{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T18:07:35Z","timestamp":1770746855653,"version":"3.49.0"},"reference-count":241,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2026,2,2]],"date-time":"2026-02-02T00:00:00Z","timestamp":1769990400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Advantageous functions have been attributed to amyloid \u03b2, which helps explain its expression despite a propensity to aggregate. Besides supporting cognitive processes, it has antimicrobial activity, e.g., amyloid \u03b2 can entrap pathogens or disrupt their membranes. Since iron is an essential element for invading organisms, limiting its availability is an antimicrobial strategy. This can be achieved by various means, such as reducing circulating iron, as is the case for anemia of inflammation or anemia of chronic disease, which may occur in Alzheimer\u2019s disease. The protein lactoferrin both sequesters iron and generates proteolytic fragments with antimicrobial properties, and amyloid \u03b2 may have similar traits. Amyloid \u03b2, which is derived from proteolytic cleavage of amyloid precursor protein, directly inhibits microorganisms. In addition, it binds redox-active metals, such as iron and copper. After being generated, amyloid \u03b2 can enter the interstitial fluid and undergo clearance by a variety of mechanisms (e.g., glymphatic system, transport across the blood\u2013brain barrier, and uptake by microglia or astrocytes). This clearance, together with its small size and iron-binding properties, positions amyloid \u03b2 to perform a surveillance function to access, capture, and export labile iron. By removing extraneous iron, amyloid \u03b2 also helps to limit metal-catalyzed reactions that cause tissue damage. In summary, besides preventing the aggregation and neurotoxicity of amyloid \u03b2, the clearance of amyloid \u03b2 from the CNS may serve a surveillance function to remove loosely bound iron to avert injury by redox reactions and enable amyloid \u03b2 to function as a mammalian siderophore making iron unavailable to invading microorganisms.<\/jats:p>","DOI":"10.3390\/ijms27031485","type":"journal-article","created":{"date-parts":[[2026,2,2]],"date-time":"2026-02-02T16:12:37Z","timestamp":1770048757000},"page":"1485","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Reexamining the Role of Amyloid \u03b2 Clearance from the Brain: Exporting Labile Iron from the Interstitial Fluid Performs a Protective Function"],"prefix":"10.3390","volume":"27","author":[{"given":"Steven M.","family":"LeVine","sequence":"first","affiliation":[{"name":"Department of Cell Biology and Physiology, University of Kansas Medical Center, 3901 Rainbow Blvd., Mail Stop 3043, Kansas City, KS 66160, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2026,2,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0197-0186(99)00125-4","article-title":"What the evolution of the amyloid protein precursor supergene family tells us about its function","volume":"36","author":"Coulson","year":"2000","journal-title":"Neurochem. 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