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Life
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Amyloids, Prions, and Related Phenomena
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Amyloids, Prions, and Related Phenomena

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

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 3455

Special Issue Editor

Dr. Vitaly Kushnirov

E-Mail Website
Guest Editor
A.N. Bach Institute of Biochemistry, Federal Research Center “Fundamentals of Biotechnology” of the Russian Academy of Sciences, 119071 Moscow, Russia
Interests: Prion; amyloid; chaperone; Sup35; yeast; translation termination; amyloidosis; Alzheimer's disease
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues,

Amyloids and prions are a rapidly growing field of research. Initially they were associated with incurable diseases in humans and animals. However, later, it was found that some amyloids can serve as a basis for several biologically important mechanisms, like long-term memory. Prions were also found in yeast and fungi, where they manifest themselves as heritable and potentially useful phenotypes. A recent addition to this group was the finding of a large number of proteins forming non-amyloid yeast prions. Their structural basis is still unclear. In many cases, amyloids are formed by natively unfolded proteins or protein domains. Such proteins can also form a separate liquid phase (a reversible “liquid” aggregate). Such aggregates can serve for the compartmentalization of certain processes, for the preservation and storage of certain proteins and mRNA, but they can also facilitate amyloid formation de novo.

This Special issue will cover all the described phenomena, and we invite you to enrich and enlarge this field with your research.

You may choose our Joint Special Issue in International Journal of Molecular Sciences.

Dr. Vitaly Kushnirov
Guest Editor

Manuscript Submission Information

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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 2600 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
  • Prion
  • Functional amyloid
  • Heritable protein aggregates
  • Liquid–liquid phase separation
  • Chaperones
  • amyloidosis
  • Alzheimer's disease

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Published Papers (1 paper)

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19 pages, 2945 KiB  
Article
Right Heart Changes Impact on Clinical Phenotype of Amyloid Cardiac Involvement: A Single Centre Study
by Sebastiano Cicco, Antonio Giovanni Solimando, Roberta Buono, Nicola Susca, Gianfranco Inglese, Assunta Melaccio, Marcella Prete, Roberto Ria, Vito Racanelli and Angelo Vacca
Life 2020, 10(10), 247; https://doi.org/10.3390/life10100247 - 18 Oct 2020
Cited by 8 | Viewed by 3028
Abstract
Amyloidosis is due to deposition of an excessive amount of protein in many parenchymal tissues, including myocardium. The onset of cardiac Amyloidosis (CA) is an inauspicious prognostic factor, which can lead to sudden death. We retrospectively analyzed 135 patients with systemic amyloidosis, admitted [...] Read more.
Amyloidosis is due to deposition of an excessive amount of protein in many parenchymal tissues, including myocardium. The onset of cardiac Amyloidosis (CA) is an inauspicious prognostic factor, which can lead to sudden death. We retrospectively analyzed 135 patients with systemic amyloidosis, admitted to our ward between 1981 and 2019. Among them, 54 patients (46.30% F/53.70% M, aged 63.95 ± 12.82) presented CA at baseline. In 53 patients, it was associated with a multiorgan involvement, while in one there was a primary myocardial deposition. As a control group, we enrolled 81 patients (49.30% F/50.70% M, aged 58.33 ± 15.65) who did not meet the criteria for CA. In 44/54 of patients CA was associated with AL, 5/54 with AA and 3/54 of patients with ATTR, and in 1/54 AL was related to hemodialysis and in 1/54 to Gel-Amyloidosis. The most common AL type was IgG (28/44); less frequent forms were either IgA (7/44) or IgD (2/44), while seven patients had a λ free light chain form. The 32 AL with complete Ig were 31 λ-chain and just one k-chain. CA patients presented normal BP (SBP 118.0 ± 8.4 mmHg; DBP 73.8 ± 4.9 mmHg), while those with nCA had an increased proteinuria (p = 0.02). TnI and NT-proBNP were significantly increased compared to nCA (p = 0.031 and p = 0.047, respectively). In CA patients we found an increased LDH compared to nCA (p = 0.0011). CA patients were also found to have an increased interventricular septum thickness compared to nCA (p = 0.002), a decreased Ejection Fraction % (p = 0.0018) and Doppler velocity E/e’ ratio (p = 0.0095). Moreover, CA patients had an enhanced right atrium area (p = 0.0179), right ventricle basal diameter (p = 0.0112) and wall thickness (p = 0.0471) compared to nCA, and an increased inferior cava vein diameter (p = 0.0495) as well. TAPSE was the method chosen to evaluate systolic function of the right heart. In CA subjects very poor TAPSE levels were found compared to nCA patients (p = 0.0495). Additionally, we found a significant positive correlation between TAPSE and lymphocyte count (r = 0.47; p = 0.031) as well as Gamma globulins (r = 0.43, p = 0.033), Monoclonal components (r = 0.72; p = 0.047) and IgG values (r = 0.62, p = 0.018). Conversely, a significant negative correlation with LDH (r = −0.57, p = 0.005), IVS (r = −0.51, p = 0.008) and diastolic function evaluated as E/e’ (r = −0.60, p = 0.003) were verified. CA patients had very poor survival rates compared to controls (30 vs. 66 months in CA vs. nCA, respectively, p = 0.15). Mean survival of CA individuals was worse also when stratified according to NT-proBNP levels, using 2500 pg/mL as class boundary (174 vs. 5.5 months, for patients with lower vs. higher values than the median, respectively p = 0.013). In much the same way, a decreased right heart systolic function was correlated with a worse prognosis (18.0 months median survival, not reached in subjects with lower values than 18 mm, p = 0.0186). Finally, our data highlight the potential prognostic and predictive value of right heart alterations characterizing amyloidosis, as a novel clinical parameter correlated to increased LDH and immunoglobulins levels. Overall, we confirm the clinical relevance of cardiac involvement suggests that right heart evaluation may be considered as a new marker for clinical risk stratification in patients with amyloidosis. Full article
(This article belongs to the Special Issue Amyloids, Prions, and Related Phenomena)
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