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10.3390/cells10071768

http://scihub22266oqcxt.onion/10.3390/cells10071768
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34359938!8307983!34359938
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suck abstract from ncbi


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pmid34359938      Cells 2021 ; 10 (7): ä
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  • Transthyretin: From Structural Stability to Osteoarticular and Cardiovascular Diseases #MMPMID34359938
  • Wieczorek E; Ozyhar A
  • Cells 2021[Jul]; 10 (7): ä PMID34359938show ga
  • 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(2+). 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(2+), 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.
  • |Amyloid/chemistry/metabolism[MESH]
  • |Amyloidosis/metabolism[MESH]
  • |Animals[MESH]
  • |Arthritis/*metabolism[MESH]
  • |Cardiovascular Diseases/*metabolism[MESH]
  • |Humans[MESH]
  • |Osteoporosis/*metabolism[MESH]
  • |Oxidative Stress[MESH]
  • |Prealbumin/chemistry/*metabolism[MESH]
  • |Protein Conformation[MESH]


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