Colocalization of cytokeratin 18 and villin in type III alveolar cells (brush cells) of the rat lung

Kasper, Michael; Höfer, Dirk; Woodcock‐Mitchell, Janet; Migheli, Antonio; Attanasio, A.; Rudolf, Thomas; Müller, Martin; Drenckhahn, Detlev

doi:10.1007/bf00315832

Cited by 49 publications

(39 citation statements)

References 20 publications

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“…This result is similar to the result of a previous 2-DE study that reported that phosphorylated Villin 2 protein was expressed during myoblast growth of C2C12 cells and was not expressed during early myogenesis (12). Generally, Villin 2 protein is called ezrin, and it is one the proteins that belong to ezrin-radixin-moesin (ERM) cytoskeleton-associated protein family (13)(14)(15). Villin 2 provides a crucial morphological link between the cell plasma membrane and the http://bmbreports.org BMB reports actin-based cytoskeleton (16,17), maintaining cell shape and polarity, and participating in cell migration, signaling, growth regulation, and differentiation (18,19).…”

Section: Functional Analysis Of Villin 2 Proteinsupporting

confidence: 90%

Functional study of Villin 2 protein expressed in longissimus dorsi muscle of Korean native cattle in different growth stages

Jin

Han²,

Xu³

et al. 2012

BMB Reports

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The aim of this study was to investigate protein profiles related to the induction of adipogenesis within the bovine longissimus dorsi muscle (BLDM) by proteomic analysis. We analyzed BLDM proteins at different growth stages to clarify the physiological mechanisms of marbled muscle development in 20 head of Korean native cattle (11 month: 10 head, 17 month: 10 head). BLDM proteins were analyzed by two-dimensional electrophoresis and image analysis. Villin 2 was specifically identified by mass spectrometry and a protein search engine. Villin 2 protein expression in BLDM decreased during the fat development stage in test steers. In a Western blot cell culture study of spontaneously immortal bovine muscle fibroblasts, the abundance of Villin 2 was shown to be down-regulated during differentiation into muscle. In 3T3-L1 mouse embryonic fibroblasts, Villin 2 was decreased during differentiation into adipocytes. The results suggest that Villin 2 may be related to the induction of transdifferentiation and adipogenesis in bovine longissimus dorsi muscle. [BMB reports 2012; 45(2): 102-107]

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Section: Functional Analysis Of Villin 2 Proteinsupporting

confidence: 90%

Functional study of Villin 2 protein expressed in longissimus dorsi muscle of Korean native cattle in different growth stages

Jin

Han²,

Xu³

et al. 2012

BMB Reports

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“…1 F and G). This intermediate filament protein is present in considerably higher concentrations in brush cells than in any other epithelial cell type of the lung and the gastrointestinal epithelium (10). At low antibody concentrations, brush cells (Fig.…”

Section: Resultsmentioning

confidence: 92%

“…§1734 solely to indicate this fact. against a-gustducin and the actin filament-bundling protein villin, a marker molecule for brush cells (10,12), identified these cells as brush cells (Fig. 1 D and E).…”

Section: Resultsmentioning

confidence: 93%

Taste receptor-like cells in the rat gut identified by expression of alpha-gustducin.

Höfer

Püschel²,

Drenckhahn³

1996

Proc. Natl. Acad. Sci. U.S.A.

361

292

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The a-subunit of the trimeric G-protein complex specific for taste receptor cells of the tongue, a-gustducin, is described here to be also expressed in the stomach and intestine. The a-gustducin-containing cells were identified as brush cells that are scattered throughout the surface epithelium of the gut and share structural features of taste receptor cells of the tongue. These findings provide clues to the long-sought molecular and cellular basis for chemoreception in the gut.It is generally believed that the epithelium lining the inner surface of the gut can sense chemical components of the lumenal contents. This chemosensory information appears to be important for the regulation of various aspects of gastrointestinal secretion, resorption, and motility (1, 2). Classical examples of intestinal chemosensitivity are the dependence of gastric emptying on the chemical nature of the nutrients present in the small intestine and the involvement of chemical preabsorption information in short-term regulation of food intake (2). The cellular and molecular basis for chemoreception in the gut is hitherto unknown. In this study we addressed the question ofwhether the epithelium of the gut might express a-gustducin, the GTP-binding a-subunit of a trimeric Gprotein complex that is specific for taste receptor cells of the tongue (3). Here we show that a-gustducin is also expressed in the epithelium of the gut where it is associated with a specialized cell type long known under the names brush cell, tufted cell, or caveolated cell (4-6). The function of this cell type, which is present in humans, rats, and probably all other mammals, had been enigmatic until now. MATERIALS AND METHODSAntibodies and Immunostaining. A polyclonal antibody specific for a-gustducin was raised in a rabbit immunized with a synthetic peptide comprising amino acid residues 92-113 of the rat a-gustducin sequence (3). This sequence stretch is unique for a-gustducin and is not present in the sequences of any other known G-protein. Antibodies were affinity-purified to the peptide adsorbed to nitrocellulose (7,8). Polyclonal rabbit antibodies specific for chromogranin A and serotonin (9) and mouse monoclonal antibodies to villin (Dianova, Hamburg, Germany) and cytokeratin 18 (Progen, Heidelberg) were also used in this study. Indirect immunofluorescence was applied to 1-,um thick tissue sections of quick-frozen and Epon-embedded tissues as described (8). For doubleimmunofluorescence sections were incubated with a mixture of the rabbit antibody against a-gustducin and mouse monoclonal antibodies either specific for villin or cytokeratin 18. Primary antibodies were diluted with PBS: anti-gustducin (1:200), anti-chromogranin (1:4,000), anti-serotonin (1:10,000), anti-villin (0.1 /Lg/ml-1), anti-cytokeratin 18 (0.5 ,ug/ml-1). As secondary antibodies fluorescein isothiocyanate-labeled goat anti-mouse IgG and tetramethylrhodamine isothiocyanate-labeled goat anti-rabbit IgG (Dianova) were used at concentrations of 0.1 Ag/ml-1.Immunoblotting. Various tissue...

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“…CK 18 belongs to the group of acidic keratins type I IF (Herrmann and Aebi 2000) that has been shown to be expressed in BCs of epithelia covering different organs of the GI tract (Kasper et al 1994). Because of the strong immunoreaction that BCs display after application of antibodies directed against CK peptide 18, these have been proposed and used as specific LM markers to identify BCs in various epithelia (Höfer and Drenckhahn 1996;Gebert et al 2000), although there are differences in species crossreactivity between antibody clones (Gebert et al 2000;and this study).…”

Section: Immunodetection Of Peripherinmentioning

confidence: 99%

“…Even in earlier detailed descriptions after thin-section transmission electron microscopy (Luciano et al 1968;Luciano and Reale 1969), two main characteristics of BCs were evident: the prominent microvillous brush border (from which they received their name; Rhodin and Dalhamn 1956) and the architecture of the cytoskeleton. The three building elements F-actin, microtubules, and intermediate filaments are uncommonly abundant and display an extremely ordered spatial arrangement and distribution in the cytoplasm (Luciano and Reale 1997 (Kasper et al 1994). Antibodies against CK 18 were then proposed and used as specific markers to identify BCs by light microscopy (Höfer and Drenckhahn 1996;Gebert et al 2000).…”

mentioning

confidence: 99%

Brush Cells of Rodent Gallbladder and Stomach Epithelia Express Neurofilaments

Luciano

Groos

Reale

2003

J Histochem Cytochem.

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S U M M A R Y It has been suggested that brush cells (BCs), a distinct type of cell occurring in various epithelia of the respiratory and gastrointestinal tracts, may function as receptor cells. The major characteristics of BCs are a prominent brush border and an unusually highly ordered arrangement of cytoskeletal elements (F-actin, microtubules, and intermediate filaments). In this study we aimed to characterize the nature of the intermediate filaments in BCs by light and electron microscopic immunostaining. Gallbladder and stomach specimens from mice and rats, respectively, were fixed in various solutions, embedded either in paraffin or epoxy resin, and processed for immunodetection. Commercially available, well-characterized antibodies against neurofilaments, peripherin, and cytokeratin peptide 18 were used. The polyclonal antiserum cocktail to neurofilaments was applied as a supplement in a double-labeling procedure with anti-actin and anti-cytokeratin 18 antibodies. The results demonstrate that the BCs of both organs express two types of intermediate filaments, i.e., neurofilaments and cytokeratin 18 filaments, and that these have a compartmentalized distribution in the cytoplasm. BCs do not express peripherin

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Colocalization of cytokeratin 18 and villin in type III alveolar cells (brush cells) of the rat lung

Cited by 49 publications

References 20 publications

Functional study of Villin 2 protein expressed in longissimus dorsi muscle of Korean native cattle in different growth stages

Functional study of Villin 2 protein expressed in longissimus dorsi muscle of Korean native cattle in different growth stages

Taste receptor-like cells in the rat gut identified by expression of alpha-gustducin.

Brush Cells of Rodent Gallbladder and Stomach Epithelia Express Neurofilaments

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