期刊
JOURNAL OF ALZHEIMERS DISEASE
卷 58, 期 1, 页码 185-192出版社
IOS PRESS
DOI: 10.3233/JAD-161298
关键词
Alzheimer's disease; amyloid; amyloid-beta; glycosaminoglycan; heparan sulfate; heparanase
资金
- Health Department of the Basque Country [2014111060]
- Government of the Principado de Asturias (Spain) [FC15- GRUPIN14- 141]
- Fundacion de Investigacion Oftalmologica through the Fundacion Cristina Masaveu Peterson [Instituto Universitario Fernandez- Vega
Background: Heparan sulfate proteoglycans (HSPGs) promote amyloid-beta peptide and tau fibrillization in Alzheimer's disease (AD) and provide resistance against proteolytic breakdown. Heparanase (HPSE) is the only enzyme that cleaves heparan sulfate (HS). Heparanase 2 (HPSE2) lacks HS-degrading activity, although it is able to interact with HS with high affinity. Objective: To analyze HPSE and HPSE2 expressions at different stages of AD. Methods: RT-PCR was used to analyze transcription levels of both heparanases at different stages of AD, and immunohistochemistry was performed to localize each one in different parts of the brain. Results: Both proteins appeared overexpressed at different stages of AD. Immunohistochemistry indicated that the presence of the heparanases was related to AD pathology, with intracellular deposits found in degenerated neurons. At the extracellular level, HPSE was observed only in neuritic plaques with a fragmented core, while HPSE2 appeared in those with compact cores as well. Conclusion: Given the involvement of HSPGs in AD pathology, there would seem to be a relationship between the regulation of heparanase expression, the features of the disease, and a possible therapeutic alternative.
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