Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin
H. Furuichi et al., Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin, BIOC BIOP R, 270(3), 2000, pp. 1002-1008
Citations number
14
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
To elucidate the molecular mechanism involved in the suppression of keloids
and hypertrophic scars by tranilast, we investigated the target protein of
tranilast in bovine skin and aorta. A specific tranilast-binding protein w
as isolated from both tissues by drug affinity chromatography and was ident
ified as 36-kDa microfibril-associated glycoprotein (36-kDa MAGP). Binding
of 36-kDa MAGP to tranilast seemed to be specific since 36-kDa MAGP could b
e eluted from the drug affinity column by tranilast itself and also binding
of 36-kDa MAGP to other anti-allergy drugs (amlexanox and cromolyn) is sig
nificantly weaker than that to tranilast, Light and electron microscopic im
munohistochemistry detected the protein at the periphery of elastic fibers
in normal human skin. In hypertrophic scar tissue, however, 36-kDa MAGP was
located on small bundles of micro fibrils. These findings provide support
for the concept that elastogenesis occurs in scar tissue and 36-kDa MAGP mi
ght be one of the targets for tranilast. (C) 2000 Academic Press.