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A novel GCAP1 missense mutation (L151F) in a large family with autosomal dominant cone-rod dystrophy (adCORD)
Journal article   Open access   Peer reviewed

A novel GCAP1 missense mutation (L151F) in a large family with autosomal dominant cone-rod dystrophy (adCORD)

Izabela Sokal, William J Dupps, Michael A Grassi, Jeremiah Brown Jr, Louisa M Affatigato, Nirmalya Roychowdhury, Lili Yang, Slawomir Filipek, Krzysztof Palczewski, Edwin M Stone, …
Investigative ophthalmology & visual science, Vol.46(4), pp.1124-1132
04/2005
DOI: 10.1167/iovs.04-1431
PMCID: PMC1352313
PMID: 15790869

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Abstract

To elucidate the phenotypic and biochemical characteristics of a novel mutation associated with autosomal dominant cone-rod dystrophy (adCORD). Twenty-three family members of a CORD pedigree underwent clinical examinations, including visual acuity tests, standardized full-field ERG, and fundus photography. Genomic DNA was screened for mutations in GCAP1 exons using DNA sequencing and single-strand conformational polymorphism (SSCP) analysis. Function and stability of recombinant GCAP1-L151F were tested as a function of [Ca(2+)], and its structure was probed by molecular dynamics. Affected family members experienced dyschromatopsia, hemeralopia, and reduced visual acuity by the second to third decade of life. Electrophysiology revealed a nonrecordable photopic response with later attenuation of the scotopic response. Affected family members harbored a C-->T transition in exon 4 of the GCAP1 gene, resulting in an L151F missense mutation affecting the EF hand motif 4 (EF4). This change was absent in 11 unaffected family members and in 100 unrelated normal subjects. GCAP1-L151F stimulation of photoreceptor guanylate cyclase was not completely inhibited at high physiological [Ca(2+)], consistent with a lowered affinity for Ca(2+)-binding to EF4. A novel L151F mutation in the EF4 hand domain of GCAP1 is associated with adCORD. The clinical phenotype is characterized by early cone dysfunction and a progressive loss of rod function. The biochemical phenotype is best described as persistent stimulation of photoreceptor guanylate cyclase, representing a gain of function of mutant GCAP1. Although a conservative substitution, molecular dynamics suggests a significant change in Ca(2+)-binding to EF4 and EF2 and changes in the shape of L151F-GCAP1.
Humans Middle Aged Molecular Sequence Data Immunoblotting Male Mutation, Missense Retinal Degeneration - metabolism Polymorphism, Single-Stranded Conformational Genes, Dominant DNA Mutational Analysis Aged, 80 and over Adult Female Guanylate Cyclase-Activating Proteins Child Calcium-Binding Proteins - metabolism Electroretinography Amino Acid Sequence Retinal Degeneration - genetics Electrophoresis, Polyacrylamide Gel Genotype Visual Acuity Chromosomes, Human, Pair 6 - genetics Pedigree Adolescent Aged Photoreceptor Cells, Vertebrate - metabolism Retinal Degeneration - pathology Photoreceptor Cells, Vertebrate - pathology Calcium-Binding Proteins - genetics

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