Diagnostic and Treatment Approaches Involving Transthyretin in Amyloidogenic Diseases
- Authors
- Park, Gil Yong; Jamerlan, Angelo; Shim, Kyu Hwan; An, Seong Soo A.
- Issue Date
- 2-Jun-2019
- Publisher
- MDPI
- Keywords
- transthyretin; mutation; protein aggregation; amyloid; amyloidosis
- Citation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.20, no.12
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Volume
- 20
- Number
- 12
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/1352
- DOI
- 10.3390/ijms20122982
- ISSN
- 1422-0067
- Abstract
- Transthyretin (TTR) is a thyroid hormone-binding protein which transports thyroxine from the bloodstream to the brain. The structural stability of TTR in tetrameric form is crucial for maintaining its original functions in blood or cerebrospinal fluid (CSF). The altered structure of TTR due to genetic mutations or its deposits due to aggregation could cause several deadly diseases such as cardiomyopathy and neuropathy in autonomic, motor, and sensory systems. The early diagnoses for hereditary amyloid TTR with cardiomyopathy (ATTR-CM) and wild-type amyloid TTR (ATTRwt) amyloidosis, which result from amyloid TTR (ATTR) deposition, are difficult to distinguish due to the close similarities of symptoms. Thus, many researchers investigated the role of ATTR as a biomarker, especially its potential for differential diagnosis due to its varying pathogenic involvement in hereditary ATTR-CM and ATTRwt amyloidosis. As a result, the detection of ATTR became valuable in the diagnosis and determination of the best course of treatment for ATTR amyloidoses. Assessing the extent of ATTR deposition and genetic analysis could help in determining disease progression, and thus survival rate could be improved following the determination of the appropriate course of treatment for the patient. Here, the perspectives of ATTR in various diseases were presented.
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