Early diagnosis in patients with transthyretin familial amyloid polyneuropathy: A comparative study

Raya‐Cruz, Manuel; Buades-Reinés, Juan; Gállego-Lezáun, Cristina; Ripoll‐Vera, Tomás; Usón-Martín, Mercedes; Cisneros-Barroso, Eugenia

doi:10.1016/j.medcle.2016.09.042

Cited by 2 publications

(3 citation statements)

References 10 publications

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“…Ряд исследований был проведен для установления ранних нейрофизиологических маркеров минимального повреждения волокон и выявления признаков начального повреждения нерва. Лазерные вызванные потенциалы, симпатический кожный вызванный потенциал, определение порогов температурных ощущений и вариабельность частоты сердечных сокращений как показатели функционирования тонких нервных волокон обладали более высокой чувствительностью в выявлении ранних признаков ТСАП, чем обычные нейрофизиологические исследования толстых нервных волокон [15,22]. Было обнаружено снижение плотности интраэпидермальных нервных волокон у пациентов с ТСАП, что коррелировало с тяжестью полинейропатии тонких волокон [23].…”

Section: обзорыunclassified

Transthyretin familial amyloid polyneuropathy

Kopishinskaya

2018

Z. nevrol. psikhiatr. im. S.S. Korsakova

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Транстиретиновая семейная амилоидная полинейропатия (ТСАП)-прогрессирующее, приводящее к летальному исходу, заболевание. ТСАП обусловлена внеклеточным отложением нерастворимых амилоидных фибрилл в эндоневрии и проявляется сенсорными, моторными и вегетативными расстройствами и/или кардиомиопатией. Причиной ТСАП являются мутации гена белка транстиретина; известно более 100 типов таких мутаций. Ввиду фенотипического разнообразия ТСАП клиницистам часто сложно установить правильный диагноз. Ошибочная диагностика-частое явление, что увеличивает риск возникновения органной патологии. В статье изложены вопросы патогенеза, диагностики и лечения больных ТСАП.

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Section: обзорыunclassified

Transthyretin familial amyloid polyneuropathy

Kopishinskaya

2018

Z. nevrol. psikhiatr. im. S.S. Korsakova

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“…More than 100 mutations of TTR have been reported, and most of them are amyloidogenic 12,19 . The destabilizing TTR variants have been found to predispose individuals to the beginning of familial amyloid polyneuropathy, 20 familial amyloid cardiomyopathy, 17 and central nervous system selective amyloidosis 21 …”

Section: Introductionmentioning

confidence: 99%

“…18 More than 100 mutations of TTR have been reported, and most of them are amyloidogenic. 12,19 The destabilizing TTR variants have been found to predispose individuals to the beginning of familial amyloid polyneuropathy, 20 familial amyloid cardiomyopathy, 17 and central nervous system selective amyloidosis. 21 Neutron crystallographic study of the human TTR has shown that a significant hydrogen bond network around the histidine residue at position 88 is essential for the quaternary and tertiary structural stabilities.…”

Section: Introductionmentioning

confidence: 99%

Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation

Lee

Kuczera

2022

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Human transthyretin (TTR) is a homotetrameric plasma protein associated with a high percentage of β-sheet, which forms amyloid fibrils and accumulates in tissues or extracellular matrix to cause amyloid diseases. Free energy simulations based on allatom molecular dynamics simulations were carried out to analyze the effects of the His88 ! Arg, Phe, and Tyr mutations on the stability of human TTR. The calculated free energy change differences (ΔΔG) caused by the His ! Arg, Phe, and Tyr mutations at position 88 are 6.48 ± 0.45, À9.99 ± 0.54, and 2.66 ± 0.33 kcal/mol, respectively. These calculated free energy change differences between wild type and the mutants are in excellent agreement with prior experimental values. Our simulation results show that the wild type of the TTR is more stable than H88R and H88Y mutants, whereas it is less stable than the H88F mutant. The free energy component analysis shows that the primary contribution to the free energy change difference (ΔΔG) for the His ! Arg mutation arises from electrostatic interaction; the ΔΔG for the His ! Phe mutation is from van der Waals and electrostatic interactions and that for the His ! Tyr mutation from covalent interaction. The simulation results show that the free energy calculation with thermodynamic integration is beneficial for understanding the detailed microscopic mechanism of protein stability. The implications of the results for understanding stabilizing and destabilizing effect of the mutation and the contribution to protein stability are discussed.

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Early diagnosis in patients with transthyretin familial amyloid polyneuropathy: A comparative study

Cited by 2 publications

References 10 publications

Transthyretin familial amyloid polyneuropathy

Transthyretin familial amyloid polyneuropathy

Modulation of human transthyretin stability by the mutations at histidine 88 studied by free energy simulation

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