Analysis of the structure and neuritogenic activity of chondroitin sulfate/dermatan sulfate hybrid chains from porcine fetal membranes
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概要
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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.
- Springer Netherlandsの論文
著者
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Sugahara Kazuyuki
神戸薬科大学 生化
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Sugahara Kazuyuki
Hokkaido Univ. Sapporo
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Sugahara Kazuyuki
Dept. Of Biochemistry. Kobe Pharmaceutical University
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Yamada S
Department Of Bioscience And Biotechnology Fuculty Of Engineering Okayama University
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