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

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Affinity chromatography
Affinity Chromatography
Skin
Carrier Proteins
Pharmaceutical Preparations
Hypertrophic Cicatrix
Tissue
Microfibrils
Keloid
Anti-Allergic Agents
Cromolyn Sodium
Elastic Tissue
tranilast
microfibrillar protein
Cicatrix
Aorta
Proteins
Immunohistochemistry
Electrons
Light

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin. / Furuichi, Hiromi; Yamashita, Kayoko; Okada, Miki; Toyoshima, Tetsuhiko; Hata, Yuirou; Suzuki, Shigehiko; Itano, Toshifumi; Shishibori, Tsuyoshi; Tokumitsu, Hiroshi; Kobayashi, Ryoji.

In: Biochemical and Biophysical Research Communications, Vol. 270, No. 3, 21.04.2000, p. 1002-1008.

Research output: Contribution to journalArticle

Furuichi, Hiromi ; Yamashita, Kayoko ; Okada, Miki ; Toyoshima, Tetsuhiko ; Hata, Yuirou ; Suzuki, Shigehiko ; Itano, Toshifumi ; Shishibori, Tsuyoshi ; Tokumitsu, Hiroshi ; Kobayashi, Ryoji. / Identification of tranilast-binding protein as 36-kDa microfibril-associated glycoprotein by drug affinity chromatography, and its localization in human skin. In: Biochemical and Biophysical Research Communications. 2000 ; Vol. 270, No. 3. pp. 1002-1008.
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