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Title: Study of actin mutations linked to muscle disease
Author: Feng, Juanjuan
ISNI:       0000 0001 3459 2890
Awarding Body: Imperial College London
Current Institution: Imperial College London
Date of Award: 2008
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Mutations in actin, the major protein that forms the backbone of the thin filaments in all muscles, cause a variety of muscle diseases including nemaline myopathy (NM), congenital fibre type disproportion (CFTO), hypertrophic cardiomyopathy (HCM), and dilated cardiomyopathy (OCM). Actin is a multi-functional protein, any of its functions could be altered due to the mutation. Two assays were developed, the total internal reflectance microscopy (TIRF) polymerisation assay for visualising actin polymerisation in real time and the binding competition assay for measuring the relative binding affinity of actin for a Z-Iine protein a-actinin.. The in vitro motility assay was applied to investigate the motor and regulatory properties of actin. Six disease-causing actin mutations: V163M, E2050, 0286G, 0292V, P332S, and K336E with different clinical phenotypes were functionally characterised at the molecular level. All the mutant actins were isolated from patients' biopsies except 0286G actin, which was extracted from transgenic mouse muscle. . It has been demonstrated that actin mutations with the same clinical phenotype do not cause one common defect but rather affect various functions of actin, and there is no apparent correlations between genotype and phenotype of actin mutations.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available