The extracellular matrix enriched with membrane metalloendopeptidase and insulin‐degrading enzyme suppresses the deposition of amyloid‐beta peptide in Alzheimer's disease cell models. (28th August 2019)

• Record Type: Journal Article
• Authors: Zhang, Shumang; Xiao, Tongqian; Yu, Yanzhen; Qiao, Yong; Xu, Zhongjuan; Geng, Junsa; Liang, Yu; Mei, Yan; Dong, Qun; Wang, Bin; Wei, Jiali; Suo, Guangli
• Is Part Of: Journal of tissue engineering and regenerative medicine. Volume 13:Number 10(2019)
• Page Start: 1759
• Page End: 1769
• Publication Date: 2019-08-28
• Subjects: AD cell model -- Alzheimer's disease -- beta‐amyloid peptides -- extracellular matrix biomaterial -- insulin‐degrading enzyme -- membrane metalloendopeptidase; Tissue engineering -- Periodicals; Regeneration (Biology) -- Periodicals; 610.28
• DOI: 10.1002/term.2906
• Languages: English
• ISSNs: 1932-6254

Abstract

Abstract: Amyloid plaque is a typical feature of Alzheimer's disease (AD) and is one of the targets for AD therapy. Membrane metalloendopeptidase (MME) and insulin‐degrading enzyme (IDE) are two types of proteases that could cleave beta‐amyloid (Aβ) peptides generated by neuron cells of AD patients. Extracellular matrix (ECM) plays a crucial role in regulating tissue‐specific functions and is an ideal biomaterial for tissue repair. In this study, we extracted the liquid ECM enriched with collagen‐binding‐domain‐fused IDE or MME from human foreskin fibroblast cells. We found that these ECM biomaterials reduced the aggregation of Aβ peptides, prevented the formation of amyloid plaques, and also suppressed phosphorylation of Tau protein in AD cell models. Overall, our research provides a novel ECM biomaterial that can be potentially used for AD therapy.