• Analysis of the structure and neuritogenic activity of chondroitin sulfate/dermatan sulfate hybrid chains from porcine fetal membranes

Hashiguchi, Taishi

Mizumoto, Shuji

Yamada, Shuhei

Sugahara, Kazuyuki

    • The final publication is available at
  • Other Chondroitin sulfate
  • Other Dermatan sulfate
  • Other L-Iduronic acid
  • Other Amniotic membrane
  • Other Fetal membranes
  • Other Neurite outgrowth-promoting activity
  • NDC 464
  • The amniotic membrane (AM) is the innermost layer of fetal membranes and possesses various biological activities. Although the mechanism underlying these biological activities remains unclear, unique components seem to be involved. AM contains various extracellular matrix components such as type I collagen, laminin, fibronectin, hyaluronic acid, and proteoglycans bearing chondroitin sulfate/dermatan sulfate (CS/DS) glycosaminoglycan side chains. To elucidate the function of CS/DS in AM, the structure and bioactivity of the CS/DS chains from porcine fetal membranes (FM-CS/DS) were investigated. A compositional analysis using various chondroitinases revealed that the characteristic DS domain comprised of iduronic acid-containing disaccharide units is embedded in FM-CS/DS, along with predominant disaccharide units, GlcA-GalNAc, GlcA-GalNAc(4-O-sulfate), and GlcA-GalNAc (6-O-sulfate), where GlcA and GalNAc represent D-glucuronic acid and N-acetyl-D-galactosamine, respectively. The average molecular size of FM-CS/DS chains was unusually large and estimated to be 250 - 300 kDa. The FM-CS/DS chains showed neurite outgrowth-promoting activity with a dendrite-like morphology, which was eliminated by digestion with chondroitinase ABC of the CS/DS chains. This activity was suppressed by antibodies against growth factors including pleiotrophin, midkine, and fibroblast growth factor-2. The binding of these growth factors to FM-CS/DS was also demonstrated by surface plasmon resonance spectroscopy.
PublisherSpringer Netherlands
Date Issued 2010-01
NIItypejournal article
Identifier URI
  • isIdenticalTo PMID 19806451
  • isIdenticalTo DOI
    • ISSN 0282-0080
    • ISSN 1573-4986
    • Glycoconjugate Journal
    27(1), 49-60