期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 73, 期 12, 页码 2735-2741出版社
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.90637
关键词
polysialic acid; glycosaminoglycan; brain-derived neurotrophic factor (BDNF); neurotrophin-3 (NT-3); neurotrophic factor
类别
资金
- Ministry of Education, Science, and Sports of Japan [20570107]
- CREST of Japan Science and Technology Agency
- Grants-in-Aid for Scientific Research [20570107] Funding Source: KAKEN
Glycosaminoglycans (GAGs), large anionic glycopolymers, are the glycan portion of proteoglycans and are important components of the extracellular matrix. Recently we reported that polysialic acid, a polyanionic glycopolymer specific to the brain, binds neurotrophic factors to form a large complex. It is not clear whether GAGs also bind neurotrophic factors to form a large complex. In the present study, we demonstrate that a brain-derived neurotrophic factor (BDNF) dimer directly binds GAGs other than chondroitin and hyaluronic acid to form a large complex. Neurotrophin-3 showed similar GAG binding properties. Furthermore, BDNF, after forming a large complex with GAG, bound to the BDNF receptors tropomyosin-related kinase (Trk) B and p75 neurotrophin receptor (NTR). These findings suggest that GAGs function to produce a reservoir of BDNF and other neurotrophic factors, and may serve to regulate their local concentrations on the cell surface.
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