{"entity": "researcher", "timestamp": "2026-08-22T08:31:55.369Z", "family": "Ozsan McMillan", "given": "Ilayda", "initials": "I", "orcid": "0000-0003-2265-5852", "affiliations": ["Department of Molecular Pharmacology & Physiology, Morsani College of Medicine, University of South Florida, Tampa, Florida, United States.", "Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida, United States."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ec112240d6845168f9cb25702a20ebf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ec112240d6845168f9cb25702a20ebf"}}, "publications": [{"entity": "publication", "iuid": "a2a84f83b77f40269b83f336a515b525", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a2a84f83b77f40269b83f336a515b525.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a2a84f83b77f40269b83f336a515b525"}}, "title": "Heparan sulfate proteoglycan in Alzheimer's disease: aberrant expression and functions in molecular pathways related to amyloid-\u03b2 metabolism.", "authors": [{"family": "Ozsan McMillan", "given": "Ilayda", "initials": "I", "orcid": "0000-0003-2265-5852", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ec112240d6845168f9cb25702a20ebf.json"}}, {"family": "Li", "given": "Jin-Ping", "initials": "JP", "orcid": "0000-0002-4255-3581", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2ab4d6e3d5eb4551a1cc622b5917dc3b.json"}}, {"family": "Wang", "given": "Lianchun", "initials": "L", "orcid": "0000-0003-1454-2719", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/85315d991d1e46b3a9ebe4c75e98b0ae.json"}}], "type": "journal article", "published": "2023-04-01", "journal": {"title": "Am. J. Physiol., Cell Physiol.", "issn": "1522-1563", "volume": "324", "issue": "4", "pages": "C893-C909", "issn-l": "0363-6143"}, "abstract": "Alzheimer's disease (AD) is the most common form of dementia. Currently, there is no effective treatment for AD, as its etiology remains poorly understood. Mounting evidence suggests that the accumulation and aggregation of amyloid-\u03b2 peptides (A\u03b2), which constitute amyloid plaques in the brain, is critical for initiating and accelerating AD pathogenesis. Considerable efforts have been dedicated to shedding light on the molecular basis and fundamental origins of the impaired A\u03b2 metabolism in AD. Heparan sulfate (HS), a linear polysaccharide of the glycosaminoglycan family, co-deposits with A\u03b2 in plaques in the AD brain, directly binds and accelerates A\u03b2 aggregation, and mediates A\u03b2 internalization and cytotoxicity. Mouse model studies demonstrate that HS regulates A\u03b2 clearance and neuroinflammation in vivo. Previous reviews have extensively explored these discoveries. Here, this review focuses on the recent advancements in understanding abnormal HS expression in the AD brain, the structural aspects of HS-A\u03b2 interaction, and the molecules involved in modulating A\u03b2 metabolism through HS interaction. Furthermore, this review presents a perspective on the potential effects of abnormal HS expression on A\u03b2 metabolism and AD pathogenesis. In addition, the review highlights the importance of conducting further research to differentiate the spatiotemporal components of HS structure and function in the brain and AD pathogenesis.", "doi": "10.1152/ajpcell.00247.2022", "pmid": "36878848", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC10069967"}], "notes": [], "created": "2026-08-21T12:27:53.614Z", "modified": "2026-08-21T12:27:53.755Z"}]}