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Case study of wong gillmore

It is a homotetrameric protein synthesized mainly in liver, choroid plexus, retinal pigment epithelium, and pancreas. Mutant and wildtype TTR give rise to various forms of amyloid deposition amyloidosisoriginally defined pathologically by the formation and aggregation of misfolded proteins which result in extracellular deposits that impair organ function.

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The clinical syndromes associated with TTR aggregation are familial amyloid polyneuropathy FAP and cardiomyopathy FAPin which mutant TTR protein aggregates in peripheral and autonomic nerves and heart, respectively; and senile systemic amyloidosis SSAa late-onset disorder in which wildtype protein deposits primarily in heart, but also in gut and carpal tunnel summary by Buxbaum and Reixach, However, it has no structural relationship to albumin.

Use of the term 'transthyretin' is recommended to avoid possible confusion with proalbumin and with other 'prealbumins. The mature protein consists of residues after cleavage of a amino acid signal peptide.

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Results were in agreement with those of Kanda et al. Transthyretin is a plasma transport protein for thyroxine T4 and for retinol vitamin Athrough the association with retinol-binding protein see RBP4, summary by Saraiva, Using gene targeting techniques, they generated a null mutation at the mouse Ttr locus.

Although the resultant mutant animals were phenotypically normal, viable and fertile, they had significantly depressed levels of these serum metabolites.

It is curious that in amyloid polyneuropathy, amyloid deposits do not occur in the CNS, with the exception of the blood vessels. Two equivalents of T4 bind in symmetry-related sites in the central cavity of TTR. T4 binding stabilizes the TTR tetramer and slows the rate of tetramer dissociation, which is the rate-determining step of in vitro TTR fibril formation.

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