Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases
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-str...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/10/7/1768 |
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| author | Elżbieta Wieczorek Andrzej Ożyhar |
| author_facet | Elżbieta Wieczorek Andrzej Ożyhar |
| author_sort | Elżbieta Wieczorek |
| collection | DOAJ |
| description | 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 Ca<sup>2+</sup>. 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 Ca<sup>2+</sup>, 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. |
| first_indexed | 2024-03-10T09:43:24Z |
| format | Article |
| id | doaj.art-b76163adbb054bceac369997147820a9 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T09:43:24Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-b76163adbb054bceac369997147820a92023-11-22T03:29:47ZengMDPI AGCells2073-44092021-07-01107176810.3390/cells10071768Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular DiseasesElżbieta Wieczorek0Andrzej Ożyhar1Department of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wroclaw, PolandDepartment of Biochemistry, Molecular Biology and Biotechnology, Faculty of Chemistry, Wroclaw University of Science and Technology, Wybrzeże Wyspiańskiego 27, 50-370 Wroclaw, PolandTransthyretin (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 Ca<sup>2+</sup>. 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 Ca<sup>2+</sup>, 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.https://www.mdpi.com/2073-4409/10/7/1768heart diseaseatherosclerosisthrombosisinflammationCOVID-19amyloid |
| spellingShingle | Elżbieta Wieczorek Andrzej Ożyhar Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases Cells heart disease atherosclerosis thrombosis inflammation COVID-19 amyloid |
| title | Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases |
| title_full | Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases |
| title_fullStr | Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases |
| title_full_unstemmed | Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases |
| title_short | Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases |
| title_sort | transthyretin from structural stability to osteoarticular and cardiovascular diseases |
| topic | heart disease atherosclerosis thrombosis inflammation COVID-19 amyloid |
| url | https://www.mdpi.com/2073-4409/10/7/1768 |
| work_keys_str_mv | AT elzbietawieczorek transthyretinfromstructuralstabilitytoosteoarticularandcardiovasculardiseases AT andrzejozyhar transthyretinfromstructuralstabilitytoosteoarticularandcardiovasculardiseases |