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Titolo:
Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M
Autore:
Almeida, MR; Alves, IL; Terazaki, H; Ando, Y; Saraiva, MJ;
Indirizzi:
Kumamoto Univ, Sch Med, Unidade Amiloide, Inst Biol Mol & Celular, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 Biol Mol & Celular, Kumamoto 860, Japan Univ Porto, Dept Biol Mol, Inst Ciencias Biomed Abel Salazar, P-4100 Porto, Portugal Univ Porto Porto Portugal P-4100 ed Abel Salazar, P-4100 Porto, Portugal Kumamoto Univ, Sch Med, Dept Internal Med 1, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 ept Internal Med 1, Kumamoto 860, Japan Kumamoto Univ, Sch Med, Dept Lab Med, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 Med, Dept Lab Med, Kumamoto 860, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 3, volume: 270, anno: 2000,
pagine: 1024 - 1028
SICI:
0006-291X(20000421)270:3<1024:CSOTTV>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYROXINE-BINDING; SERUM TRANSTHYRETIN; PRE-ALBUMIN; STABILITY; MET-119; FAP;
Keywords:
amyloidosis; familial amyloidotic polyneuropathy (FAP); transthyretin (TTR); thyroxine binding; stability;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Almeida, MR Kumamoto Univ, Sch Med, Unidade Amiloide, Inst Biol Mol & Celular, Kumamoto 860, Japan Kumamoto Univ Kumamoto Japan 860 elular, Kumamoto 860, Japan
Citazione:
M.R. Almeida et al., "Comparative studies of two transthyretin variants with protective effects on familial amyloidotic polyneuropathy: TTR R104H and TTR T119M", BIOC BIOP R, 270(3), 2000, pp. 1024-1028

Abstract

Recently a new nonpathogenic transthyretin (TTR) variant-TTR R104H (TTR H104)-has been described in heterozygotic and compound heterozygotic individuals from a Japanese family with familial amyloidotic polyneuropathy (FAP). The compound heterozygotic individual, a carrier of TTR V30M (TTR M30) and TTR R104H (TTR M30/H104) presented a very mild form of FAP with slow progression of the disease. TTR and retinol binding protein (RBP) levels were found to be increased in serum from TTR H104 carriers. These characteristics are very similar to those found in compound heterozygotic carriers of TTR V30M-T119M (TTR M30/M119). To structurally compare these variants, we performed stability and thyroxine (T-4) binding studies. TTR M30/H104 showed an increased resistance to dissociation into monomers similar to TTR M30/M119. This suggests that the His104 substitution has the same stabilizing effect on tetrameric TTR as the Met119 substitution. Concerning T-4 binding, TTR H104 presents a T-4 binding affinity lower than that of TTR M119, but still higher than normal TTR, However, TTR from the compound heterozygotic carrierof TTR M30/H104 presented a T-4 binding affinity lower than normal. The results indicate that the His 104 substitution induces structural alterationsthat increase the stability of the tetramer in compound heterozygotes for TTR M30 despite a lower affinity for T-4 binding. Thus, stability of TTR and binding affinity for T-4 may not be related. More detailed characterization of these variants is needed to clarify the structural alterations responsible for their increased stability. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 14:46:08