Living with the enemy: from protein-misfolding pathologies we know, to those we want to know

被引：28

作者：

Emwas, Abdul-Hamid ^{[1
]}

Alghrably, Mawadda ^{[2
]}

Dhahri, Manel ^{[3
]}

Sharfalddin, Abeer ^{[4
]}

Alsiary, Rawiah ^{[5
]}

Jaremko, Mariusz ^{[2
]}

Faa, Gavino ^{[6
]}

Campagna, Marcello ^{[6
]}

Congiu, Terenzio ^{[6
]}

Piras, Monica ^{[6
]}

Piludu, Marco ^{[7
]}

Pichiri, Giuseppina ^{[6
]}

Coni, Pierpaolo ^{[6
]}

Lachowicz, Joanna Izabela ^{[6
]}

机构：

[1] King Abdullah Univ Sci & Technol, Core Labs, Thuwal 239556900, Saudi Arabia

[2] King Abdullah Univ Sci & Technol KAUST, Biol & Environm Sci & Engn Div BESE, Thuwal 239556900, Saudi Arabia

[3] Taibah Univ, Fac Sci Yanbu, Dept Biol, Yanbu El Bahr 46423, Saudi Arabia

[4] King Abdulaziz Univ, Fac Sci, Dept Chem, POB 80203, Jeddah 21589, Saudi Arabia

[5] King Saud Bin Abdulaziz Univ Hlth Sci, Western Reg Hosp MNGHA, King Abdullah Int Med Res Ctr, Jeddah, Saudi Arabia

[6] Univ Cagliari, Dept Med Sci & Publ Hlth, Cittadella Univ, I-09042 Monserrato, Italy

[7] Univ Cagliari, Dept Biomed Sci, Cittadella Univ, I-09042 Monserrato, Italy

来源：

AGEING RESEARCH REVIEWS | 2021年 / 70卷

关键词：

alpha-1 antitrypsin (AAT); Tau protein (Tau); human islet amyloid polypeptide (hIAPP); diabetes; neurodegeneration; metal binding; ISLET-AMYLOID-POLYPEPTIDE; UBIQUITIN-PROTEASOME SYSTEM; PANCREATIC BETA-CELLS; ALZHEIMERS-DISEASE; ALPHA-SYNUCLEIN; ALPHA-1-ANTITRYPSIN DEFICIENCY; ALPHA(1)-ANTITRYPSIN DEFICIENCY; CEREBROSPINAL-FLUID; IRON-METABOLISM; MOUSE MODEL;

D O I：

10.1016/j.arr.2021.101391

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Conformational diseases are caused by the aggregation of misfolded proteins. The risk for such pathologies develops years before clinical symptoms appear, and is higher in people with alpha-1 antitrypsin (AAT) polymorphisms. Thousands of people with alpha-1 antitrypsin deficiency (AATD) are underdiagnosed. Enemyaggregating proteins may reside in these underdiagnosed AATD patients for many years before a pathology for AATD fully develops. In this perspective review, we hypothesize that the AAT protein could exert a new and previously unconsidered biological effect as an endogenous metal ion chelator that plays a significant role in essential metal ion homeostasis. In this respect, AAT polymorphism may cause an imbalance of metal ions, which could be correlated with the aggregation of amylin, tau, amyloid beta, and alpha synuclein proteins in type 2 diabetes mellitus (T2DM), Alzheimer's and Parkinson's diseases, respectively.

引用

页数：18

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