Elastic fiber assembly is disrupted by excessive accumulation of chondroitin sulfate in the human dermal fibrotic disease, keloid

• Ikeda, Mika

• Naitoh, Motoko

• Kubota, Hiroshi

• Ishiko, Toshihiro

• Yoshikawa, Katsuhiro

• Yamawaki, Satoko

• Kurokawa, Masako

• Utani, Atsushi

• Nakamura, Tomiyuki

• Nagata, Kazuhiro

• Suzuki, Shigehiko

Abstract

Keloid is a fibrotic disease characterized by abnormal accumulation of extracellular matrix in the dermis. The keloid matrix contains excess collagen and glycosaminoglycans (GAGs), but lacks elastic fiber. However, the roles of these matrix components in the pathogenesis of keloid are largely unknown. Here, we show that elastin and DANCE (also known as fibulin-5), a protein required for elastic fiber formation, are not deposited in the extracellular matrix of keloids, due to excess accumulation of chondoitin sulfate (CS), although the expression of elastin and DANCE is not affected. Amount of CS accumulated in the keloid legion was 6.9-fold higher than in normal skin. Fibrillin-1, a scaffold protein for elastic fiber assembly, was abnormally distributed in the keloid matrix. Addition of purified CS to keloid fibroblast culture resulted in abnormal deposition of fibrillin-1, concomitant with significantly decreased accumulation of elastin and DANCE in the extracellular matrix. We propose that CS plays a crucial role in the development of keloid lesions through inhibition of elastic fiber assembly.

Journal

• Biochemical and Biophysical Research Communications

  Biochemical and Biophysical Research Communications 390 (4), 1221-1228, 2009-12-25

  Elsevier

Keywords

• Chondroitin sulfate
• DANCE/fibulin-5
• Elastic fibers
• Glycosaminoglycan
• Keloid
• Wound healing

Details

• CRID: 1050282810585806080
• NII Article ID: 120001749556
• ISSN: 0006291X
• HANDLE: 2433/88959
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles