ELA - Esclerose Lateral Amiotrófica
Autor: Silas Osório | Publicado: 2011-05-04T14:27:00-07:00

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Cassemiro 2004; define esclerose lateral amiotrófica (ELA) sendo uma doença do sistema nervoso, degenerativa e incapacitante, caracterizada por perda de neurônios motores no córtex, tronco cerebral, e medula espinhal. Usualmente é esporádica, mas entre 5 a 10% dos casos são herdados de forma autossômica dominante.Segundo Azano 2004, várias hipóteses têm sido levantadas para a causa desta doença, incluindo genética, auto-imune e neurotóxica. Todavia nenhuma destas está totalmente definida, exceto a causa genética. A causa genética corresponde a 5-10% dos pacientes com ELA, sendo 20% destes pacientes têm um defeito na mutação do gene que codifica a enzima superóxido dismutase 1(SOD1) localizada no cromossomo 21 e outros 80% são causados por mutações de outros genes.Para ele, a mais comum mutação da SOD1 é a substituição da valina por alanina na posição 4 (A 4V). A SOD1 é uma enzima que requer cobre para a catalização da conversão de radicais Superóxidos tóxicos para peróxido de hidrogênio e oxigênio. Com a mutação do gene SOD1 haveria acúmulo de radicais superóxidos, que exerceria efeito tóxico diretamente sobre as mitocôndrias, por interferir na integridade dos neurofilamentos e na homeostase do cálcio livre e sobre os receptores de glutamato permitindo a abertura dos canais de cálcio e entrada do cálcio livre extracelular.  Medinas 2010; acredita que o caráter autossômico dominante destas mutações revela que a hSod1 adquire propriedades tóxicas aos neurônios motores. Atualmente, duas hipóteses não mutuamente excludentes existem para explicar o caráter toxico das mutantes da hSod1 relacionadas à ELA. A primeira refere-se à produção de oxidantes pela atividade peroxidásica exacerbada das mutantes contribuindo para o estresse oxidativo observado em ELA. A segunda refere-se à agregação de proteínas como ocorre em outras doenças neurodegenerativas. Digno de nota, o radical carbonato produzido na atividade peroxidásica da hSod1 causa formação de um dímero covalente da proteína análogo a uma espécie de hSod1 frequentemente detectada em modelos experimentais e pacientes da doença e associada à propriedade tóxica das mutantes.
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 <![endif]-->  CASSEMIRO, C.R; ARCE, C.G. Comunicação visual por computador na esclerose lateral amiotrófica. Arq Bras Oftalmol. Campinas 2004;67:295-300.
  AZANO,A. Doenças do Neurônio Motor. In SILVA, G.E.G; VALENÇA, M.O.S (org). Neurologia Clínica. Recife: Editora Universitária UFPE, 2004. p. 15 – 24.
  MEDINAS, D, B. Atividade Peroxidásica da Enzima Superóxido Dismutase 1 Humana: Produção do Radical Carbonato, Dimerização Covalente da Enzima e Implicações para a Esclerose Lateral Aminiotrófica.. 2010. 99 f. Tese (Doutorado em Ciências - Bioquímica) – Instituto de Química, Universidade de São Paulo, São Paulo. 2010