Transthyretin

A number of proteins related to the homotetrameric trans-port protein transthyretin (TTR) forms a highly conserved protein family, whichwe present in an integrated analysis of data from different sources combined with an initial bio-chemical characterization.Homologues of the transthyretin-relatedprotein (TRP) canbe found inawide rangeof species including bacteria, plants and animals, whereas transthyre-tinshave so faronlybeen identified invertebrates.

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Retinol-binding protein transports retinol, and circulates in the plasma as a macromolecular complex with the protein transthyretin. Under acidic con-ditions retinol-binding protein undergoes a transition to the molten globule state, and releases the bound retinol ligand. A biased molecular dynamics simulation method has been used to generate models for the ensemble of conformers populated within this molten globule state.

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The relationship between the structure of the N-terminal sequence of trans-thyretin (TTR) and the binding of thyroid hormone was studied. A recom-binant human TTR and two derivatives of Crocodylus porosusTTRs, one with the N-terminal sequence replaced by that of human TTR (human⁄crocTTR), the other with the N-terminal segment removed (trun-cated crocTTR), were synthesized inPichia pastoris.

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The role of amino acid side chain oxidation in the formation of amyloid assemblies has been investigated. Chemical oxidation of amino acid side chains has been used as a facile method of introducing mutations on pro-tein structures. Oxidation promotes changes within tertiary contacts that enable identification of residues and interactions critical in stabilizing pro-tein structures.

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Familial amyloidotic polyneuropathy (FAP) is an inherited autosomal dominant disease that is commonly caused by accumulation of deposits of transthyretin (TTR) amyloid around peripheral nerves. The only effective treatment for FAP is liver transplantation.

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Transthyretin is a tetrameric binding protein involved in the transport of thyroid hormones and in the cotransport of retinol by forming a complex in plasma with retinol-binding protein. In the present study, we report the crystal structure of a macromolecular complex, in which human transthy-retin, human holo-retinol-binding protein and a murine anti-retinol-binding protein Fab are assembled according to a 1 : 2 : 2 stoichiometry.

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Human transthyretin (hTTR) is one of several proteins known to cause amyloid disease. Conformational changes in its native structure result in aggregation of the protein, leading to insoluble amyloid fibrils. The trans-thyretin (TTR)-related proteins comprise a protein family of 5-hydroxyiso-urate hydrolases with structural similarity to TTR.

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The structure of the thyroid hormone distributor protein, transthyretin, has been highly conserved during the evolution of vertebrates. Over the last decade, studies into the evolution of transthyretin have revealed the exis-tence of a transthyretin homolog, transthyretin-like protein, in all king-doms. Phylogenetic studies have suggested that the transthyretin gene in fact arose as a result of a duplication of the transthyretin-like protein gene in early protochordate evolution.

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A survey of the expression of the transthyretin and thyroxine-binding glob-ulin genes in various species during development provides clues as to how the present thyroid hormone distribution network in extracellular compart-ments developed during vertebrate evolution. Albumin may be the ‘oldest’ component of the thyroid hormone distribution network as it is found in the plasma of all vertebrates investigated.

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Thyroid hormones are involved in growth and development, particularly of the brain. Thus, it is imperative that these hormones get from their site of synthesis to their sites of action throughout the body and the brain. This role is fulfilled by thyroid hormone distributor proteins. Of particular inter-est is transthyretin, which in mammals is synthesized in the liver, choroid plexus, meninges

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Transthyretin is one of the three major thyroid hormone-binding proteins in plasma and⁄or cerebrospinal fluid of vertebrates. It transports retinol via binding to retinol-binding protein, and exists mainly as a homotetrameric protein of55 kDa in plasma. The first 3D structure of transthyretin was an X-ray crystal structure from human transthyretin.

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Accumulation ofb-amyloid protein (Ab) is one of the most important pathological features of Alzheimer’s disease. Although Abinduces neurode-generation in the cortex and hippocampus through several molecular mech-anisms, few studies have evaluated the modulation of transcription factors during Ab-induced neurotoxicity.

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Transthyretin (TTR), an amyloid-beta (Ab) scavenger protein, and metallo-thioneins 2 and 3 (MT2 and MT3), low molecular weight metal-binding proteins, have recognized impacts in Abmetabolism. Because TTR binds MT2, an ubiquitous isoform of the MTs, we investigated whether it also interacts with MT3, an isoform of the MTs predominantly expressed in the brain, and studied the role of MT2 and MT3 in human TTR–Abbinding.

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To better understand the role of neuropeptide Y (NPY) in bone homeosta-sis, as its function in the regulation of bone mass is unclear, we assessed its expression in this tissue. By immunohistochemistry, we demonstrated, both at embryonic stages and in the adult, that NPY is synthesized by osteoblasts, osteocytes, and chondrocytes.

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During vertebrate evolution, the N-terminal region of transthyretin (TTR) subunit has undergone a change in both length and hydropathy. This was previously shown to change the binding affinity for thyroid hormones (THs). However, it was not known whether this change affects other functions of TTR. In the present study, the effect of these changes on the binding of TTR to retinol-binding protein (RBP) was determined.

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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Functional characterization of Arabidopsis thaliana transthyretin-like protein

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