Induction of interleukin-1/and interleukin-8 mRNAs and proteins by TGFβ1 in rat lung alveolar epithelial cells

Tenascin (TN) is a hexameric extracellular matrix glycoprotein that may play an important role during lung development. TN protein is temporally and spatially restricted during lung organogenesis. The temporo-spatial and cellular expression of TN mRNA in lung remains unclear. Localization of message expression of TN in rat lung tissue was first investigated by using in situ hybridization performed with an antisense RNA probe. TN mRNA was present primarily within the mesenchyme of day 16 gestational age fetal rat lung tissue, whereas immunoreactive TN protein was found along the basement membrane. In postnatal day 3 rat lung tissue, TN mRNA was detected along alveolar septal walls and was concentrated at secondary septal tips. Expression of TN message was consistent with localization of immunoreactive TN protein. Accumulation of TN mRNA in alveolar septal tips suggests that mesenchyme may be the major source of TN mRNA. To investigate the cellular source of TN in rat lung, we studied the expression of TN in cultured rat lung fibroblasts, endothelial cells, and alveolar epithelial cells. Two TN isoforms having molecular mass of 230 and 180 kDa were in conditioned medium and in cellular extracts of lung fibroblasts and endothelial cells. TN was secreted and deposited in the extracellular matrix closely associated with the surface of lung fibroblasts and endothelial cells. Lung alveolar epithelial cells showed undetectable or barely detectable amounts of TN. These studies demonstrated that TN isoforms are expressed not only by lung fibroblasts but also by lung endothelial cells. The unique spatial localization of TN mRNA during lung development and expression of TN by different lung cell types suggested TN may be involved in matrix organization and cell-cell interactions during lung development.

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Cadmium exposure down-regulates 8-oxoguanine DNA glycosylase expression in rat lung and alveolar epithelial cells

Toxicology ◽

10.1016/s0300-483x(02)00579-6 ◽

2003 ◽

Vol 184 (2-3) ◽

pp. 189-202 ◽

Cited By ~ 34

Author(s):

Ryan J Potts ◽

Richard D Watkin ◽

Beth A Hart

Keyword(s):

Epithelial Cells ◽

Cadmium Exposure ◽

Alveolar Epithelial Cells ◽

Dna Glycosylase ◽

Rat Lung ◽

Alveolar Epithelial

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Lectin binding patterns to terminal sugars of rat lung alveolar epithelial cells.

Journal of Histochemistry & Cytochemistry ◽

10.1177/38.2.1688898 ◽

1990 ◽

Vol 38 (2) ◽

pp. 233-244 ◽

Cited By ~ 27

Author(s):

D J Taatjes ◽

L A Barcomb ◽

K O Leslie ◽

R B Low

Keyword(s):

Epithelial Cells ◽

Lectin Binding ◽

Alveolar Epithelial Cells ◽

Gold Complex ◽

Type I ◽

Type Ii Cells ◽

Type Ii ◽

Rat Lung ◽

Alveolar Epithelial ◽

I Cells

We used post-embedding cytochemical techniques to investigate the lectin binding profiles of rat lung alveolar epithelial cells. Sections from rat lung embedded in the hydrophilic resin Lowicryl K4M were incubated either directly with a lectin-gold complex or with an unlabeled lectin followed by a specific glycoprotein-gold complex. The binding patterns of the five lectins used could be divided into three categories according to their reactivity with alveolar epithelial cells: (a) the Limax flavus lectin and Ricinus communis I lectin bound to both type I and type II cell plasma membranes; (b) the Helix pomatia lectin and Sambucus nigra L. lectin bound to type II but not type I cells; and (c) the Erythrina cristagalli lectin reacted with type I cells but was unreactive with type II cells. The specificity of staining was assessed by control experiments, including pre-absorption of the lectins with various oligosaccharides and enzymatic pre-treatment of sections with highly purified glycosidases to remove specific sugar residues. The results demonstrate that these lectins can be used to distinguish between type I and type II cells and would therefore be useful probes for investigating cell dynamics during lung development and remodeling.

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Perfluorocarbon Suppresses Lipopolysaccharide- and α-Toxin-Induced Interleukin-8 Release from Alveolar Epithelial Cells

Neonatology ◽

10.1159/000097130 ◽

2006 ◽

Vol 91 (2) ◽

pp. 127-133 ◽

Cited By ~ 6

Author(s):

Setsuko Nakata ◽

Kozo Yasui ◽

Tomohiko Nakamura ◽

Noriko Kubota ◽

Atsushi Baba

Keyword(s):

Epithelial Cells ◽

Alveolar Epithelial Cells ◽

Interleukin 8 ◽

Alveolar Epithelial

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Nacystelyn inhibits oxidant-mediated interleukin-8 expression and NF-κB nuclear binding in alveolar epithelial cells

Free Radical Biology and Medicine ◽

10.1016/s0891-5849(01)00820-6 ◽

2002 ◽

Vol 32 (6) ◽

pp. 492-502 ◽

Cited By ~ 51

Author(s):

Frank Antonicelli ◽

Maryline Parmentier ◽

Ellen M Drost ◽

Nik Hirani ◽

Irfan Rahman ◽

...

Keyword(s):

Epithelial Cells ◽

Alveolar Epithelial Cells ◽

Interleukin 8 ◽

Alveolar Epithelial ◽

Nuclear Binding

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Identification of Na(+)-K(+)-ATPase beta-subunit in alveolar epithelial cells

AJP Lung Cellular and Molecular Physiology ◽

10.1152/ajplung.1997.272.1.l85 ◽

1997 ◽

Vol 272 (1) ◽

pp. L85-L94 ◽

Cited By ~ 3

Author(s):

X. L. Zhang ◽

S. I. Danto ◽

Z. Borok ◽

J. T. Eber ◽

P. Martin-Vasallo ◽

...

Keyword(s):

Epithelial Cells ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Alveolar Epithelial Cells ◽

Beta Subunit ◽

Rat Lung ◽

Western Blots ◽

Sodium Pumps ◽

Subunit Protein ◽

Alveolar Epithelial

The Na(+)-K(+)-ATPase is a heterodimeric plasma membrane protein that consists of a catalytic alpha-subunit and a smaller glycosylated beta-subunit that has not been fully characterized in alveolar epithelial cells (AEC) to date. In this study, we identified the Na(+)-K(+)-ATPase beta-subunit protein in rat AEC and lung membranes using immunochemical techniques. Rat AEC grown in primary culture and rat lung, brain, and kidney membranes were solubilized in either 2% sodium dodecyl sulfate (SDS) sample buffer for SDS-polyacrylamide gel electrophoresis or in 1% Nonidet P-40 lysis buffer for immunoprecipitation studies. Na(+)-K(+)-ATPase beta-subunit was not detected in either AEC or lung membranes on Western blots when probed with a panel of antibodies (Ab) against beta-subunit isoforms, whereas brain and kidney beta-subunit were recognized as broad approximately 50-kDa bands. AEC, lung, and kidney membranes were immunoprecipitated with anti-beta Ab IEC 1/48, a monoclonal Ab that recognizes beta-subunit protein only in its undenatured state. The beta-subunit was detected in the immunoprecipitate (IP) from kidney membranes by several different anti-beta-subunit Ab. The beta-subunit was faintly detectable from AEC and lung IP as a broad approximately 50-kDa band when blotted with the polyclonal anti-beta 1-subunit Ab SpET but could not be detected by blotting with other anti-beta Ab. Treatment of the IP from kidney, lung, and AEC with N-glycosidase F for 2 h at 37 degrees C resulted in immunodetection of identical approximately 35 kDa bands when probed with all anti-beta 1 Ab on Western blots. From these results, we conclude that rat lung and AEC possess immunoreactive beta-subunit protein that is only readily detectable after deglycosylation. Because anti-beta Ab fail to detect the Na(+)-K(+)-ATPase beta-subunit in rat lung or AEC by standard Western blotting techniques under the conditions of these experiments, our results suggest that lung beta-subunit may be glycosylated differently from kidney and other tissues. These differences appear to be due to organ- or cell-specific posttranslational processing of the beta 1-subunit and may result in altered regulation of sodium pumps in lung compared with other epithelia.

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