Amyloid and Amyloid-Like Aggregates: Diversity and the Term Crisis
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Amyloid and AmyloidLike Aggregates: Diversity and the Term Crisis A. B. Matiiv1, N. P. Trubitsina1, A. G. Matveenko1, Y. A. Barbitoff1,2, G. A. Zhouravleva1,3, and S. A. Bondarev1,3,a,b* 1
Department of Genetics and Biotechnology, Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia 2 Bioinformatics Institute, 197342 St. Petersburg, Russia 3 Laboratory of Amyloid Biology, St. Petersburg State University, 199034 St. Petersburg, Russia a email: [email protected] b email: [email protected] Received July 16, 2020 Revised August 5, 2020 Accepted August 5, 2020
Abstract—Active accumulation of the data on new amyloids continuing nowadays dissolves boundaries of the term “amy loid”. Currently, it is most often used to designate aggregates with crossβ structure. At the same time, amyloids also exhib it a number of other unusual properties, such as: detergent and protease resistance, interaction with specific dyes, and abil ity to induce transition of some proteins from a soluble form to an aggregated one. The same features have been also demon strated for the aggregates lacking crossβ structure, which are commonly called “amyloidlike” and combined into one group, although they are very diverse. We have collected and systematized information on the properties of more than two hundred known amyloids and amyloidlike proteins with emphasis on conflicting examples. In particular, a number of pro teins in membraneless organelles form aggregates with crossβ structure that are morphologically indistinguishable from the other amyloids, but they can be dissolved in the presence of detergents, which is not typical for amyloids. Such paradoxes signify the need to clarify the existing definition of the term amyloid. On the other hand, the demonstrated structural diver sity of the amyloidlike aggregates shows the necessity of their classification. DOI: 10.1134/S0006297920090035 Keywords: amyloids, amyloidlike aggregates, crossβ structure, prions
INTRODUCTION. BRIEF OVERVIEW OF AMYLOID RESEARCH METHODS DEVELOPMENT The term “amyloid” was introduced to scientific lit erature by the German botanist Matthias Schleiden. One of his ideas was the use the iodinestarch test to study chemical and anatomical composition of a plant cell. Originally described in 1814 by JeanJacques Colin and HenriFrançois Gaultier de Claubry, this test is based on detection of a blue stain produced in the course of reac tion of starch with iodine in the presence of sulfuric acid. Abbreviations: β2M, β2microglobulin; Aβ, amyloid β; ALS, amyotrophic lateral sclerosis; AMP, antimicrobial peptide; CRES, cystatinrelated epididymal spermatogenic (amyloid); IgLC, immunoglobulin light chain; LC, lowcomplexity (domain); RAC, reversible amyloid core; PrP, prion protein; RHIM, Rip homotypic interaction motif; TTR, transthyretin. * To whom correspondence should be addressed.
When applying this technique to analyze plant prepara tions, Schleiden was the first to use the term “amyloid” (from the Latin word
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