Identification of Multiple Amyloidogenic Sequences in Laminin-1
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- 作者：Shingo Kasai ; Shunsuke Urushibata ; Kentaro Hozumi ; Fumiharu Yokoyama ; Naoki Ichikawa ; Yuichi Kadoya ; Norio Nishi ; Nobuhisa Watanabe ; Yoshihiko Yamada ; Motoyoshi Nomizu
- 刊名：Biochemistry
- 出版年：2007
- 出版时间：April 3, 2007
- 年：2007
- 卷：46
- 期：13
- 页码：3966 - 3974
- 全文大小：730K
- 年卷期：v.46,no.13(April 3, 2007)
- ISSN：1520-4995
文摘
Amyloid fibril formation is associated with several pathologies, including Alzheimer's disease,Parkinson's disease, type II diabetes, and prion diseases. Recently, a relationship between basementmembrane components and amyloid deposits has been reported. The basement membrane protein, laminin,may be involved in amyloid-related diseases, since laminin is present in amyloid plaques in Alzheimer'sdisease and binds to amyloid precursor protein. Recently, we showed that peptide A208 (AASIKVAVSADR),the IKVAV-containing peptide, formed amyloid-like fibrils. We previously identified 60 cell adhesivesequences in laminin-1 using a total of 673 12-mer synthetic peptides. Here, we screened for additionalamyloidogenic sequences among 60 cell adhesive peptides derived from laminin-1. We first examinedamyloid-like fibril formation by the 60 active peptides with Congo red, a histological dye binding tomany amyloid-like proteins. Thirteen peptides were stained with Congo red. Four of the 13 peptidespromoted cell attachment and neurite outgrowth like the IKVAV-containing peptide. The four peptidesalso showed amyloid-like fibril formation in both X-ray diffraction and electron microscopic analyses.The amyloidogenic peptides contain consensus amino acid components, including both basic and acidicamino acids and Ser and Ile residues. These results indicate that at least five laminin-derived peptides canform amyloid-like fibrils. We conclude that the laminin-derived amyloidogenic peptides have the potentialto form amyloid-like fibrils in vivo, possibly when laminin-1 is degraded.