Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The stria vascularis in the cochlea and the dark-cell areas in the vestibular endorgans are structures involved in the production of endolymphatic fluid. This study investigated the dark-cell areas in the vestibular endorgans of the dog by classical staining and by immunohistochemistry (anti-Na,K-ATPase beta2 isoform, anti-cytokeratins (against cytokeratins 5 and 8), anti-vimentin and anti-S100A6) from birth to 110 postnatal days. Using classical staining, it was not possible to discriminate dark cells from other epithelial cells lining the vestibular endolymphatic spaces. From birth, the Na,K-ATPase beta2 isoform was expressed in the lateral and basal cell membranes of a subset of cells located in the utricular wall, at the base of the cristae ampullaris and was identified as dark cells. From birth, anti-cytokeratins labelled all the cells forming the epithelial lining, including the dark cells, while anti-vimentin labelled the underlying mesenchymal cells. From postnatal day 10, anti-S100A6 labelled subepithelial cells exclusively located underneath the dark-cell areas and were identified as vestibular melanocyte-like cells. From birth, Fontana staining evidenced fine melanin granules in the subepithelial layer. The amount of melanin granules increased during the first month. Melanin distribution was closely associated with the region where S100A6-positive cells were located. The cell-specific antigen expression in the dog dark-cell areas was clearly comparable to that of the dog stria vascularis previously described. The present investigation also suggested an earlier histological and immunohistological maturity in the dark-cell areas than in the stria vascularis of dogs. This preliminary morphological description of the normal dark-cell areas in dogs by means of immunomarkers may be instrumental in studying pathological processes involving the fluid-secreting structures in vestibular endorgans.
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PMID:Dark-cell areas in the dog vestibular endorgans: an immunohistochemical study. 1537 66

The oesophageal tonsil of the chicken is a novel member of the mucosal-associated lymphoid tissue (MALT), which is located around the entrance of the proventriculus. It consists of 6 to 8 single units, which are surrounded by a thin fibrous capsule. Each one is organised around the bottom of the longitudinal folds of the oesophagus, and serves as a 'tonsillar crypt'. Stratified squamous epithelium is infiltrated by lymphoid cells, i.e. T cells, plasma cells, macrophages, and dendritic cells, but not B cells, to form lymphoepithelium (LE). In the LE vimentin-, MHC II- and ATPase-positive cells possibly represent Langerhans' cells, but the appearance of 74.3 positive cells in the LE is unusual, because the 74.3 monoclonal antibody (mAb) recognises chicken follicular dendritic cells in the germinal centre and medulla of the bursal follicles. The subepithelial lymphoid tissue is organised into T- and B-dependent regions, which are the interfollicular areas and the germinal centres, respectively. Existence of high-endothelial venules in the interfollicular region suggests an extensive cellular connection between the oesophageal tonsil and the other lymphoid organs. In the resting oesophagus the lumen is closed, but during swallowing a bolus the crypt opens and the lymphoepithelium can be exposed to undigested food, antigens, infectious agents and vaccines. The location of the oesophageal tonsil, cranial to the stomach, may provide this organ with a unique role as compared to the other parts of the MALT; namely, it may contribute to the replication of infectious bursal disease virus (IBDV) and/or the pathogenesis of infectious bursal disease.
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PMID:Oesophageal tonsil of the chicken. 1595 76

Lipid rafts and caveolae are biochemically similar, specialized domains of the PM (plasma membrane) that cluster specific proteins. However, they are morphologically distinct, implying different, possibly complementary functions. Two-dimensional gel electrophoresis preceding identification of proteins by MS was used to compare the relative abundance of proteins in DRMs (detergent-resistant membranes) isolated from HUVEC (human umbilical-vein endothelial cells), and caveolae immunopurified from DRM fractions. Various signalling and transport proteins were identified and additional cell-surface biotinylation revealed the majority to be exposed, demonstrating their presence at the PM. In resting endothelial cells, the scaffold of immunoisolated caveolae consists of only few resident proteins, related to structure [CAV1 (caveolin-1), vimentin] and transport (V-ATPase), as well as the GPI (glycosylphosphatidylinositol)-linked, surface-exposed protein CD59. Further quantitative characterization by immunoblotting and confocal microscopy of well-known [eNOS (endothelial nitric oxide synthase) and CAV1], less known [SNAP-23 (23 kDa synaptosome-associated protein) and BASP1 (brain acid soluble protein 1)] and novel [C8ORF2 (chromosome 8 open reading frame 2)] proteins showed different subcellular distributions with none of these proteins being exclusive to either caveolae or DRM. However, the DRM-associated fraction of the novel protein C8ORF2 (approximately 5% of total protein) associated with immunoseparated caveolae, in contrast with the raft protein SNAP-23. The segregation of caveolae from lipid rafts was visually confirmed in proliferating cells, where CAV1 was spatially separated from eNOS, SNAP-23 and BASP1. These results provide direct evidence for the previously suggested segregation of transport and signalling functions between specialized domains of the endothelial plasma membrane.
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PMID:Spatial segregation of transport and signalling functions between human endothelial caveolae and lipid raft proteomes. 1688 9

It has been known for 15 years that the chicken epidermis contains ATPase+ and major histocompatibility complex class II-positive (MHCII+) dendritic cells. These cells were designated as Langerhans cells but neither their detailed phenotype nor their function was further investigated. In the present paper we demonstrate a complete overlapping of ATPase, CD45 and vimentin staining in all dendritic cells of the chicken epidermis. The CD45+ ATPase+ vimentin+ dendritic cells could be divided into three subpopulations: an MHCII+ CD3- KUL01+ and 68.1+ (monocyte-macrophage subpopulation markers) subpopulation, an MHCII- CD3- KUL01- and 68.1- subpopulation and an MHCII- CD3+ KUL01- and 68.1- subpopulation. The first population could be designated as chicken Langerhans cells. The last population represents CD4- CD8- T-cell receptor-alphabeta- and -gammadelta- natural killer cells with cytoplasmic CD3 positivity. The epidermal dendritic cells have a low proliferation rate as assessed by bromodeoxyuridine incorporation. Both in vivo and in vitro experiments showed that dendritic cells could be mobilized from the epidermis. Hapten treatment of epidermis resulted in the decrease of the frequency of epidermal dendritic cells and hapten-loaded dendritic cells appeared in the dermis or in in vitro culture of isolated epidermis. Hapten-positive cells were also found in the so-called dermal lymphoid nodules. We suggest that these dermal nodules are responsible for some regional immunological functions similar to the mammalian lymph nodes.
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PMID:Characterization of chicken epidermal dendritic cells. 1688 40

The anuran Xenopus laevis is an experimental model for vertebrate development, immunology, and regenerative biology. Using histochemistry and immunohistochemistry (IHC) we examined embryonic, larval, and postmetamorphic Xenopus skin for the presence of dendritic cells (DCs), Langerhans cells (LCs), and dendritic epidermal T cells (DETCs), all components of cutaneous immunity that have been implicated in skin repair and regeneration. Cells expressing three markers for dendritic and Langerhans cells (formalin-resistant ATPase activity, major histocompatibility complex [MHC] class II antigens, and vimentin) and having morphology like that of these cells first appeared during late embryonic stages, becoming abundant by prometamorphosis. Cells positive for these markers were also numerous in the wound epithelia of regenerating hindlimbs at both early and late larval stages. Cells tentatively identified as DETCs were found, beginning at early larval stages, using IHC with antibodies against heterologous CD3epsilon chain and T-cell receptor delta. Further characterization and work with the putative DCs, LCs, and DETCs demonstrated here will allow not only greater understanding of the amphibian immune system, but also further elucidation of regenerative growth and scarring.
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PMID:Cells of cutaneous immunity in Xenopus: studies during larval development and limb regeneration. 1692 47

Voltage-gated chloride channels (ClCs) are important mediators of cellular ion homeostasis and volume regulation. In an earlier study, we used immunohistochemical, Western blot, and reverse transcriptase PCR (RT-PCR) approaches to identify ClC-K variants in types II, IV, and V fibrocytes of the rodent spiral ligament. We have now confirmed the expression of ClC-K2 in these cells by in situ hybridization. All three of these fibrocyte subtypes are thought to be involved in cochlear K(+) recycling; thus, it is important to understand the precise mechanisms regulating their membrane conductance and the role played by ClCs in this process. In this study, we report the characterization of a secondary cell line derived from explants from the region of the rat spiral ligament underlying and inferior to the spiral prominence. The cultured cells were immunopositive for vimentin, Na,K/ATPase, Na,K,Cl-cotransporter, carbonic anhydrase isozyme II, and creatine kinase isozyme BB, but not for cytokeratins or Ca/ATPase, an immunostaining profile indicative of the type IV subtype. Evaluation of the cultures by RT-PCR and Western blot analysis confirmed the presence of both ClC-2 and -K2. Whole-cell patch clamp recordings identified two biophysically distinct Cl(-) currents in the cultured cells. One, an inwardly rectifying Cl(-) current activated by hyperpolarization or decreasing extracellular pH corresponded with the properties of ClC-2. The other, a weak outwardly rectifying Cl(-) current regulated by extracellular pH, Cl(-), and Ca(2+) resembled the channel characteristics of ClC-K2 when expressed in Xenopus oocytes. These findings suggest that at least two functionally different chloride channels are involved in regulating membrane anion conductance in cultured type IV spiral ligament fibrocytes.
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PMID:Identification of ClC-2 and CIC-K2 chloride channels in cultured rat type IV spiral ligament fibrocytes. 1733 50

Apoptosis contributes to cell death after cerebral ischaemia. A quantitative proteomics approach has been employed to define alterations in protein levels in apoptosis induced with staurosporine (STS). Human neuroblastoma derived SH-SY5Y cells were treated with STS (500 nM for 6 h) to induce apoptosis. Quantitative 2-DE was used to determine the changing protein levels with MALDI-TOF MS identification of proteins. Of the 154 proteins analysed, 13 proteins were significantly altered as a result of the apoptotic stimulus; ten of the proteins showed an increase in level with STS and were identified as heat shock cognate 71 (Hsc71), two isoforms of heat shock protein 70 (Hsp70), glucose regulated protein 78 (GRP78), F-actin capping protein, stress-induced phosphoprotein 1, chromatin assembly factor 1 (CAF-1), protein disulphide isomerase A3 (PDI A3) precursor, transitional ER ATPase and actin interacting protein 1 (AIP 1). Three proteins which displayed significant decrease in levels with STS were identified as tubulin, vimentin and glucose regulated protein 94 (GRP94). The functional roles and subcellular locations of these proteins collectively indicate that STS-induced apoptosis provokes induces an unfolded protein response involving molecular chaperones, cochaperones and structural proteins indicative of ER stress.
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PMID:Apoptosis induced by staurosporine alters chaperone and endoplasmic reticulum proteins: Identification by quantitative proteomics. 1767 60

A specific mutation (DeltaE) in torsinA underlies most cases of the dominantly inherited movement disorder, early-onset torsion dystonia (DYT1). TorsinA, a member of the AAA+ ATPase superfamily, is located within the lumen of the nuclear envelope (NE) and endoplasmic reticulum (ER). We investigated an association between torsinA and nesprin-3, which spans the outer nuclear membrane (ONM) of the NE and links it to vimentin via plectin in fibroblasts. Mouse nesprin-3alpha co-immunoprecipitated with torsinA and this involved the C-terminal region of torsinA and the KASH domain of nesprin-3alpha. This association with human nesprin-3 appeared to be stronger for torsinADeltaE than for torsinA. TorsinA also associated with the KASH domains of nesprin-1 and -2 (SYNE1 and 2), which link to actin. In the absence of torsinA, in knockout mouse embryonic fibroblasts (MEFs), nesprin-3alpha was localized predominantly in the ER. Enrichment of yellow fluorescent protein (YFP)-nesprin-3 in the ER was also seen in the fibroblasts of DYT1 patients, with formation of YFP-positive globular structures enriched in torsinA, vimentin and actin. TorsinA-null MEFs had normal NE structure, but nuclear polarization and cell migration were delayed in a wound-healing assay, as compared with wild-type MEFs. These studies support a role for torsinA in dynamic interactions between the KASH domains of nesprins and their protein partners in the lumen of the NE, with torsinA influencing the localization of nesprins and associated cytoskeletal elements and affecting their role in nuclear and cell movement.
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PMID:TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton. 1882 15

The FXYD family, which contains seven members, are tissue specific regulators of the Na,K-ATPase. Increased expression of FXYD5, a cancer-cell-associated membrane glycoprotein, has been associated with increased cell motility and metastatic potential. To better understand how FXYD5 may modulate cell motility, we analyzed S163, a conserved residue in all FXYD family members located in the C-terminus. Ectopic expression of human FXYD5 S163 mutants in HEK 293 cells showed that negative charge at S163 (S163D) decreased membrane localization, assessed by immunofluorescence. Coimmunoprecipitation studies revealed decreased FXYD5/Na,K-ATPase interaction for S163D compared with wild-type or S163A mutants. Interestingly, FXYD5 overexpression induced expression of vimentin, a marker of epithelial-mesenchymal transition, in murine airway epithelial cells. Because Na,K-ATPase expression is decreased in some forms of cancer and is critical for establishing cell polarity and suppressing cell motility, we analyzed S163 mutants in an epithelial cell scratch-wound model as a measure of cell migration. Wild-type FXYD5 overexpression increased reepithelialization (p<0.0001), which was further increased in S163D mutants (p<0.005). However, S163A mutants inhibited epithelial cell migration compared with wild-type FXYD5 overexpression (p<0.0001). We conclude that negative charge at S163 regulates FXYD5/Na,K-ATPase interaction and that this interaction modulates cell migration across a wound in airway epithelial cells.
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PMID:S163 is critical for FXYD5 modulation of wound healing in airway epithelial cells. 1912 50

We recently demonstrated that the cardiotonic steroid marinobufagenin (MBG) induced fibrosis in rat hearts through direct stimulation of collagen I secretion by cardiac fibroblasts. This stimulation was also responsible for the cardiac fibrosis seen in experimental renal failure. In this study, the effect of MBG on the development of renal fibrosis in rats was investigated. Four weeks of MBG infusion triggered mild periglomerular and peritubular fibrosis in the cortex and the appearance of fibrotic scars in the corticomedullary junction of the kidney. MBG also significantly increased the protein levels and nuclear localization of the transcription factor Snail in the tubular epithelia. It is known that activation of Snail is associated with epithelial-to-mesenchymal transition (EMT) during renal fibrosis. To examine whether MBG alone can trigger EMT, we used the porcine proximal tubular cell line LLC-PK1. MBG (100 nM) caused LLC-PK1 cells grown to confluence to acquire a fibroblast-like shape and have an invasive motility. The expressions of the mesenchymal proteins collagen I, fibronectin, and vimentin were increased twofold. However, the total level of E-cadherin remained unchanged. These alterations in LLC-PK1 cells in the presence of MBG were accompanied by elevated expression and nuclear translocation of Snail. During the time course of EMT, MBG did not have measurable inhibitory effects on the ion pumping activity of its natural ligand, Na(+)-K(+)-ATPase. Our data suggest that the MBG may be an important factor in inducing EMT and, through this mechanism, elevated levels of MBG in chronic renal failure may play a role in the progressive fibrosis.
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PMID:The cardiotonic steroid hormone marinobufagenin induces renal fibrosis: implication of epithelial-to-mesenchymal transition. 1917 1


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