Open AccessCollagen synthesis of human arterial smooth muscle cells: Effects of platelet‐derived growth factor, transforming growth factor‐β1 and interleukin‐1
Author(s) -
Okada Yoshikatsu,
Katsuda Shogo,
Watanabe Hideto,
Nakanishi Isao
Publication year - 1993
Publication title -
acta patholigica japonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
ISSN - 0001-6632
DOI - 10.1111/j.1440-1827.1993.tb01127.x
Subject(s) - transforming growth factor , growth factor , platelet , smooth muscle , interleukin , platelet derived growth factor , pathology , interleukin 1β , transforming growth factor beta , chemistry , microbiology and biotechnology , medicine , immunology , endocrinology , biology , platelet derived growth factor receptor , cytokine , receptor
The effects of platelet‐derived growth factor (PDGF), transforming growth factor‐β1 (TGF‐β1) and interleukin‐1 (IL‐1) on collagen synthesis of cultured human arterial smooth muscle cells in a confluent state were investigated. Synthetic activity of collagenous protein was determined with [ 3 H]‐proline uptake, and subsequent analysis of collagen types by sodium dodecylsulfte‐polyacrylmide gel electrophoresis (SDS‐PAGE) followed by fluorography. Although PDGF (0.5 U/mL and 5.0 U/mL) enhanced total collagen synthesis per dish, it suppressed total collagen synthesis per DNA (DNA content in a dish). TGF‐β1 (10 pmol/L and 100 pmol/L) enhanced total collagen synthesis both per dish and per DNA. IL‐1 (0.1 U/mL and 1.0 U/mL) suppressed total collagen synthesis both per dish and per DNA. A fluorogram revealed that human arterial smooth muscle cells synthesize types I, III, IV and V collagen. Densitometric analysis showed PDGF suppressed the proportion of type V collagen. TGF‐β1 increased the proportions of types IV and V collagen. IL‐1 elicited un‐remarkable change in the proportion of collagen types. These results suggest that, in the event of human atherosclerosis, TGS‐β1 is most effective in enhancing collagen synthesis, and PDGF modulates collagen metabolism by stimulating a cell division of smooth muscle cells with a resultant increase of collagenous protein, especially of type V collagen.