Colleagues are mourning the loss of David Allsop, a pioneer in Alzheimer's research. Allsop passed away March 8 after a battle with cancer. He was 67. An Alzforum member and contributor, Allsop co-chaired, with Ashley Bush, one of our early webinars on the role of metals in amyloid fibril toxicity. “Although somewhat shy, David was a man of many firsts. He was widely respected for his many contributions to AD and protein aggregation research,” wrote Dominic Walsh, Brigham and Women’s Hospital, Boston. Allsop and Walsh were collaborators.
Allsop had a varied career, working in both academia and industry. In his early days, while working with Michael Kidd at the University of Nottingham, U.K., he isolated plaque cores from human AD brains. He determined their amino acid composition, which would later turn out to be spot-on with the amyloid-β sequence (Allsop et al., 1983). Allsop was the first to raise monoclonal antibodies to that peptide, and he showed that they reacted with plaque cores and cerebral amyloid angiopathy, but not with neurofibrillary tangles (Allsop et al., 1988). This helped settle a major debate at the time, about whether plaques and tangles were related.
Allsop continued to study plaques, in both AD and Down’s syndrome, when he worked with George Glenner at the University of California, San Diego. His 1990 review, together with John Hardy, then at St. Mary’s Hospital, London, on amyloid deposition as a central event in AD has been cited more than 600 times (Hardy and Allsop, 1991).
Allsop spent two years working on AD in Japan, where he became assistant director of what was then the Psychiatric Research Institute of Tokyo, now part of the Tokyo Metropolitan Institute of Medical Science. Together with Tsuyoshi Ishii and colleagues, he found evidence for an amyloid precursor protein secretase in rat brain (Allsop et al., 1991). He subsequently joined the faculty at Queen’s University, Belfast, and worked in industry for a brief period, at SmithKline Beecham. He ultimately became chair of the department of neuroscience at Lancaster University, where he worked until his death.
Allsop was fascinated by the role of metals in fibril toxicity and by what could be learned from biological fluid markers. The first report of α-synuclein in cerebrospinal fluid came from his lab (El-Agnaf et al., 2003). More recently, Allsop became interested in the role of pollutants in dementia (Tabner et al., 2010; Mayes et al., 2014; Maher et al., 2016).
“He was someone to have a beer with, swap a bit of gossip with, as well as swap ideas,” wrote Hardy, now at University College London, and Eric Karran, who worked with Allsop at SmithKline Beecham. “He did not get the recognition he deserved, but I am sure that did not bother him. He just liked scientific experiments and generating and interpreting data. We’ll both miss him.” See tributes below.—Tom Fagan
- Allsop D, Landon M, Kidd M. The isolation and amino acid composition of senile plaque core protein. Brain Res. 1983 Jan 24;259(2):348-52. PubMed.
- Allsop D, Wong CW, Ikeda S, Landon M, Kidd M, Glenner GG. Immunohistochemical evidence for the derivation of a peptide ligand from the amyloid beta-protein precursor of Alzheimer disease. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2790-4. PubMed.
- Hardy J, Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci. 1991 Oct;12(10):383-8. PubMed.
- Allsop D, Yamamoto T, Kametani F, Miyazaki N, Ishii T. Alzheimer amyloid beta/A4 peptide binding sites and a possible 'APP-secretase' activity associated with rat brain cortical membranes. Brain Res. 1991 Jun 14;551(1-2):1-9. PubMed.
- El-Agnaf OM, Salem SA, Paleologou KE, Cooper LJ, Fullwood NJ, Gibson MJ, Curran MD, Court JA, Mann DM, Ikeda S, Cookson MR, Hardy J, Allsop D. Alpha-synuclein implicated in Parkinson's disease is present in extracellular biological fluids, including human plasma. FASEB J. 2003 Oct;17(13):1945-7. PubMed.
- Tabner BJ, Mayes J, Allsop D. Hypothesis: soluble aβ oligomers in association with redox-active metal ions are the optimal generators of reactive oxygen species in Alzheimer's disease. Int J Alzheimers Dis. 2010;2011:546380. PubMed.
- Mayes J, Tinker-Mill C, Kolosov O, Zhang H, Tabner BJ, Allsop D. β-amyloid fibrils in Alzheimer disease are not inert when bound to copper ions but can degrade hydrogen peroxide and generate reactive oxygen species. J Biol Chem. 2014 Apr 25;289(17):12052-62. Epub 2014 Mar 11 PubMed.
- Maher BA, Ahmed IA, Karloukovski V, MacLaren DA, Foulds PG, Allsop D, Mann DM, Torres-Jardón R, Calderon-Garciduenas L. Magnetite pollution nanoparticles in the human brain. Proc Natl Acad Sci U S A. 2016 Sep 27;113(39):10797-801. Epub 2016 Sep 6 PubMed.
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