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Sequence traces of all identified mutations top and their segregation in the respective families bottom are displayed. B Heterologous splicing assay of the c. Sequence sections of RT—PCR products from RNA of COS7 cells transfected with either mutant bottom or wildtype constructs top , and schematic overview of the deduced processing of wildtype and mutant transcripts.
Expression of an exon 16—18 minigene construct in COS7 cells revealed the activation of a cryptic splice site in the c. The mis-spliced cDNA carries a frame-shift followed by a premature termination codon. In addition to CHRO , which was found to be compound heterozygous for two nonsense mutations [c. RX and c. R29W and c. PL Fig. All mutations showed consistent independent segregation in the respective families.
All three putative splicing mutations and the c. In addition to the previously reported defects in transcript splicing induced by the c. MIfsX2 Fig. In addition to the five missense mutations identified in our study, we also included the p. YN mutation, reported by Thiadens and co-workers 14 Fig. Four of the mutant proteins p. R29W, p.
RW, p. PL and p. HL showed only minute catalytic activity that ranged between 4. In contrast, we observed considerable residual enzymatic activity for the p. EK and the p. YN mutants. YN substitution localizes within the non-catalytic GAFb domain, known to have regulatory function. In comparison with the normalized wildtype activity, this mutant showed a residual enzyme activity of The mutants p. YN and p.
EK were then further analyzed for the kinetics of the enzymatic activity in comparison with the chimeric wildtype protein. For the p. EK mutant as well as the p. YN mutant, we obtained K m values of 0. Overview of the localization of all currently known PDE6C mutations, including seven missense mutations, five splice defects, three nonsense and one frame-shift mutations.
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Equal amounts of purified protein were assayed for cGMP hydrolysis activity. Activities were normalized to the wildtype protein. Untransfected Sf9 insect cells were measured as control for intrinsic PDE activity. All the other mutants p. HL, p. PL, p.
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RW and p. R29W showed only low PDE activity not significantly different from the untransfected control. A Analysis of the substrate-binding properties of the chimeric wildtype black, filled squares , the p. YN blue, filled inverted triangles and the p. EK mutants red, filled triangles. The K m values of 0. EK and 0. YN were calculated from the fitting curves.
The activities of chimeric wildtype black, filled squares , p. EK red, filled triangles and p. YN mutants with zaprinast. Inhibition of cGMP phosphodiesterase activity by zaprinast. The rates of cGMP hydrolysis of chimeric wildtype black, filled triangles , p. EK red, filled squares and p.
YN blue, filled inverted triangles mutant protein were determined in the presence of 5 m cGMP and increasing concentrations of zaprinast. The IC 50 values of 2. EK and 8. YN mutant were calculated from the inhibition curves. Zaprinast, a competitive inhibitor specific for PDE6 and PDE5, was used to further investigate the properties of the catalytic pocket of the p.
In comparison with that, we obtained a 2. YN that showed residual enzymatic activity Fig. The IC 50 value of n m for the p. YN was approximately 3-fold higher when compared with wildtype, whereas for the p.
Counting Blue Triangles von Kimberly Haugan (E-Book) – Lulu DE
EK mutant an IC 50 value of 2. The All patients had a clinical diagnosis of ACHM, and a family history compatible with an autosomal recessive trait. Ophthalmoscopic fundus appearance was unremarkable in most subjects, but some patients showed atrophy of the retinal pigment epithelium RPE or granular pigmentation in the macula. Fundus examination was unremarkable in both patients Fig. YX E-G.
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A Fundus autofluorescence OD , B redfree OD and C blue nm OD fundus photography were unremarkable, except for a pale, thin line around the foveola of the right eye on autofluorescence imaging. D Photoreceptor layer discontinuity and optically empty cavity in the center of the fovea OD , E redfree OD , F fundus photography showed a central cystic macular lesion and G OCT also showed an optical cavity in the center of the fovea. From this study and the previous report by Thiadens and co-workers 14 , 16 different pathogenic mutations in PDE6C are known to date Fig.
This includes nine protein truncation mutations three nonsense mutations, one frame-shift mutation and five splice site mutation producing aberrant transcripts with altered reading frame , but also seven missense mutations. Two mutations c. RW were found in exon 1, and c.
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RW localizes in the GAFa domain. The c. YN mutation in exon 6 and the c. PL mutation in exon 9 are situated in the second regulatory GAFb domain, while the c. MV mutation in exon 10 is closely behind that.
HL in exon 14 and c. Except for the c. R29W mutation, which has been found in this study as well as in the study of Thiadens and co-workers 14 , all other mutations were only detected in single families. Currently our cohort comprises independent patients and families with a clinical diagnosis of autosomal recessive ACHM. In this paper we compiled all data of our study on PDE6C mutations including new mutations and a complete mutation spectrum, the prevalence of PDE6C mutations in our cohort of independent ACHM patients and families, the clinical phenotype and a detailed functional characterization of PDE6C missense mutations using purified recombinant protein.
For the latter, we investigated two novel PDE6C missense mutations p. PL as well as four previously described amino acid substitutions p. YN, p. HL and p. Up to now, no disease-associated PDE6C mutation had been functionally characterized in detail, leaving uncertainty about the pathogenicity of these missense mutations.
The results of our functional analyses now confirm that all six missense mutations are in fact pathogenic. Four mutations p. HL showed highly significant reduction in PDE activity, to almost baseline levels, and are unlikely to mediate any cone function under physiological conditions. The missense mutation p. R29W was observed in one ACHM family in our study and has also been reported by Thiadens and co-workers, in this case in homozygous state For this mutant, we observed a complete loss of enzymatic function.
In previous studies it has been shown that dimerization of PDE6 is mediated by multiple regions in the N-terminal domain We therefore reason that the function loss of the p.