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

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Title: Analysis of the structure and neuritogenic activity of chondroitin sulfate/dermatan sulfate hybrid chains from porcine fetal membranes
Authors: Hashiguchi, Taishi Browse this author
Mizumoto, Shuji Browse this author →KAKEN DB
Yamada, Shuhei Browse this author →KAKEN DB
Sugahara, Kazuyuki Browse this author →KAKEN DB
Keywords: Chondroitin sulfate
Dermatan sulfate
L-Iduronic acid
Amniotic membrane
Fetal membranes
Neurite outgrowth-promoting activity
Issue Date: Jan-2010
Publisher: Springer Netherlands
Journal Title: Glycoconjugate Journal
Volume: 27
Issue: 1
Start Page: 49
End Page: 60
Publisher DOI: 10.1007/s10719-009-9253-x
PMID: 19806451
Abstract: 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.
Rights: The final publication is available at www.springerlink.com
Type: article (author version)
URI: http://hdl.handle.net/2115/49186
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 水本 秀二

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