Document Detail


Activation of elastin transcription by transforming growth factor-beta in human lung fibroblasts.
MedLine Citation:
PMID:  17209135     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Elastin synthesis is essential for lung development and postnatal maturation as well as for repair following injury. Using human embryonic lung fibroblasts that express undetectable levels of elastin as assessed by Northern analyses, we found that treatment with exogenous transforming growth factor-beta (TGF-beta) induced rapid and transient increases in levels of elastin heterogeneous nuclear RNA (hnRNA) followed by increases of elastin mRNA and protein expression. In fibroblasts derived from transgenic mice, TGF-beta induced increases in the expression of a human elastin gene promoter fragment driving a chloramphenicol acetyl transferase reporter gene. The induction of elastin hnRNA and mRNA expression by TGF-beta was abolished by pretreatments with TGF-beta receptor I inhibitor, global transcription inhibitor actinomycin D, and partially blocked by addition of protein synthesis inhibitor cycloheximide, but was not affected by the p44/42 MAPK inhibitor U0126. Pretreatment with the p38 MAPK inhibitor SB-203580 also partially attenuated the levels of TGF-beta-induced elastin mRNA but not its hnRNA. Western analysis indicated that TGF-beta stimulated Akt phosphorylation. Inhibition of phosphatidylinositol 3-kinase and Akt phosphorylation by LY-294002 abolished TGF-beta-induced increases in elastin hnRNA and mRNA expression. Treatment of lung fibroblasts with interleukin-1beta or the histone deacetylase inhibitor trichostatin A inhibited TGF-beta-induced elastin mRNA and hnRNA expression by a mechanism that involved inhibition of Akt phosphorylation. Downregulation of Akt2 but not Akt1 expression employing small interfering RNA duplexes blocked TGF-beta-induced increases of elastin hnRNA and mRNA levels. Together, our results demonstrated that TGF-beta activates elastin transcription that is dependent on phosphatidylinositol 3-kinase/Akt activity.
Authors:
Ping-Ping Kuang; Xiao-Hui Zhang; Celeste B Rich; Judith A Foster; Mangalalaxmy Subramanian; Ronald H Goldstein
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2007-01-05
Journal Detail:
Title:  American journal of physiology. Lung cellular and molecular physiology     Volume:  292     ISSN:  1040-0605     ISO Abbreviation:  Am. J. Physiol. Lung Cell Mol. Physiol.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-12     Completed Date:  2007-05-24     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100901229     Medline TA:  Am J Physiol Lung Cell Mol Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  L944-52     Citation Subset:  IM    
Affiliation:
Pulmonary Center, Boston University School of Medicine, 80 E. Concord St., Boston, MA 02118, USA. ppkuang@bu.edu
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MeSH Terms
Descriptor/Qualifier:
Cells, Cultured
Chromones / pharmacology
Down-Regulation
Elastin / biosynthesis*
Fibroblasts / metabolism
Histone Deacetylase Inhibitors
Humans
Hydroxamic Acids / pharmacology
Lung / metabolism*
Morpholines / pharmacology
Phosphorylation
Proto-Oncogene Proteins c-akt / biosynthesis,  metabolism
RNA, Messenger / metabolism
Transcription, Genetic / drug effects*
Transforming Growth Factor beta / physiology*
Grant Support
ID/Acronym/Agency:
P01-HL-46902/HL/NHLBI NIH HHS; R01-HL-66547/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Chromones; 0/Histone Deacetylase Inhibitors; 0/Hydroxamic Acids; 0/Morpholines; 0/RNA, Messenger; 0/Transforming Growth Factor beta; 154447-36-6/2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; 58880-19-6/trichostatin A; 9007-58-3/Elastin; EC 2.7.1.37/AKT1 protein, human; EC 2.7.1.37/AKT2 protein, human; EC 2.7.11.1/Proto-Oncogene Proteins c-akt

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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