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[Transthyretin-its function and pathogenesis].

¹Department of Diagnostic Medicine, Graduate School of Medical Sciences, Kumamoto University, Kuma-moto 860-0811.

Rinsho Byori. the Japanese Journal of Clinical Pathology

|June 23, 2006

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Transthyretin (TTR) is a key transport protein that can become amyloidogenic. Instability and misfolding of TTR lead to amyloid formation in diseases like senile systemic amyloidosis and familial amyloidotic polyneuropathy.

Area of Science:

Biochemistry
Molecular Biology
Pathology

Context:

Transthyretin (TTR) is a vital transport protein for thyroxin and retinol-binding protein.
Its rapid turnover and presence of four tryptophans make it a useful nutrition assessment marker.
However, TTR also serves as a precursor for amyloid fibrils in specific diseases.

Purpose:

To explore the role of TTR instability and misfolding in amyloid formation.
To understand the mechanisms leading to amyloidosis in senile systemic amyloidosis (SSA) and familial amyloidotic polyneuropathy (FAP).

Summary:

TTR's tetrameric structure can become unstable due to mutations and post-translational modifications.
This instability triggers misfolding and subsequent amyloid fibril formation in tissues.

Related Experiment Videos

The process is implicated in the pathogenesis of SSA and FAP.

Impact:

Identifies TTR instability and misfolding as central to SSA and FAP pathogenesis.
Provides a basis for ongoing therapeutic strategies targeting TTR amyloidosis.
Highlights the dual role of TTR in normal physiology and disease states.