molecular characterisation of a transthyretin variant and an amyloidogenic apolipoprotein A-1
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molecular characterisation of a transthyretin variant and an amyloidogenic apolipoprotein A-1 by Nicholas J. S. Fitch

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Published by University of Birmingham in Birmingham .
Written in English


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Edition Notes

Thesis (Ph.D.)- University of Birmingham, Dept. of Genetics.

Statementby NicholasJ. S. Fitch.
ID Numbers
Open LibraryOL13929200M

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However, the molecular mechanisms of amyloid formation are still poorly characterised. In certain forms of familial amyloidotic polyneuropathy (FAP), the amyloid fibrils are mostly constituted by variants of transthyretin (TTR). V30M-TTR is the most frequent variant, and L55P-TTR is the variant associated with the most aggressive form of by:   Normal transthyretin itself is amyloidogenic, causing systemic and cardiac amyloidosis in the elderly. 7,8 Other proteins involved in familial amyloidosis are gelsolin, fibrinogen, lysozyme, and apolipoprotein AI (apoAI or apoLPAI). This Commentary will focus on familial amyloidosis and specifically on the form described as AapoAI, in which the. A new transthyretin variant (Glu61Gly) associated with cardiomyopathy. Amyloid , 14, DOI: / Akira Shimizu, Toyofumi Nakanishi, Ayako Miyazaki. Detection and characterization of variant and modified structures of proteins in Cited by: Sequence of the apolipoprotein A-1 gene was normal except for a G/C transversion at position which predicts an Arg to Pro substitution at residue This mutation, unlike previously described amyloidogenic mutations is not in the N-terminal fragment which is incorporated into the fibril. The mutation is at the same residue as in apolipoprotein A-1 Milano (ArgCys) which does not result in amyloid by:

  Human transthyretin (TTR) is implicated in several fatal forms of amyloidosis. Many mutations of TTR have been identified; most of these are pathogenic, but some offer protective by: 9. Transthyretin (TTR) pVI (rs‐A) is one of the variants in the human TTR gene associated with systemic amyloidosis. It results from a G to A transition at a CG dinucleotide in the codon for amino acid of the mature protein (TTR VI).Cited by: 7. Takada Y, Sasaki J, Ogata S, Nakanishi T, Ikehara Y, et al. () Isolation and characterization of human apolipoprotein A-I Fukuoka ( Glu––Lys). A novel apolipoprotein variant. Biochim Biophys Acta –Cited by:   Transthyretin amyloidosis is a slowly progressive condition characterized by the buildup of abnormal deposits of a protein called amyloid (amyloidosis) in the body's organs and tissues. These protein deposits most frequently occur in the peripheral nervous system, which is made up of nerves connecting the brain and spinal cord to muscles and sensory cells that detect sensations such as .

  Certain forms of systemic amyloidosis have been associated with the pathologic deposition as fibrils of three different apolipoprotein-related proteins—apolipoprotein A-I, apolipoprotein A-II Cited by:   A glimpse of a possible amyloidogenic intermediate of transthyretin. whereas ∼ 70 single site variants are associated with F A molecular mechanism for transthyretin Cited by: Transthyretin (TTR) is a tetrameric protein found in the bloodstream at a concentration of ≈ 5 μM, comprising identical amino-acid β-sheet-rich subunits in homozygotes (Fig. 1a).2, 3, 4 In heterozygotes, TTR tetramers are made up of variant and/or wild-type subunits combined in a statistical fashion. 5 The established function of TTR in the blood is to transport holoretinol binding Cited by: Two different types of amyloid deposits - Apolipoprotein A-IV and transthyretin - In a patient with systematic amyloidosis Article PDF Available.