplasm.

Amino Acid Sequence↗

Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain.

The cytoplasmic domains of viral glycoproteins influence the trafficking and subcellular localization of the glycoproteins and their incorporation into virions. They also promote correct virus morphology and viral budding. The cytoplasmic domains of murine-leukemia-virus envelope-protein TM subunits regulate membrane fusion. During virion maturation the carboxy-terminal 16 amino acid residues of the TM protein are removed by the retroviral protease. Deletion of these residues activates envelope-protein-mediated membrane fusion. Our quantitative analysis of the effects of Moloney murine leukemia virus TM mutations on envelope-protein function support the proposition that a trimeric coiled coil in the TM cytoplasmic domain inhibits fusion. The data demonstrate that cleavage of the TM cytoplasmic domain is not required for viral entry and provide evidence for a model in which fusogenic and nonfusogenic conformations of the envelope protein exists in an equilibrium that is regulated by the cytoplasmic domain. In addition, a conserved tyrosine residue in the TM cytoplasmic domain was shown to play an important role in envelope-protein incorporation into retroviral particles.

3T3 Cells↗

Modification of virus infectivity by cytoplasmic tail of HIV-1 TM protein.

Envelope glycoprotein incorporation is an essential process in formation of infectious particles of human immunodeficiency virus. Accumulated data have indicated that the cytoplasmic tail of Env gp41 is required for efficient incorporation. By analyzing mutant viruses with truncated cytoplasmic tails, we found that the domain was required in a cell-type-dependent manner for maintaining virus infectivity. Although the viruses with truncated cytoplasmic tails produced from HeLa, A3.01 and SupT1 cells showed a greatly reduced infectivity, those from SW480 and MT-4 cells retained a significant infectivity. To clarify the different effect of the cytoplasmic tail mutation on virus infectivity, we performed biochemical studies on the virions produced from HeLa and SW480 cells. Although the truncation of cytoplasmic tail appeared to reduce the Env incorporation in both cell lines, it caused a significant incorporation of Env precursor with HeLa cells. The results suggested that the cytoplasmic tail regulated selective incorporation of processed Env into virions in a cell-type-dependent manner.

Cell Line↗

Cytoplasmic delivery and nuclear targeting of synthetic macromolecules.

Delivery of macromolecular drugs (e.g. antisense oligonucleotides, polymer-drug conjugates, etc.) designed to work in specific sites inside cells is complicated as macromolecules typically have access to fewer biological compartments than small molecules. To better understand the fate of macromolecules in cells and begin to alter that fate, we investigated the internalization and subcellular fate of N-(2-hydroxypropyl)methacrylamide (HPMA) copolymers and HPMA copolymer-drug conjugates in Hep G2 and A2780 cells. The subcellular fate of fluorescently labeled polymers was monitored by confocal microscopy and subcellular fractionation. Initially, the HPMA copolymers and HPMA copolymer-drug conjugates were internalized by endocytosis and remained in endosomes/lysosomes. At longer incubation times (>8 h), small amounts of the HPMA copolymers were observed to enter the cytoplasm and accumulate in the nucleus of the cells. Nuclear accumulation was confirmed after cytoplasmic microinjection. Oligonucleotides conjugated via lysosomally degradable spacers entered into the cytoplasm and nucleus of the cells faster than the polymers. The effect of the subcellular location was correlated to the toxicity of the photosensitizer, mesochlorin e(6) (Mce(6))-HPMA copolymer conjugates. The plasma membrane and late endosomes were more sensitive to damage by Mce(6). Targeting the polymer conjugates to the nucleus with the nuclear localization sequence (NLS) as well as conjugating the Mce(6) via a degradable spacer increased cell adhesion and uptake, promoted their entry into the cytoplasm and nucleus of the cells, and increased their toxicity. To further promote entry of the polymers into the cytoplasm and nucleus of the cells, the protein transduction domain, Tat peptide, was conjugated to the HPMA copolymers. This resulted in high binding to the cell membrane, but also facilitated rapid (<5 min) entry of the macromolecules into the cytoplasm and nucleus of cells. These results will prove valuable in the future design of macromolecular therapeutics.

Animals↗

Release of viruses and viral DNA from nucleus to cytoplasm of HeLa cells at late stages of productive adenovirus infection as revealed by electron microscope in situ hybridization.

Considerable progress has been made over the past 10 years towards a full understanding of the functional significance of the structural changes resulting from the production of adenoviruses in permissive cells. Similarly, the host-virus interactions which are involved in viral replication and gene expression as well as in RNA nuclear export have been investigated. Post-embedding nonisotopic in situ hybridization has been proven to be a powerful tool for the study of nucleic acids in infected cells provided that controlled elimination of artifacts by appropriate treatments was undertaken. Adenovirus infected cells present two biological characteristics which could lead to false positive or negative results. First, they contain large amounts of single-stranded portions of viral DNA which are revealed with viral RNA molecules. Second, DNA-binding proteins are present which hide some nucleic acid sequences. By using a DNA probe and appropriate variations in the experimental protocol, it is possible to reveal specifically different kinds of targets, simultaneously single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), or only ssDNA, or only dsDNA, or only RNA. By using two probes labeled with different haptens, biotine and digoxigenin, it is possible to detect concomitantly two nucleic acid targets and, therefore, to study their relationships. In order to gain insight into the changes in the nucleus before cell lysis and to improve our knowledge on the series of steps leading to the release of adenoviruses from the nucleus, examination of cells at 41 h post-infection and identification of structures containing adenoviral nucleic acids were undertaken. In addition to the ultrastructural changes and precise distribution of cellular DNA and viral nucleic acid molecules already described in cells up to 24 h post-infection (for a review, see Puvion E, Puvion-Dutilleul F (1996) Exp Cell Res 229, 217-225), new results were obtained. Routine observation revealed the presence of: i) viruses in the cytoplasm, some being located next to nuclear pores; ii) abnormally large portions of the nuclear envelope devoid of underlying condensed chromatin; iii) proliferation of either the inner nuclear membrane only or both membranes of the nuclear envelope; and iv) electron-opaque grains in the nuclear compartment involved in viral genome transcription, and also in the clusters of interchromatin granules known to contain mature viral messenger RNA (Bridge E et al (1996) J Cell Biol 135, 303-314). In situ hybridization revealed the presence of: i) dsDNA in the cytoplasmic viruses indicating that they were mature viruses; ii) free viral dsDNA and ssDNA molecules in the cytoplasm whereas host DNA remained confined at the nuclear border; and iii) viral RNA in the newly-described electron-opaque grains we call, therefore, viral-RNA containing grains. Immunodetection of bromodeoxyuridine (BrdU) incorporated into DNA in pulse and pulse-chase experiments allowed us to ascertain that cells at 41 h post-infection were truly living cells and that at least part of the newly-synthesized viral DNA migrated from the nucleus to the cytoplasm. Taken together, the data suggest that modifications of the nuclear matrix, cytoskeleton, and nucleo-cytoplasmic interactions might occur near the termination of adenovirus infection inducing the progressive release of viruses, vial dsDNA and ssDNA molecules in the cytoplasm. In addition, the observation of a new structural support for the intranuclear viral RNA in the clusters of interchromatin granules emphasizes the role of these cellular structures in the intranuclear trafficking of messenger RNA leading to the regulation of its nuclear export.

Adenoviruses, Human↗