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Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases.
Wieczorek, Elzbieta; Ozyhar, Andrzej.
  • Wieczorek E; Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
  • Ozyhar A; Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland.
Cells ; 10(7)2021 07 13.
Article in English | MEDLINE | ID: covidwho-1314588
ABSTRACT
Transthyretin (TTR) is a tetrameric protein transporting hormones in the plasma and brain, which has many other activities that have not been fully acknowledged. TTR is a positive indicator of nutrition status and is negatively correlated with inflammation. TTR is a neuroprotective and oxidative-stress-suppressing factor. The TTR structure is destabilized by mutations, oxidative modifications, aging, proteolysis, and metal cations, including Ca2+. Destabilized TTR molecules form amyloid deposits, resulting in senile and familial amyloidopathies. This review links structural stability of TTR with the environmental factors, particularly oxidative stress and Ca2+, and the processes involved in the pathogenesis of TTR-related diseases. The roles of TTR in biomineralization, calcification, and osteoarticular and cardiovascular diseases are broadly discussed. The association of TTR-related diseases and vascular and ligament tissue calcification with TTR levels and TTR structure is presented. It is indicated that unaggregated TTR and TTR amyloid are bound by vicious cycles, and that TTR may have an as yet undetermined role(s) at the crossroads of calcification, blood coagulation, and immune response.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Osteoporosis / Arthritis / Prealbumin / Cardiovascular Diseases Limits: Animals / Humans Language: English Year: 2021 Document Type: Article Affiliation country: Cells10071768

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Osteoporosis / Arthritis / Prealbumin / Cardiovascular Diseases Limits: Animals / Humans Language: English Year: 2021 Document Type: Article Affiliation country: Cells10071768