Premium
EFFECT OF THE HYDROXYL RADICAL ON FIBROBLAST‐MEDIATED COLLAGEN REMODELLING IN VITRO
Author(s) -
Arisawa Shoko,
Arisawa Tomiyasu,
Ohashi Masaru,
Nitta Yukiko,
Ikeya Toshihiko,
Asai Junpei
Publication year - 1996
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/j.1440-1681.1996.tb02600.x
Subject(s) - radical , chemistry , fibroblast , hydroxyl radical , hydrogen peroxide , biophysics , in vitro , fibronectin , dimethyl sulfoxide , viability assay , biochemistry , cell , organic chemistry , biology
SUMMARY 1. It has been reported that free radicals prevent wound healing. However, the mechanism of this effect is not yet clear. We attempted to clarify the influence of hydroxyl radicals on wound healing in vitro. 2. We used an ascorbate‐copper ion system (ACS) to produce hydroxyl radicals in accordance with variables of time elapsed and concentration of copper ion. The effects of hydroxyl radical on fibroblast‐mediated collagen remodelling, cell viability, the functions of fibroblasts and collagen fibrils were studied. 3. With a copper ion concentration of 100μmol/L ACS significantly reduced contraction, while 10μmol/L stimulated contraction. Hydrogen peroxide (H 2 O 2 ) was employed in observing these findings. ACS did not influence cell viability, the expression of α 2 β 1 integrin and cellular fibronectin, or the cytoskeletal organization of fibroblasts involving actin until 3h. A concentration of ACS at 10μmol/L of copper ion induced the polymerization of collagen after 30 min, while ACS at 100 μmol/L induced collagen degradation; this finding was also established by using H 2 O 2 . Collagen reduced the amount of formaldehyde produced by trapping hydroxyl radical with dimethyl sulfoxide. 4. Our findings suggest that collagen is denatured by scavenging the hydroxyl radical before fibroblasts are damaged, so that the radical may influence the remodelling of collagen.