Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin

Hiromi Furuichi, Kayoko Yamashita, Miki Okada, Tetsuhiko Toyoshima, Yuirou Hata, Shigehiko Suzuki, Toshifumi Itano, Tsuyoshi Shishibori, Hiroshi Tokumitsu, Ryoji Kobayashi

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

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 was isolated from both tissues by drug affinity chromatography and was identified 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 be 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 significantly weaker than that to tranilast. Light and electron microscopic immunohistochemistry 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 microfibrils, These findings provide support for the concept that elastogenesis occurs in scar tissue and 36-kDa MAGP might be one of the targets for tranilast. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1002-1008
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume270
Issue number3
DOIs
Publication statusPublished - Apr 21 2000
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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