Retinoic acid-induced inhibition of type I collagen gene expression by human lung fibroblasts

1994 ◽  
Vol 1219 (2) ◽  
pp. 335-341 ◽  
Author(s):  
Meir Krupsky ◽  
Alan Fine ◽  
John L. Berk ◽  
Ronald H. Goldstein
Keyword(s):  
Gene Expression ◽  
Retinoic Acid ◽  
Type I Collagen ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Type I ◽  
Collagen Gene ◽  
Human Lung Fibroblasts ◽  
Collagen Gene Expression

Tissue specificity of type I collagen gene expression is determined at both transcriptional and post-transcriptional levels

1984 ◽  
Vol 4 (9) ◽  
pp. 1843-1852
Author(s):  
R J Focht ◽  
S L Adams
Keyword(s):  
Gene Expression ◽  
Rna Structure ◽  
Type I Collagen ◽  
Translational Efficiency ◽  
Type I ◽  
Collagen Gene ◽  
Differentiated Cells ◽  
Collagen Gene Expression

We analyzed the control of type I collagen synthesis in four kinds of differentiated cells from chicken embryos which synthesize very different amounts of the protein. Tendon, skin, and smooth muscle cells were found to have identical amounts of type I collagen RNAs; however, the RNAs had inherently different translatabilities, which were observed both in vivo and in vitro. Chondrocytes also had substantial amounts of type I collagen RNAs, even though they directed no detectable synthesis of the protein either in vivo or in vitro. Type I collagen RNAs in chondrocytes display altered electrophoretic mobilities, suggesting that in these cells the reduction in translational efficiency may be mediated in part by changes in the RNA structure. These data indicate that control of type I collagen gene expression is a complex process which is exerted at both transcriptional and post-transcriptional levels.

Phenylbutyrate decreases type I collagen production in human lung fibroblasts

2004 ◽  
Vol 91 (4) ◽  
pp. 740-748 ◽  
Author(s):  
David C. Rishikof ◽  
Dennis A. Ricupero ◽  
Hanqiao Liu ◽  
Ronald H. Goldstein
Keyword(s):  
Type I Collagen ◽  
Human Lung ◽  
Lung Fibroblasts ◽  
Type I ◽  
Collagen Production ◽  
Human Lung Fibroblasts

Effect of subcellular matrix on glycosaminoglycan synthesis by human lung fibroblasts

1987 ◽  
Vol 63 (6) ◽  
pp. 2181-2188 ◽  
Author(s):  
D. J. Cui ◽  
B. A. Dubaybo ◽  
R. A. Durr ◽  
L. A. Thet
Keyword(s):  
Type I Collagen ◽  
Human Lung ◽  
Basement Membranes ◽  
Lung Fibroblasts ◽  
Type I ◽  
Glycosaminoglycan Synthesis ◽  
Human Lung Fibroblasts ◽  
Cell Matrix ◽  
Matrix Layer ◽  
The Matrix

The influences modulating glycosaminoglycan production by lung cells are not well understood. We examined the effect of three different subcellular matrices, plastic, type I collagen, and reconstituted basement membrane-like material (RBM), on the synthesis of sulfated glycosaminoglycans by cultured IMR-90 human lung fibroblasts. Accumulation of 35SO4-labeled glycosaminoglycans into the cell-matrix layer or medium was measured. Cells on collagen synthesized significantly less total glycosaminoglycans than cells on plastic but had a higher fraction of labeled glycosaminoglycans present in the cell-matrix layer (35 vs. 18%) with the increases being highest for dermatan and chondroitin sulfates. Cells grown on the RBM synthesized significantly more glycosaminoglycans than cells on plastic or collagen and also had 260% more labeled glycosaminoglycans present in the cell-matrix layer than cells on plastic. We conclude that the matrix to which lung fibroblasts are exposed can influence the amount and type of glycosaminoglycans synthesized and the degree of incorporation into the matrix. This may be relevant to fibrotic lungs with increased type I collagen or to severely injured lungs in which intra-alveolar fibroblasts are in contact with denuded basement membranes.

Factors Involved in the Regulation of Type I Collagen Gene Expression: Implication in Fibrosis

2002 ◽  
Vol 227 (5) ◽  
pp. 301-314 ◽  
Author(s):  
Asish K. Ghosh
Keyword(s):  
Gene Expression ◽  
Collagen Synthesis ◽  
Molecular Mechanisms ◽  
Type I Collagen ◽  
Regulatory Elements ◽  
Transcriptional Level ◽  
Type I ◽  
Collagen Gene ◽  
Cis Acting ◽  
Collagen Gene Expression

Type I collagen, the major component of extracellular matrix in skin and other tissues, is a heterotrimer of two α1 and one α2 collagen polypeptides. The synthesis of both chains is highly regulated by different cytokines at the transcriptional level. Excessive synthesis and deposition of collagen in the dermal region causes thick and hard skin, a clinical manifestation of scleroderma. To better understand the causes of scleroderma or other tissue fibrosis, it is very Important to investigate the molecular mechanisms that cause upregulation of the Type I collagen synthesis in these tissues. Several cis-acting regulatory elements and trans-acting protein factors, which are involved in basal as well as cytokine-modulated Type I collagen gene expression, have been identified and characterized. Hypertranscription of Type I collagen in scleroderma skin fibroblasts may be due to abnormal activities of different positive or negative transcription factors In response to different abnormally induced signaling pathways. In this review, I discuss the present day understanding about the involvement of different factors in the regulation of basal as well as cytokine-modulated Type I collagen gene expression and its implication in scleroderma research.

scholarly journals A Novel Role of Annexin A2 in Human Type I Collagen Gene Expression

2015 ◽  
Vol 116 (3) ◽  
pp. 408-417 ◽  
Author(s):  
Georgia Schäfer ◽  
Jessica K. Hitchcock ◽  
Tamlyn M. Shaw ◽  
Arieh A. Katz ◽  
M. Iqbal Parker
Keyword(s):  
Gene Expression ◽  
Type I Collagen ◽  
Annexin A2 ◽  
Type I ◽  
Collagen Gene ◽  
Human Type ◽  
Collagen Gene Expression
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