Transthyretin

Also known as: ATTR, Prealbumin, TBPA, TTR, P02766

**Mechanism of Action** Transthyretin (TTR), also known as prealbumin, is a homotetrameric transport protein primarily synthesized in the liver and choroid plexus. It functions as a carrier for thyroxine (T4) and retinol-binding protein (RBP), facilitating the systemic transport of thyroid hormones and vitamin A. Its tetrameric structure is critical for stability; dissociation into monomers is a rate-limiting step in amyloid fibril formation, particularly in the context of transthyretin amyloidosis (ATTR). **Key Research Findings** Experimental studies have identified over 120 TTR mutations linked to familial amyloid polyneuropathy and cardiomyopathy, with the V30M variant being most prevalent. Research demonstrates that TTR tetramer stabilization via small molecules (e.g., tafamidis) or gene-silencing approaches (e.g., patisiran) reduces amyloid deposition and improves clinical outcomes. Preclinical models show that TTR aggregation is influenced by pH, metal ions, and proteolytic cleavage, with kinetic stabilizers and CRISPR-based editing under investigation as therapeutic strategies. **Clinical Relevance** TTR is a validated biomarker for nutritional status and a therapeutic target in ATTR amyloidosis. Approved therapies include tafamidis (tetramer stabilizer) and RNA-targeting agents (patisiran, vutrisiran), which slow disease progression. Experimental approaches include gene editing (CRISPR-Cas9) and novel stabilizers in early-phase trials. TTR’s role in thyroid hormone transport remains clinically relevant in metabolic and neurological disorders. For research purposes only — not medical advice.

Key data

Mechanism of action

Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain

Research & studies

Frequently asked questions

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