Insulin inhibits surfactant protein A and B gene expression in the H441 cell line

1998 ◽  
Vol 1442 (1) ◽  
pp. 60-70 ◽  
Author(s):  
Olga L. Miakotina ◽  
Steven A. Dekowski ◽  
Jeanne M. Snyder
Keyword(s):  
Gene Expression ◽  
Cell Line ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A

Gene Expression of Surfactant Protein A mRNA of the Lung in Endotoxin and Thiourea Treated Rats

2003 ◽  
Vol 55 (3) ◽  
pp. 257
Author(s):  
Jae Young Lee ◽  
Mi Ok Kim ◽  
Jang Won Sohn ◽  
Ho Joo Yoon ◽  
Dong Ho Shin ◽  
...  
Keyword(s):  
Gene Expression ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A

Antisense inhibition of surfactant protein A decreases tubular myelin formation in human fetal lung in vitro

2002 ◽  
Vol 282 (3) ◽  
pp. L386-L393 ◽  
Author(s):  
Jonathan M. Klein ◽  
Troy A. McCarthy ◽  
John M. Dagle ◽  
Jeanne M. Snyder
Keyword(s):  
Gene Expression ◽  
Protein A ◽  
Fetal Lung ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Mrna Levels ◽  
Phosphorothioate Oligonucleotide ◽  
Myelin Formation ◽  
Surfactant Phospholipids ◽  
Human Fetal Lung

Surfactant protein A (SP-A) is the most abundant of the surfactant-associated proteins. SP-A is involved in the formation of tubular myelin, the modulation of the surface tension-reducing properties of surfactant phospholipids, the metabolism of surfactant phospholipids, and local pulmonary host defense. We hypothesized that elimination of SP-A would alter the regulation of SP-B gene expression and the formation of tubular myelin. Midtrimester human fetal lung explants were cultured for 3–5 days in the presence or absence of an antisense 18-mer phosphorothioate oligonucleotide (ON) complementary to SP-A mRNA. After 3 days in culture, SP-A mRNA was undetectable in antisense ON-treated explants. After 5 days in culture, levels of SP-A protein were also decreased by antisense treatment. SP-B mRNA levels were not affected by the antisense SP-A ON treatment. However, there was decreased tubular myelin formation in the antisense SP-A ON-treated tissue. We conclude that selective elimination of SP-A mRNA and protein results in a decrease in tubular myelin formation in human fetal lung without affecting SP-B mRNA. We speculate that SP-A is critical to the formation of tubular myelin during human lung development and that the regulation of SP-B gene expression is independent of SP-A gene expression.

Transcriptional activation and protein binding by two regions of the rat surfactant protein A promoter

1999 ◽  
Vol 277 (1) ◽  
pp. L134-L141
Author(s):  
Elizabeth Rosenberg ◽  
Feng Li ◽  
Candyce I. Smith ◽  
Samuel R. Reisher ◽  
Sheldon I. Feinstein
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Promoter Activity ◽  
Protein A ◽  
Surfactant Protein ◽  
Clara Cell ◽  
Surfactant Protein A ◽  
Type Ii ◽  
Recognition Element ◽  
Type Ii Cell

Surfactant protein A (SP-A) is expressed in lung alveolar type II cells and bronchiolar Clara cells. We have identified two active regions in the promoter of the rat SP-A gene by deletion analysis of a plasmid containing 163 bp before the start of transcription (−163 bp), linked to a reporter gene. Constructs were transfected into lung cell lines derived from each of the cell types that produces SP-A. We found a novel region of promoter activity at ∼90 bp before the transcriptional start (SP-A−90). Mutation of four nucleotides in SP-A−90 that are highly conserved among species (−92 to −89 bp) decreased expression of the SP-A construct by ∼50% in both cell lines. Electrophoretic mobility shift analysis showed specific binding to SP-A−90 by nuclear proteins from the cell lines, as well as from rat lung and liver. The electrophoretic mobility of the bands shifted by lung nuclear proteins changed late in fetal development. Although in the Clara cell line no reduction of promoter activity was seen on deletion of the region upstream of SP-A−90, in the type II cell line, deletion of residues −163 to −133 did reduce activity by ∼50%. This region contains a recognition element for thyroid transcription factor-1 (TTF-1). Endogenous TTF-1 binding activity was substantially higher in the type II cell line than in the Clara cell line, but cotransfection of a TTF-1 expression plasmid enhanced expression of the SP-A construct better in the Clara cell line than in the type II cell line. These results suggest that the recognition element for TTF-1 has varying activity in the lung cell lines of different origin due to the availability of TTF-1.

scholarly journals Jaagsiekte Sheep Retrovirus Proviral Clone JSRVJS7, Derived from the JS7 Lung Tumor Cell Line, Induces Ovine Pulmonary Carcinoma and Is Integrated into the Surfactant Protein A Gene

2001 ◽  
Vol 75 (9) ◽  
pp. 4239-4246 ◽  
Author(s):  
James C. DeMartini ◽  
Jeanette V. Bishop ◽  
Thomas E. Allen ◽  
F. A. Jassim ◽  
J. Michael Sharp ◽  
...  
Keyword(s):  
Tumor Cell ◽  
Cell Line ◽  
Lung Tumor ◽  
Protein A ◽  
Tumor Cell Line ◽  
Surfactant Protein ◽  
Surfactant Protein A ◽  
Jaagsiekte Sheep Retrovirus ◽  
Pulmonary Carcinoma ◽  
Lung Tumor Cell

ABSTRACT Ovine pulmonary carcinoma (OPC) is a contagious neoplasm of alveolar epithelial type II (ATII) or Clara cells caused by a type D/B chimeric retrovirus, jaagsiekte sheep retrovirus (JSRV). Here we report the isolation, sequencing, pathogenicity, and integration site of a JSRV provirus isolated from a sheep lung tumor cell line (JS7). The sequence of the virus was 93 to 99% identical to other JSRV isolates and contained all of the expected open reading frames. To produce virions and test its infectivity, the JS7 provirus (JSRVJS7) was cloned into a plasmid containing a cytomegalovirus promoter and transfected into 293T cells. After intratracheal inoculation with virions from concentrated supernatant fluid, JSRV-associated OPC lesions were found in one of four lambs, confirming that JSRVJS7 is pathogenic. In JS7-cell DNA, the viral genome was inserted in the protein-coding region for the surfactant protein A (SP-A) gene, which is highly expressed in ATII cells, in an orientation opposite to the direction of transcription of the SP-A gene. No significant transcription was detected from either the viral or the SP-A gene promoter in the JS7 cell line at passage level 170. The oncogenic significance of the JSRV proviral insertion involving the SP-A locus in the JS7 tumor cell line is unknown.

A role for C/EBPδ in human surfactant protein A (SP-A) gene expression

2002 ◽  
Vol 1575 (1-3) ◽  
pp. 91-98 ◽  
Author(s):  
Anjaneyulu Matlapudi ◽  
Mengshu Wang ◽  
Elizabeth Rosenberg ◽  
Jacqueline R. Ewing ◽  
Sheldon I. Feinstein
Keyword(s):  
Gene Expression ◽  
Protein A ◽  
Surfactant Protein ◽  
Surfactant Protein A
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