Complementation test of Rpe65 knockout and tvrm148

Investigative Ophthalmology and Visual Science

Volumn 54, Issue 7, 2013, Pages 5111-5122

  Wright, Charles B ^a   Chrenek, Micah A ^a   Foster, Stephanie L ^a   Duncan, Todd ^b   Redmond, T Michael ^b   Pardue, Machelle T ^a,c   Boatright, Jeffrey H ^a   Nickerson, John M ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NATIONAL EYE INSTITUTE   (United States)

^c ATLANTA VA MEDICAL CENTER   (United States)

Author keywords

Mutation; RPE65 Rpe65; Visual cycle

Indexed keywords

RETINOID;

ALLELE; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; COMPUTER PREDICTION; CONTROLLED STUDY; DENSITOMETRY; ELECTRORETINOGRAPHY; GENE; GENE MUTATION; GENETIC COMPLEMENTATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HISTOLOGY; IMMUNOBLOTTING; INHERITANCE; KNOCKOUT GENE; MICROSCOPY; MORPHOMETRICS; MOUSE; NONHUMAN; OPTOKINETIC STIMULATION; PATHOGENICITY; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RPE 65 GENE; TRANSMISSION ELECTRON MICROSCOPY; TVRM 148 GENE; VISUAL ACUITY; VISUAL SYSTEM FUNCTION;

MUTATION; RPE65/RPE65; VISUAL CYCLE;

ALLELES; ANALYSIS OF VARIANCE; ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIS-TRANS-ISOMERASES; DISEASE MODELS, ANIMAL; ELECTRORETINOGRAPHY; GENETIC COMPLEMENTATION TEST; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; MODELS, GENETIC; MUTATION; RETINAL DEGENERATION; RETINOIDS; VISUAL ACUITY;

EID: 84880931014     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.13-12336     Document Type: Article

References (72)

1. Won J, Shi LY, Hicks W, et al. Mouse model resources for vision research. J Ophthalmol. 2011;2011:391384.
2. Redmond TM, Yu S, Lee E, et al. Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Nat Genet. 1998;20:344-351.
3. Kumar P, Henikoff S, Ng PC. Predicting the effects of codingnon-synonymous variants on protein function using the SIFT algorithm. Nat Protoc. 2009;4:1073-1081.
4. Ng PC, Henikoff S. Predicting the effects of amino acid substitutions on protein function. Ann Rev Genomics Hum Genet. 2006;7:61-80.
5. Ng PC, Henikoff S. SIFT: predicting amino acid changes that affect protein function. Nucleic Acids Res. 2003;31:3812- 3814.
6. Ng PC, Henikoff S. Accounting for human polymorphisms predicted to affect protein function. Nucleic Acids Res. 2003; 31:3812-3814.
7. Ng PC, Henikoff S. Predicting deleterious amino acid substitutions. Genome Res. 2001;11:863-874.
8. Adzhubei IA, Schmidt S, Peshkin L, et al. A method and server for predicting damaging missense mutations. Nat Methods. 2010;7:248-249.
9. Ramensky V, Bork P, Sunyaev S. Human non-synonymous SNPs: server and survey. Nucleic Acids Res. 2002;30:3894-3900.
10. Sunyaev SR, Eisenhaber F, Rodchenkov IV, Eisenhaber B, Tumanyan VG, Kuznetsov EN. PSIC: profile extraction from sequence alignments with position-specific counts of independent observations. Protein Eng. 1999;12:387-394.
11. Mi H, Muruganujan A, Thomas PD. PANTHER in 2013: modeling the evolution of gene function, and other gene attributes, in the context of phylogenetic trees. Nucleic Acids Res. 2013;41:D377-D386.
12. Flicek P, Aken BL, Beal K, et al. Ensembl 2008. Nucleic AcidsRes. 2008;36:D707-D714.
13. Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A. ExPASy: The proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res. 2003;31:3784- 3788.
14. Grantham R. Amino acid difference formula to help explain protein evolution. Science. 1974;185:862-864.
15. Pollard KS, Hubisz MJ, Rosenbloom KR, Siepel A. Detection of nonneutral substitution rates on mammalian phylogenies. Genome Res. 2010;20:110-121.
16. Abecasis GR, Auton A, Brooks LD, et al. An integrated map of genetic variation from 1,092 human genomes. Nature. 2012; 491:56-65.
17. Reese MG, Eeckman FH, Kulp D, Haussler D. Improved splice site detection in Genie. J Comput Biol. 1997;4:311-323.
18. Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol. 1990;215:403-410.
19. Tabaska JE, Zhang MQ. Detection of polyadenylation signals in human DNA sequences. Gene. 1999;231:77-86.
20. Ferrer-Costa C, Gelpi JL, Zamakola L, Parraga I, de la Cruz X, Orozco M.PMUT: a web-based tool for the annotation of pathological mutations on proteins. Bioinformatics. 2005;21: 3176-3178.
21. Bromberg Y, Rost B. SNAP: predict effect of non-synonymous polymorphisms on function. Nucleic Acids Res. 2007;35: 3823-3835.
22. Yue P, Li Z, Moult J. Loss of protein structure stability as a major causative factor in monogenic disease. J Mol Biol. 2005; 353:459-473.
23. Yue P, Moult J. Identification and analysis of deleterious human SNPs. J Mol Biol. 2006;356:1263-1274.
24. Yue P, Melamud E, Moult J. SNPs3D: candidate gene and SNP selection for association studies. BMC Bioinformatics. 2006;7: 166.
25. Capriotti E, Calabrese R, Casadio R. Predicting the insurgence of human genetic diseases associated to single point protein mutations with support vector machines and evolutionary information. Bioinformatics. 2006;22:2729-2734.
26. Capriotti E, Fariselli P, Calabrese R, Casadio R. Predicting protein stability changes from sequences using support vector machines. Bioinformatics. 2005;21(suppl 2):ii54-ii58.
27. Capriotti E, Fariselli P, Casadio R. I-Mutant2.0: predicting stability changes upon mutation from the protein sequence or structure. Nucleic Acids Res. 2005;33:W306-W310.
28. Altschul SF, Madden TL, Schaffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997;25:3389-3402.
29. Choi Y, Sims GE, Murphy S, Miller JR, Chan AP. Predicting the functional effect of amino acid substitutions and indels. PloS One. 2012;7:e46688.
30. Chang B, Hawes NL, Pardue MT, et al. Two mouse retinal degenerations caused by missense mutations in the betasubunit of rod cGMP phosphodiesterase gene. Vision Res. 2007;47:624-633.
31. Jablonski MM, Dalke C, Wang X, et al. An ENU-induced mutation in Rs1h causes disruption of retinal structure and function. Mol Vis. 2005;11:569-581.
32. Pardue MT, McCall MA, LaVail MM, Gregg RG, Peachey NS. A naturally occurring mouse model of X-linked congenital stationary night blindness. Invest Ophthalmol Vis Sci. 1998; 39:2443-2449.
33. Pardue MT, Phillips MJ, Yin H, et al. Neuroprotective effect of subretinal implants in the RCS rat. Invest Ophthalmol Vis Sci. 2005;46:674-682.
34. Akula JD, Hansen RM, Martinez-Perez ME, Fulton AB. Rod photoreceptor function predicts blood vessel abnormality in retinopathy of prematurity. Invest Ophthalmol Vis Sci. 2007; 48:4351-4359.
35. Akula JD, Mocko JA, Moskowitz A, Hansen RM, Fulton AB. The oscillatory potentials of the dark-adapted electroretinogram in retinopathy of prematurity. Invest Ophthalmol Vis Sci. 2007; 48:5788-5797.
36. Weymouth AE, Vingrys AJ. Rodent electroretinography: methods for extraction and interpretation of rod and cone responses. Prog Retin Eye Res. 2008;27:1-44.
37. Landers GM, Olson JA. Rapid, simultaneous determination of isomers of retinal, retinal oxime and retinol by highperformance liquid chromatography. J Chromatogr. 1988; 438:383-392.
38. Garwin GG, Saari JC. High-performance liquid chromatography analysis of visual cycle retinoids. Methods Enzymol. 2000; 316:313-324.
39. Douglas RM, Alam NM, Silver BD, McGill TJ, Tschetter WW, Prusky GT. Independent visual threshold measurements in the two eyes of freely moving rats and mice using a virtual-reality optokinetic system. Vis Neurosci. 2005;22:677-684.
40. Prusky GT, Alam NM, Beekman S, Douglas RM. Rapid quantification of adult and developing mouse spatial vision using a virtual optomotor system. Invest Ophthalmol Vis Sci. 2004;45:4611-4616.
41. Carter-Dawson LD, LaVail MM. Rods and cones in the mouse retina. I. Structural analysis using light and electron microscopy. J Comp Neurol. 1979;188:245-262.
42. Seeliger MW, Grimm C, Stahlberg F, et al. New views on RPE65 deficiency: the rod system is the source of vision in a mouse model of Leber congenital amaurosis. Nat Genet. 2001;29:70-74.
43. Pang JJ, Chang B, Hawes NL, et al. Retinal degeneration 12 (rd12): a new, spontaneously arising mouse model for human Leber congenital amaurosis (LCA). Mol Vis. 2005;11:152-162.
44. Samardzija M, von Lintig J, Tanimoto N, et al. R91W mutation in Rpe65 leads to milder early-onset retinal dystrophy due to the generation of low levels of 11-cis-retinal. Hum Mol Genet. 2008;17:281-292.
45. Jacobson SG, Aleman TS, Cideciyan AV, et al. Defining the residual vision in Leber congenital amaurosis caused by RPE65 mutations. Invest Ophthalmol Vis Sci. 2009;50:2368-2375.
46. Cachafeiro M, Bemelmans AP, Canola K, et al. Remaining rod activity mediates visual behavior in adult Rpe65-/- mice. Invest Ophthalmol Vis Sci. 2010;51:6835-6842.
47. Caruso RC, Aleman TS, Cideciyan AV, et al. Retinal disease in Rpe65-deficient mice: comparison to human leber congenital amaurosis due to RPE65 mutations. Invest Ophthalmol Vis Sci. 2010;51:5304-5313.
48. Pasadhika S, Fishman GA, Stone EM, et al. Differential macular morphology in patients with RPE65-, CEP290-, GUCY2D-, and AIPL1-related Leber congenital amaurosis. Invest Ophthalmol Vis Sci. 2010;51:2608-2614.
49. Chen Y, Moiseyev G, Takahashi Y, Ma JX. Impacts of two point mutations of RPE65 from Leber's congenital amaurosis on the stability, subcellular localization and isomerohydrolase activity of RPE65. FEBS Lett. 2006;580:4200-4204.
50. Rohrer B, Lohr HR, Humphries P, Redmond TM, Seeliger MW, Crouch RK. Cone opsin mislocalization in Rpe65-/- mice: a defect that can be corrected by 11-cis retinal. Invest Ophthalmol Vis Sci. 2005;46:3876-3882.
51. Zhang T, Zhang N, Baehr W, Fu Y. Cone opsin determines the time course of cone photoreceptor degeneration in Leber congenital amaurosis. Proc Natl Acad Sci U S A. 2011;108: 8879-8884.
52. Umino Y, Solessio E, Barlow RB. Speed, spatial, and temporal tuning of rod and cone vision in mouse. J Neurosci. 2008;28: 189-198.
53. Ablonczy Z, Crouch RK, Goletz PW, et al. 11-cis-retinal reduces constitutive opsin phosphorylation and improves quantum catch in retinoid-deficient mouse rod photoreceptors. J Biol Chem. 2002;277:40491-40498.
54. Cachafeiro M, Bemelmans A-P, Canola K, et al. Remaining rod activity mediates visual behavior in adult Rpe65-/- mice. Invest Ophthalmol Vis Sci. 2010;51:6835-6842.
55. Tang PH, Wheless L, Crouch RK. Regeneration of photopigment is enhanced in mouse cone photoreceptors expressing RPE65 protein. J Neurosci. 2011;31:10403-10411.
56. Fan J, Rohrer B, Moiseyev G, Ma JX, Crouch RK. Isorhodopsin rather than rhodopsin mediates rod function in RPE65 knockout mice. Proc Natl Acad Sci U S A. 2003;100:13662-13667.
57. Van Hooser JP, Liang Y, Maeda T, et al. Recovery of visual functions in a mouse model of Leber congenital amaurosis. J Biol Chem. 2002;277:19173-19182.
58. Wang JS, Kefalov VJ. The cone-specific visual cycle. Prog Retin Eye Res. 2011;30:115-128.
59. Takahashi Y, Moiseyev G, Chen Y, Nikolaeva O, Ma JX. An alternative isomerohydrolase in the retinal Muller cells of a cone-dominant species. FEBS J. 2011;278:2913-2926.
60. Kaylor JJ, Yuan Q, Cook J, et al. Identification of DES1 as a vitamin A isomerase in Muller glial cells of the retina. Nat Chem Biol. 2013;9:30-36.
61. Kiser PD, Golczak M, Lodowski DT, Chance MR, Palczewski K. Crystal structure of native RPE65, the retinoid isomerase of the visual cycle. Proc Natl Acad Sci U S A. 2009;106:17325- 17330.
62. Golczak M, Kiser PD, Lodowski DT, Maeda A, Palczewski K. Importance of membrane structural integrity for RPE65 retinoid isomerization activity. J Biol Chem. 2010;285:9667- 9682.
63. Kiser PD, Palczewski K. Membrane-binding and enzymatic properties of RPE65. Prog Retin Eye Res. 2010;29:428-442.
64. Kiser PD, Farquhar ER, Shi W, Sui X, Chance MR, Palczewski K. Structure of RPE65 isomerase in a lipidic matrix reveals roles for phospholipids and iron in catalysis. Proc Natl Acad Sci U S A. 2012;109:E2747-E2756.
65. Gu SM, Thompson DA, Srikumari CR, et al. Mutations in RPE65 cause autosomal recessive childhood-onset severe retinal dystrophy. Nat Genet. 1997;17:194-197.
66. Nikolaeva O, Moiseyev G, Rodgers KK, Ma JX. Binding to lipid membrane induces conformational changes in RPE65: implications for its isomerohydrolase activity. Biochem J. 2011;436: 591-597.
67. Marlhens F, Bareil C, Griffoin JM, et al. Mutations in RPE65 cause Leber's congenital amaurosis. Nat Genet. 1997;17:139- 141.
68. Morimura H, Fishman GA, Grover SA, Fulton AB, Berson EL, Dryja TP. Mutations in the RPE65 gene in patients with autosomal recessive retinitis pigmentosa or leber congenital amaurosis. Proc Natl Acad Sci U S A. 1998;95:3088-3093.
69. Philp AR, Jin M, Li S, et al. Predicting the pathogenicity of RPE65 mutations. Hum Mutat. 2009;30:1183-1188.
70. Stone EM. Leber congenital amaurosis - a model for efficient genetic testing of heterogeneous disorders: LXIV Edward Jackson Memorial Lecture. Am J Ophthalmol. 2007;144:791- 811.
71. Sundaresan P, Vijayalakshmi P, Thompson S, Ko AC, Fingert JH, Stone EM. Mutations that are a common cause of Leber congenital amaurosis in northern America are rare in southern India. Mol Vis. 2009;15:1781-1787.
72. Pang J, Boye SE, Lei B, et al. Self-complementary AAV-mediatedgene therapy restores cone function and prevents cone degeneration in two models of Rpe65 deficiency. Gene Ther. 2010;17:815-826.