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Book: Immunotherapy and biomarkers in neurodegenerative disorders

Ingelsson, Martin / Lannfelt, Lars

(Methods in pharmacology and toxicology ; Springer protocols)

2016

Author's details	edited by Martin Ingelsson and Lars Lannfelt, Department of Public Health and Caring Sciences/Geriatrics, Uppsala University, Uppsala, Sweden
Series title	Methods in pharmacology and toxicology Springer protocols
Language	English
Size	X, 289 Seiten, Illustrationen, Diagramme
Publisher	Humana Press
Publishing place	New York
Publishing country	United States
Document type	Book
HBZ-ID	HT018964217
ISBN	978-1-4939-3558-1 ; 9781493935604 ; 1-4939-3558-5 ; 1493935607
Database	Catalogue ZB MED Medicine, Health

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2016 A 1706	available for loan (reading room)	Lesesaal EG

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Article ; Online: A light at the end of the tunnel - from mutation identification to a potential treatment for Alzheimer's disease.

Lannfelt, Lars

Upsala journal of medical sciences

2023 Volume 128

Abstract: Recent advances have driven the development of immunotherapies that act by either promoting or suppressing a patient's immune system to treat inflammation, autoimmune disease, cardiovascular disease, infectious diseases, and several cancers. In addition, ...

Abstract	Recent advances have driven the development of immunotherapies that act by either promoting or suppressing a patient's immune system to treat inflammation, autoimmune disease, cardiovascular disease, infectious diseases, and several cancers. In addition, research conducted over the past 25 years has identified therapeutic targets and indicated that immunotherapy could be used to treat Alzheimer's disease (AD). Despite a number of setbacks, this approach has now led to the development of the first disease-modifying treatments for this devastating disease. A key neuropathological feature of AD is the accumulation of a ~40-amino acid peptide known as amyloid β (Aβ) in the brain and cerebrovasculature. Our detection of an Aβ precursor protein mutation that caused early-onset AD in a Swedish family by enhancing Aβ protofibril formation sharpened the focus on soluble Aβ aggregates (oligomers and protofibrils) as viable therapeutic targets. Initial studies developed and tested a mouse monoclonal antibody (mAb158) with specific conformation-dependent binding to these soluble Aβ aggregates. Treatment with mAb158 selectively reduced Aβ protofibrils in the brain and cerebrospinal fluid of a transgenic mouse model of AD. A humanized version of mAb158 (lecanemab) subsequently entered clinical trials. Based on promising Phase 2 data showing plaque clearance and reduced cognitive decline, a Phase 3 trial found that lecanemab slowed decline on the primary cognitive endpoint by 27% over 18 months and also produced positive effects on secondary clinical endpoints and key biomarkers. In July 2023, the FDA granted lecanemab a full approval, and this therapeutic antibody will be marketed as Leqembi®. This represents a significant advance for patients with AD, although many challenges remain. In particular, it is now more important than ever to identify individuals who are vulnerable to AD, so that treatment can be initiated at an early stage in the disease process.
MeSH term(s)	Mice ; Humans ; Animals ; Alzheimer Disease/genetics ; Alzheimer Disease/therapy ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/chemistry ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Mice, Transgenic ; Mutation
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor
Language	English
Publishing date	2023-11-28
Publishing country	Sweden
Document type	Journal Article ; Review
ZDB-ID	183949-4
ISSN	2000-1967 ; 0300-9734
ISSN (online)	2000-1967
ISSN	0300-9734
DOI	10.48101/ujms.v128.10316
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Book: Immunotherapy and biomarkers in neurodegenerative disorders

Ingelsson, Martin / Lannfelt, Lars

(Methods in pharmacology and toxicology, ; Springer protocols)

2016

Author's details	edited by Martin Ingelsson and Lars Lannfelt
Series title	Methods in pharmacology and toxicology, Springer protocols
MeSH term(s)	Nervous System Diseases/therapy ; Immunotherapy ; Biomarkers
Language	English
Size	x, 289 pages :, illustrations (some color) ;, 26 cm.
Document type	Book
ISBN	9781493935581 ; 1493935585 ; 9781493935604 ; 1493935607
Database	Catalogue of the US National Library of Medicine (NLM)

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Article ; Online: Mutation analysis of disease causing genes in patients with early onset or familial forms of Alzheimer's disease and frontotemporal dementia.

Pagnon de la Vega, María / Näslund, Carl / Brundin, RoseMarie / Lannfelt, Lars / Löwenmark, Malin / Kilander, Lena / Ingelsson, Martin / Giedraitis, Vilmantas

BMC genomics

2022 Volume 23, Issue 1, Page(s) 99

Abstract: Background: Most dementia disorders have a clear genetic background and a number of disease genes have been identified. Mutations in the tau gene (MAPT) lead to frontotemporal dementia (FTD), whereas mutations in the genes for the amyloid-β precursor ... ...

Abstract	Background: Most dementia disorders have a clear genetic background and a number of disease genes have been identified. Mutations in the tau gene (MAPT) lead to frontotemporal dementia (FTD), whereas mutations in the genes for the amyloid-β precursor protein (APP) and the presenilins (PSEN1, PSEN2) cause early-onset, dominantly inherited forms of Alzheimer's disease (AD). Even if mutations causing Mendelian forms of these diseases are uncommon, elucidation of the pathogenic effects of such mutations have proven important for understanding the pathogenic processes. Here, we performed a screen to identify novel pathogenic mutations in known disease genes among patients undergoing dementia investigation. Results: Using targeted exome sequencing we have screened all coding exons in eleven known dementia genes (PSEN1, PSEN2, APP, MAPT, APOE, GRN, TARDBP, CHMP2B, TREM2, VCP and FUS) in 102 patients with AD, FTD, other dementia diagnoses or mild cognitive impairment. We found three AD patients with two previously identified pathogenic mutations in PSEN1 (Pro264Leu and Met146Val). In this screen, we also identified the recently reported APP mutation in two siblings with AD. This mutation, named the Uppsala mutation, consists of a six amino acid intra-amyloid β deletion. In addition, we found several potentially pathogenic mutations in PSEN2, FUS, MAPT, GRN and APOE. Finally, APOE ε4 was prevalent in this patient group with an allele frequency of 54%. Conclusions: Among the 102 screened patients, we found two disease causing mutations in PSEN1 and one in APP, as well as several potentially pathogenic mutations in other genes related to neurodegenerative disorders. Apart from giving important information to the clinical investigation, the identification of disease mutations can contribute to an increased understanding of disease mechanisms.
MeSH term(s)	Alzheimer Disease/genetics ; Amyloid beta-Peptides ; Frontotemporal Dementia/genetics ; Humans ; Membrane Glycoproteins ; Mutation ; Presenilin-1/genetics ; Presenilin-2/genetics ; Receptors, Immunologic
Chemical Substances	Amyloid beta-Peptides ; Membrane Glycoproteins ; Presenilin-1 ; Presenilin-2 ; Receptors, Immunologic ; TREM2 protein, human
Language	English
Publishing date	2022-02-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2041499-7
ISSN	1471-2164 ; 1471-2164
ISSN (online)	1471-2164
ISSN	1471-2164
DOI	10.1186/s12864-022-08343-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Lecanemab, Aducanumab, and Gantenerumab - Binding Profiles to Different Forms of Amyloid-Beta Might Explain Efficacy and Side Effects in Clinical Trials for Alzheimer's Disease.

Söderberg, Linda / Johannesson, Malin / Nygren, Patrik / Laudon, Hanna / Eriksson, Fredrik / Osswald, Gunilla / Möller, Christer / Lannfelt, Lars

Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics

2022 Volume 20, Issue 1, Page(s) 195–206

Abstract: Immunotherapy against amyloid-beta (Aβ) is a promising option for the treatment of Alzheimer's disease (AD). Aβ exists as various species, including monomers, oligomers, protofibrils, and insoluble fibrils in plaques. Oligomers and protofibrils have been ...

Abstract	Immunotherapy against amyloid-beta (Aβ) is a promising option for the treatment of Alzheimer's disease (AD). Aβ exists as various species, including monomers, oligomers, protofibrils, and insoluble fibrils in plaques. Oligomers and protofibrils have been shown to be toxic, and removal of these aggregates might represent an effective treatment for AD. We have characterized the binding properties of lecanemab, aducanumab, and gantenerumab to different Aβ species with inhibition ELISA, immunodepletion, and surface plasmon resonance. All three antibodies bound monomers with low affinity. However, lecanemab and aducanumab had very weak binding to monomers, and gantenerumab somewhat stronger binding. Lecanemab was distinctive as it had tenfold stronger binding to protofibrils compared to fibrils. Aducanumab and gantenerumab preferred binding to fibrils over protofibrils. Our results show different binding profiles of lecanemab, aducanumab, and gantenerumab that may explain clinical results observed for these antibodies regarding both efficacy and side effects.
MeSH term(s)	Humans ; Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism
Chemical Substances	aducanumab (105J35OE21) ; Amyloid beta-Peptides ; gantenerumab (4DF060P933) ; lecanemab (12PYH0FTU9)
Language	English
Publishing date	2022-10-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	2316693-9
ISSN	1878-7479 ; 1933-7213
ISSN (online)	1878-7479
ISSN	1933-7213
DOI	10.1007/s13311-022-01308-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Altered amyloid-β structure markedly reduces gliosis in the brain of mice harboring the Uppsala APP deletion.

Pagnon de la Vega, María / Syvänen, Stina / Giedraitis, Vilmantas / Hooley, Monique / Konstantinidis, Evangelos / Meier, Silvio R / Rokka, Johanna / Eriksson, Jonas / Aguilar, Ximena / Spires-Jones, Tara L / Lannfelt, Lars / Nilsson, Lars N G / Erlandsson, Anna / Hultqvist, Greta / Ingelsson, Martin / Sehlin, Dag

Acta neuropathologica communications

2024 Volume 12, Issue 1, Page(s) 22

Abstract: Deposition of amyloid beta (Aβ) into plaques is a major hallmark of Alzheimer's disease (AD). Different amyloid precursor protein (APP) mutations cause early-onset AD by altering the production or aggregation properties of Aβ. We recently identified the ... ...

Abstract	Deposition of amyloid beta (Aβ) into plaques is a major hallmark of Alzheimer's disease (AD). Different amyloid precursor protein (APP) mutations cause early-onset AD by altering the production or aggregation properties of Aβ. We recently identified the Uppsala APP mutation (APPUpp), which causes Aβ pathology by a triple mechanism: increased β-secretase and altered α-secretase APP cleavage, leading to increased formation of a unique Aβ conformer that rapidly aggregates and deposits in the brain. The aim of this study was to further explore the effects of APPUpp in a transgenic mouse model (tg-UppSwe), expressing human APP with the APPUpp mutation together with the APPSwe mutation. Aβ pathology was studied in tg-UppSwe brains at different ages, using ELISA and immunohistochemistry. In vivo PET imaging with three different PET radioligands was conducted in aged tg-UppSwe mice and two other mouse models; tg-ArcSwe and tg-Swe. Finally, glial responses to Aβ pathology were studied in cell culture models and mouse brain tissue, using ELISA and immunohistochemistry. Tg-UppSwe mice displayed increased β-secretase cleavage and suppressed α-secretase cleavage, resulting in AβUpp42 dominated diffuse plaque pathology appearing from the age of 5-6 months. The γ-secretase cleavage was not affected. Contrary to tg-ArcSwe and tg-Swe mice, tg-UppSwe mice were [
MeSH term(s)	Animals ; Humans ; Mice ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Amyloid Precursor Protein Secretases/metabolism ; Brain/pathology ; Disease Models, Animal ; Gliosis/pathology ; Ligands ; Mice, Transgenic
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Ligands
Language	English
Publishing date	2024-02-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2715589-4
ISSN	2051-5960 ; 2051-5960
ISSN (online)	2051-5960
ISSN	2051-5960
DOI	10.1186/s40478-024-01734-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: The interwoven fibril-like structure of amyloid-beta plaques in mouse brain tissue visualized using super-resolution STED microscopy.

Johansson, Björn / Oasa, Sho / Muntsant Soria, Aida / Tiiman, Ann / Söderberg, Linda / Amandius, Ebba / Möller, Christer / Lannfelt, Lars / Terenius, Lars / Giménez-Llort, Lydia / Vukojević, Vladana

Cell & bioscience

2023 Volume 13, Issue 1, Page(s) 142

Abstract: Background: Standard neuropathologic analysis of Alzheimer's brain relies on traditional fluorescence microscopy, which suffers from limited spatial resolution due to light diffraction. As a result, it fails to reveal intricate details of amyloid ... ...

Abstract	Background: Standard neuropathologic analysis of Alzheimer's brain relies on traditional fluorescence microscopy, which suffers from limited spatial resolution due to light diffraction. As a result, it fails to reveal intricate details of amyloid plaques. While electron microscopy (EM) offers higher resolution, its extensive sample preparation, involving fixation, dehydration, embedding, and sectioning, can introduce artifacts and distortions in the complex brain tissue. Moreover, EM lacks molecular specificity and has limited field of view and imaging depth. Results: In our study, we employed super-resolution Stimulated Emission Depletion (STED) microscopy in conjunction with the anti-human APP recombinant antibody 1C3 fluorescently labelled with DyLight Conclusions: The utilization of STED microscopy represents a groundbreaking advancement in the field, enabling researchers to delve into the characterization of local mechanisms that underlie Amyloid (Aβ) deposition into plaques and their subsequent clearance. This unprecedented level of detail is especially crucial for comprehending the etiology of Alzheimer's disease and developing the next generation of anti-amyloid treatments. By facilitating the evaluation of drug candidates and non-pharmacological interventions aiming to reduce amyloid burden, STED microscopy emerges as an indispensable tool for driving scientific progress in Alzheimer's research.
Language	English
Publishing date	2023-08-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2593367-X
ISSN	2045-3701
ISSN	2045-3701
DOI	10.1186/s13578-023-01086-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Alzheimers sjukdom – diagnostik och behandling i dag och i framtiden.

Bogdanovic, Nenad / Hansson, Oskar / Zetterberg, Henrik / Basun, Hans / Ingelsson, Martin / Lannfelt, Lars / Blennow, Kaj

Lakartidningen

2020 Volume 117

Abstract: Alzheimer's disease is the most common cause of dementia. As many as 250,000 people in Sweden will have a dementia disease in 2050. The »amyloid cascade hypothesis« is a common model which explains how β-amyloid affects the function of the nerve cells. ... ...

Title translation	Alzheimer's disease - the most common cause of dementia.
Abstract	Alzheimer's disease is the most common cause of dementia. As many as 250,000 people in Sweden will have a dementia disease in 2050. The »amyloid cascade hypothesis« is a common model which explains how β-amyloid affects the function of the nerve cells. Alzheimer's disease has a long-lasting course and can present in typical and atypical forms. CSF analyses for »core AD CSF biomarkers« and synaptic proteins have been available for clinical diagnostics. PET scanning can detect either β-amyloid or tau aggregates in the brain of living humans. Current Alzheimer's disease therapy is based on two classes of cognition-enhancing drugs: acetylcholinesterase inhibitor and NMDA-receptor antagonist, which delays cognitive decline in most patients. The latest clinical development of potential therapy for Alzheimer's is active or passive immunotherapy against brain β-amyloid and tau, where several studies have shown varying but promising treatment effects. Non-pharmacological interventions in patients with AD aim to delay the loss of mental abilities, helping people to be independent in everyday life for as long as possible, and to increase their well-being and quality of life.
MeSH term(s)	Alzheimer Disease/complications ; Alzheimer Disease/genetics ; Amyloid beta-Peptides ; Biomarkers ; Dementia/etiology ; Humans ; Quality of Life ; Sweden ; tau Proteins
Chemical Substances	Amyloid beta-Peptides ; Biomarkers ; tau Proteins
Language	Swedish
Publishing date	2020-03-09
Publishing country	Sweden
Document type	Journal Article
ZDB-ID	391010-6
ISSN	1652-7518 ; 0023-7205
ISSN (online)	1652-7518
ISSN	0023-7205
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The amyloid-β pathway in Alzheimer's disease: a plain language summary.

Hampel, Harald / Hu, Yan / Hardy, John / Blennow, Kaj / Chen, Christopher / Perry, George / Kim, Seung Hyun / Villemagne, Victor L / Aisen, Paul / Vendruscolo, Michele / Iwatsubo, Takeshi / Masters, Colin L / Cho, Min / Lannfelt, Lars / Cummings, Jeffrey L / Vergallo, Andrea

Neurodegenerative disease management

2023 Volume 13, Issue 3, Page(s) 141–149

Abstract: What is this summary about?: This plain language summary of an article published in : Why is this important?: Aβ is a protein fragment (or peptide) that exists in several forms distinguished by their size, shape/structure, degree of solubility and ... ...

Abstract	What is this summary about?: This plain language summary of an article published in Why is this important?: Aβ is a protein fragment (or peptide) that exists in several forms distinguished by their size, shape/structure, degree of solubility and disease relevance. The accumulation of Aβ plaques is a hallmark of AD. However, smaller, soluble aggregates of Aβ - including Aβ protofibrils - also play a role in the disease. Because Aβ-related disease mechanisms are complex, the diagnosis, treatment and management of AD should be reflective of and guided by up-to-date scientific knowledge and research findings in this area. This article describes the Aβ protein and its role in AD, summarizing the evidence showing that altered Aβ clearance from the brain may lead to the imbalance, toxic buildup and misfolding of the protein - triggering a cascade of cellular, molecular and systematic events that ultimately lead to AD. What are the key takeaways?: The physiological balance of brain Aβ levels in the context of AD is complex. Despite many unanswered questions, mounting evidence indicates that Aβ has a central role in driving AD progression. A better understanding of the Aβ pathway biology will help identify the best therapeutic targets for AD and inform treatment approaches.
MeSH term(s)	Humans ; Alzheimer Disease/drug therapy ; Amyloid beta-Peptides ; Brain/metabolism ; Amyloidosis ; Plaque, Amyloid
Chemical Substances	Amyloid beta-Peptides
Language	English
Publishing date	2023-03-30
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't ; Comment
ZDB-ID	2608846-0
ISSN	1758-2032 ; 1758-2024
ISSN (online)	1758-2032
ISSN	1758-2024
DOI	10.2217/nmt-2022-0037
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Aβ and tau prions feature in the neuropathogenesis of Down syndrome.

Condello, Carlo / Maxwell, Alison M / Castillo, Erika / Aoyagi, Atsushi / Graff, Caroline / Ingelsson, Martin / Lannfelt, Lars / Bird, Thomas D / Keene, C Dirk / Seeley, William W / Perl, Daniel P / Head, Elizabeth / Prusiner, Stanley B

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 46, Page(s) e2212954119

Abstract: Down syndrome (DS) is caused by the triplication of chromosome 21 and is the most common chromosomal disorder in humans. Those individuals with DS who live beyond age 40 y develop a progressive dementia that is similar to Alzheimer's disease (AD). Both ... ...

Abstract	Down syndrome (DS) is caused by the triplication of chromosome 21 and is the most common chromosomal disorder in humans. Those individuals with DS who live beyond age 40 y develop a progressive dementia that is similar to Alzheimer's disease (AD). Both DS and AD brains exhibit numerous extracellular amyloid plaques composed of Aβ and intracellular neurofibrillary tangles composed of tau. Since AD is a double-prion disorder, we asked if both Aβ and tau prions feature in DS. Frozen brains from people with DS, familial AD (fAD), sporadic AD (sAD), and age-matched controls were procured from brain biorepositories. We selectively precipitated Aβ and tau prions from DS brain homogenates and measured the number of prions using cellular bioassays. In brain extracts from 28 deceased donors with DS, ranging in age from 19 to 65 y, we found nearly all DS brains had readily measurable levels of Aβ and tau prions. In a cross-sectional analysis of DS donor age at death, we found that the levels of Aβ and tau prions increased with age. In contrast to DS brains, the levels of Aβ and tau prions in the brains of 37 fAD and sAD donors decreased as a function of age at death. Whether DS is an ideal model for assessing the efficacy of putative AD therapeutics remains to be determined.
MeSH term(s)	Adult ; Humans ; Alzheimer Disease/genetics ; Amyloid beta-Peptides/metabolism ; Brain/metabolism ; Cross-Sectional Studies ; Down Syndrome/pathology ; Prions/metabolism ; tau Proteins/metabolism
Chemical Substances	Amyloid beta-Peptides ; Prions ; tau Proteins
Language	English
Publishing date	2022-11-07
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2212954119
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