Special Issue "Amyloidosis: Perspectives and Recent Advances"

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".

Deadline for manuscript submissions: closed (15 March 2022) | Viewed by 1378

Special Issue Editor

Dr. Cassandra Terry
E-Mail Website
Guest Editor
School of Human Sciences, London Metropolitan University, London N7 8DB, UK
Interests: amyloid; protein misfolding; protein structure; human pathogens; aggregation

Special Issue Information

Dear Colleagues,

The ability of proteins to change their secondary structure and form insoluble fibrous material named amyloid in a process called amyloidosis (or protein misfolding) is the focus of this Special Issue. In this Special Issue edited by Dr Cassandra Terry, we welcome research papers and review articles that explore the phenomenon of amyloidosis and the consequences of this in biology. We welcome papers that address the roles of amyloidogenic proteins in disease and normal physiology and papers that evaluate the interaction between these different amyloidogenic proteins. Related to disease, these could include (but are not limited to) how amyloidosis is associated with neurodegenerative diseases such as Alzheimer’s disease and prion disorders or how amyloidosis affects other parts of the body such as in diabetes or cataract formation. We also welcome papers that discuss important functional amyloids such as amyloid proteins from prokaryotes (bacteria) and eukaryotes (fungi, insects, invertebrates, and humans). Importantly, we are also interested in papers that investigate recent advances in determining structures of amyloidogenic proteins and the impact this has had on understanding disease and developing therapeutics. This could include the challenges involved in developing treatments against amyloid disorders plus advances in state-of-the-art techniques being utilised for drug discovery and therapeutic development.

This Special Edition aims to highlight the importance of amyloidosis research to give the reader a comprehensive overview outlining recent developments in research and clinical applications from different perspectives.

This Special Issue is now open for submissions. Prospective authors should first send a short abstract or tentative title to the Editorial Office. If the editors deem the topic to be appropriate for inclusion in this Special Issue, the author will be encouraged to submit a full manuscript.

Dr. Cassandra Terry
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Life is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • amyloid
  • protein misfolding 
  • neurodegenerative disease
  • protein structure
  • aggregation
  • therapeutics

Published Papers (2 papers)

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Research

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Article
Assessment of Surrogate Markers for Cardiovascular Disease in Familial Mediterranean Fever-Related Amyloidosis Patients Homozygous for M694V Mutation in MEFV Gene
Life 2022, 12(5), 631; https://doi.org/10.3390/life12050631 - 25 Apr 2022
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Abstract
Cardiovascular disease (CVD) remains underestimated in familial Mediterranean fever-associated AA amyloidosis (FMF-AA). We aimed to compare early markers of endothelial dysfunction and atherosclerosis in FMF-AA with a homozygous M694V mutation (Group 1 = 76 patients) in the Mediterranean fever (MEFV) gene [...] Read more.
Cardiovascular disease (CVD) remains underestimated in familial Mediterranean fever-associated AA amyloidosis (FMF-AA). We aimed to compare early markers of endothelial dysfunction and atherosclerosis in FMF-AA with a homozygous M694V mutation (Group 1 = 76 patients) in the Mediterranean fever (MEFV) gene and in patients with other genotypes (Group 2 = 93 patients). Measures of increased risk for future CVD events and endothelial dysfunction, including flow-mediated dilatation (FMD), pentraxin-3 (PTX3), and carotid intima-media thickness (cIMT), and fibroblast growth factor 23 (FGF23) as a marker of atherosclerotic vascular disease were compared between groups. The frequency of clinical FMF manifestations did not differ between the two groups apart from arthritis (76.3% in Group 1 and 59.1% in Group 2, p < 0.05). FMD was significantly lower in Group 1 when compared with Group 2 (MD [95% CI]: −0.6 [(−0.89)–(−0.31)]). cIMT, FGF23, and PTX3 levels were higher in Group 1 (cIMT MD [95% CI]: 0.12 [0.08–0.16]; FGF23 MD [95% CI]: 12.8 [5.9–19.6]; PTX3 MD [95% CI]: 13.3 [8.9–17.5]). In patients with FMF-AA, M694V homozygosity is associated with lower FMD values and higher cIMT, FGF23, and PTX3 levels, suggesting increased CVD risk profiles. These data suggest that a genotype–phenotype association exists in terms of endothelial dysfunction and atherosclerosis in patients with FMF-AA. Full article
(This article belongs to the Special Issue Amyloidosis: Perspectives and Recent Advances)
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Review

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Review
Factors That Contribute to hIAPP Amyloidosis in Type 2 Diabetes Mellitus
Life 2022, 12(4), 583; https://doi.org/10.3390/life12040583 - 14 Apr 2022
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Abstract
Cases of Type 2 Diabetes Mellitus (T2DM) are increasing at an alarming rate due to the rise in obesity, sedentary lifestyles, glucose-rich diets and other factors. Numerous studies have increasingly illustrated the pivotal role that human islet amyloid polypeptide (hIAPP) plays in the [...] Read more.
Cases of Type 2 Diabetes Mellitus (T2DM) are increasing at an alarming rate due to the rise in obesity, sedentary lifestyles, glucose-rich diets and other factors. Numerous studies have increasingly illustrated the pivotal role that human islet amyloid polypeptide (hIAPP) plays in the pathology of T2DM through damage and subsequent loss of pancreatic β-cell mass. HIAPP can misfold and form amyloid fibrils which are preceded by pre-fibrillar oligomers and monomers, all of which have been linked, to a certain extent, to β-cell cytotoxicity through a range of proposed mechanisms. This review provides an up-to-date summary of recent progress in the field, highlighting factors that contribute to hIAPP misfolding and aggregation such as hIAPP protein concentration, cell stress, molecular chaperones, the immune system response and cross-seeding with other amyloidogenic proteins. Understanding the structure of hIAPP and how these factors affect amyloid formation will help us better understand how hIAPP misfolds and aggregates and, importantly, help identify potential therapeutic targets for inhibiting amyloidosis so alternate and more effective treatments for T2DM can be developed. Full article
(This article belongs to the Special Issue Amyloidosis: Perspectives and Recent Advances)
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