STIMULATION OF ANGIOTENSIN CONVERTING ENZYME BY TRANSFORMING GROWTH FACTOR-β1 IN RAT CARDIAC FIBROBLASTS

2000 ◽  
Vol 18 ◽  
pp. S123-S124
Author(s):  
V. Petrov ◽  
R. H. Fagard ◽  
P. J. Lijnen
Keyword(s):  
Growth Factor ◽  
Angiotensin Converting Enzyme ◽  
Transforming Growth Factor ◽  
Cardiac Fibroblasts ◽  
Transforming Growth Factor Β1 ◽  
Converting Enzyme ◽  
Stimulation Of

Angiotensin-Converting Enzyme, Transforming Growth Factor β1, and Interleukin 11 in the Osteolytic Lesions of Langerhans Cell Histiocytosis

2000 ◽  
Vol 124 (9) ◽  
pp. 1287-1290
Author(s):  
Robert E. Brown
Keyword(s):  
Growth Factor ◽  
Angiotensin Converting Enzyme ◽  
Langerhans Cell Histiocytosis ◽  
Transforming Growth Factor ◽  
Giant Cells ◽  
Transforming Growth Factor Β1 ◽  
Langerhans Cell ◽  
Converting Enzyme ◽  
Osteolytic Lesions ◽  
Interleukin 11

Abstract Objective.—To assess the expression of potential osteoclastogenic and osteolytic factors in osteolytic lesions from patients with Langerhans cell histiocytosis. Design.—Paraffin-embedded biopsy sections from 5 such archival cases underwent immunohistochemical procedures with antibodies to detect the following antigens: CD1a, S100 protein, interleukin 11, the latency-associated peptide of transforming growth factor β1, and angiotensin-converting enzyme. Results.—Commonalities noted include (1) the presence of multinucleated osteoclast-like giant cells, (2) the expression of interleukin 11 and latency-associated peptide antigens in lesional Langerhans cells, and (3) plasmalemmal immunoreactivity for angiotensin-converting enzyme antigen on non–Langerhans cell histiocytes and, on occasion, osteoclast-like giant cells and endothelial cells. Conclusions.—These observations suggest a possible pathogenetic sequence for osteolysis in Langerhans cell histiocytosis that involves angiotensin II formation, leading to the activation of latent transforming growth factor β1 and, in turn, to the enhanced production of interleukin 11, resulting in both osteoclastogenesis and impaired remodeling of bone.

Upregulation of α8β1-integrin in cardiac fibroblast by angiotensin II and transforming growth factor-β1

2001 ◽  
Vol 281 (5) ◽  
pp. C1457-C1467 ◽  
Author(s):  
Gaétan Thibault ◽  
Marie-Josée Lacombe ◽  
Lynn M. Schnapp ◽  
Alexandre Lacasse ◽  
Fatiha Bouzeghrane ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Growth Factor ◽  
Matrix Protein ◽  
Transforming Growth Factor ◽  
Cardiac Fibroblasts ◽  
Transforming Growth Factor Β1 ◽  
Cardiac Fibroblast ◽  
Extracellular Matrix Protein ◽  
Ang Ii ◽  
Tgf Β1

Using a novel pharmacological tool with125I-echistatin to detect integrins on the cell, we have observed that cardiac fibroblasts harbor five different RGD-binding integrins: α8β1, α3β1, α5β1, αvβ1, and αvβ3. Stimulation of cardiac fibroblasts by angiotensin II (ANG II) or transforming growth factor-β1 (TGF-β1) resulted in an increase of protein and heightening by 50% of the receptor density of α8β1-integrin. The effect of ANG II was blocked by an AT1, but not an AT2, receptor antagonist, or by an anti-TGF-β1 antibody. ANG II and TGF-β1 increased fibronectin secretion, smooth muscle α-actin synthesis, and formation of actin stress fibers and enhanced attachment of fibroblasts to a fibronectin matrix. The α8- and β1-subunits were colocalized by immunocytochemistry with vinculin or β3-integrin at focal adhesion sites. These results indicate that α8β1-integrin is an abundant integrin on rat cardiac fibroblasts. Its positive modulation by ANG II and TGF-β1 in a myofibroblast-like phenotype suggests the involvement of α8β1-integrin in extracellular matrix protein deposition and cardiac fibroblast adhesion.

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