Intimal smooth muscle cells of porcine and human coronary artery express S100A4, a marker of the rhomboid phenotype in vitro

Autor: Marc Bacchetta, Christine Chaponnier, Anne C. Brisset, Marie-Luce Bochaton-Piallat, Hiroyuki Hao, Edoardo Camenzind, Giulio Gabbiani, Jean-Charles Sanchez, Antoine Geinoz
Rok vydání: 2007
Předmět:
Pathology
Physiology
Swine
Cell
Muscle Proteins
ddc:616.07
Muscle
Smooth
Vascular
Cell Movement
Myocyte
Tissue Distribution
Child
Muscle Proteins/metabolism
Cells
Cultured
S100 Proteins
musculoskeletal system
Coronary Vessels
Endothelial stem cell
medicine.anatomical_structure
Phenotype
Atherosclerosis/metabolism/pathology
Circulatory system
cardiovascular system
Intercellular Signaling Peptides and Proteins
Stents
Cardiology and Cardiovascular Medicine
tissues
Adult
medicine.medical_specialty
Myocytes
Smooth Muscle
Biology
Muscle
Smooth
Vascular/ metabolism
Coronary Restenosis
In vivo
medicine
Animals
Humans
S100 Calcium-Binding Protein A4
Intercellular Signaling Peptides and Proteins/pharmacology
Stents/adverse effects
Tunica Intima/ metabolism/pathology
Actin
Cell Proliferation
Cell growth
Cell Movement/physiology
Coronary Restenosis/metabolism/pathology
Endothelial Cells
Atherosclerosis
Myocytes
Smooth Muscle/cytology/ metabolism/physiology
Coculture Techniques
Coronary Vessels/ metabolism/pathology
Smoothelin
Tunica Intima
Endothelial Cells/physiology
S100 Proteins/ metabolism
Zdroj: Circulation Research, Vol. 100, No 7 (2007) pp. 1055-1062
ISSN: 1524-4571
0009-7330
Popis: We reported that smooth muscle cell (SMC) populations isolated from normal porcine coronary artery media exhibit distinct phenotypes: spindle-shaped (S) and rhomboid (R). R-SMCs are recovered in higher proportion from stent-induced intimal thickening compared with media suggesting that they participate in intimal thickening formation. Our aim was to identify a marker of R-SMCs in vitro and to explore its possible expression in vivo. S- and R-SMC protein extracts were compared by means of 2-dimensional polyacrylamide gel electrophoresis followed by tandem mass spectrometry. S100A4 was found to be predominantly expressed in R-SMC extracts. Using a monoclonal S100A4 antibody we confirmed that S100A4 is highly expressed by R-SMCs and hardly detectable in S-SMCs. S100A4 was colocalized with α-smooth muscle actin in stress fibers of several quiescent cells and upregulated during migration. PDGF-BB, FGF-2 or coculture with endothelial cells, which modulate S-SMCs to a R-phenotype, increased S100A4 expression in both S- and R-SMCs. Silencing of S100A4 mRNA in R-SMCs decreased cell proliferation, suggesting a functional role for this protein. In vivo S100A4 was absent in normal porcine coronary artery media, but highly expressed by SMCs of stent-induced intimal thickening. In humans, S100A4 was barely detectable in coronary artery media and markedly expressed in SMCs of atheromatous and restenotic coronary artery lesions. Our results indicate that S100A4 is a marker of porcine R-SMCs in vitro and of intimal SMCs during intimal thickening development. It is also a marker of a large population of human atheromatous and restenotic SMCs. Clarifying S100A4 function might be useful to understand the evolution of atherosclerotic and restenotic processes.
Databáze: OpenAIRE
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