Novel biomarkers for the evaluation of aging-induced proteinopathies
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REVIEW ARTICLE
Novel biomarkers for the evaluation of aging-induced proteinopathies Karolin Yanar . Mehmet Can Atayik . Bahadir Simsek . Ufuk C ¸ akatay
Received: 15 February 2020 / Accepted: 2 April 2020 Ó Springer Nature B.V. 2020
Abstract Proteinopathies are characterized by aging related accumulation of misfolded protein aggregates. Irreversible covalent modifications of aging proteins may significantly affect the native three dimentional conformation of proteins, alter their function and lead to accumulation of misfolded protein as dysfunctional aggregates. Protein misfolding and accumulation of aberrant proteins are known to be associated with aging-induced proteinopathies such as amyloid ß and tau proteins in Alzheimer’s disease, a-synuclein in Parkinson’s disease and islet amyloid polypeptides in Type 2 diabetes mellitus. Protein oxidation processes such as S-nitrosylation, dityrosine formation and some of the newly elucidated processes such as carbamylation and citrullination recently drew the attention of researchers in the field of Gerontology. Studying over these processes and illuminating their relations between proteinopathies may help to diagnose early and even to treat age related disorders. Therefore, we have chosen to concentrate on aging-induced
K. Yanar U. C¸akatay (&) Department of Medical Biochemistry, Cerrahpasa Faculty of Medicine, Istanbul University-Cerrahpasa, Istanbul, Turkey e-mail: [email protected]; [email protected] M. C. Atayik B. Simsek Cerrahpasa Faculty of Medicine, Medical Program, Istanbul University-Cerrahpasa, Istanbul, Turkey
proteinopathic nature of these novel protein modifications in this review. Keywords Proteinopathy S-nitrosylation Dityrosine Carbamylation Citrullination Aging
Molecular aging of proteins Proteins play an important role in cellular structure, integrity and metabolic function. Cellular proteins fold into their correct minimal-energy conformation in order to gain their functional native conformation and maximum stability. Protein misfolding and accumulation of aberrant proteins are known to be associated with aging-induced proteinopathies such as amyloid ß and tau proteins in Alzheimer’s disease, a-synuclein in Parkinson’s disease and islet amyloid polypeptides in Type 2 diabetes mellitus (Ciceri et al. 2017; Jouanne et al. 2017; Kelly 2019; Shen et al. 2019). Molecular aging is currently thought to be inevitable an inevitable outcome of exposure of biomolecules to various types of reactive oxidants and non-ezymatic covalent modifications. As proteins are found to be highly abundant in and outside of living cells, they can easily react with variety oxidant species and they are also highly prone to nonenzymatic covalent modifications. The biological consequences of increased levels of molecular damage
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Biogerontology
are wide-ranging, including altered gene expression, genomic instability, mutations, loss of cell division potential, cell death, impaired intercellular
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