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Identification of differentially regulated proteins in a patient with Leber's Congenital Amaurosis – a proteomic study

DOI: 10.1186/1477-5956-5-5

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In the LCA retina seven protein spots were differentially expressed. Six proteins were significantly up-regulated of which three could be identified as: αA-crystallin, triosephophate isomerase, and an N-terminal fragment of the β-chain of ATP synthase. One protein spot that was down-regulated in the LCA retina was identified as a C-terminal fragment of β-tubulin.Retinal tissue in LCA is characterised by an up-regulation of αA-crystallin, triosephosphate isomerase, and ATP synthase (β-chain fragment) and down-regulation of a fragment of β-tubulin. These proteins/protein fragments may play a crucial role for the retinal degeneration processes in LCA and other retinal dystrophies.In 1869 Leber described a disorder associated with congenital amaurosis, nystagmus, and the oculodigital sign that appeared to be a variety of retinitis pigmentosa. This disorder, now referred to as Leber's congenital amaurosis (LCA), is a group of autosomal recessive dystrophies with a heterogenous clinical and genetic background [1]. To date, mutations of seven genes have been reported to be implicated in the disease: RetGC1 [2,3], RPE65 [4,5], CRX [6], AIPL1 [7,8], LRAT [9], CRB1 [10], and RPGRIP [11]. In addition, two other loci may be involved: LCA3 on 14q24 [12] and LCA5 on 6q11-16 [13].LCA occurs at an incidence of 3/100,000 newborns and currently no treatment is available. The pathophysiology of LCA is unknown, however, histological data are consistent with abnormal development of photoreceptor cells in the retina and extreme premature degeneration of retinal cells [8,14-16]. It is conceivable that analysis of the differential expression of retinal proteins in LCA may provide further insight into the pathophysiology of the disease. We, therefore, performed proteomic analysis [17] of retinal tissue in 7 normal persons and one patient with LCA due to a mutation in the AIPL1 gene [7,8]. APL1 (aryl hydrocarbon receptor-interacting protein-like 1) is a member of the FK-506-binding protein f


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