TY - JOUR
T1 - Human retina-specific amine oxidase (RAO)
T2 - cDNA cloning, tissue expression, and chromosomal mapping
AU - Imamura, Yutaka
AU - Kubota, Ryo
AU - Wang, Yimin
AU - Asakawa, Shuichi
AU - Kudoh, Jun
AU - Mashima, Yukihiko
AU - Oguchi, Yoshihisa
AU - Shimizu, Nobuyoshi
N1 - Funding Information:
The authors thank Ms. H. Harigai for her assistance in manuscript preparation. This work was supported in part by Grants in Aid for Creative Basic Research (Human Genome Program), Scienti®c Research on Priority Areas from the Ministry of Education, Science, Sports and Culture of Japan and by funds from the Research Committee on Chorioretinal Degenerations, The Ministry of Health and Welfare of Japan.
PY - 1997/3/1
Y1 - 1997/3/1
N2 - In search of candidate genes for hereditary retinal disease, we have employed a subtractive and differential cDNA cloning strategy and isolated a novel retina-specific cDNA. Nucleotide sequence analysis revealed an open reading frame of 2187 bp, which encodes a 729-amino-acid protein with a calculated molecular mass of 80,644 Da. The putative protein contained a conserved domain of copper amine oxidase, which is found in various species from bacteria to mammals. It showed the highest homology to bovine serum amine oxidase, which is believed to control the level of serum biogenic amines. Northern blot analysis of human adult and fetal tissues revealed that the protein is expressed abundantly and specifically in retina as a 2.7-kb transcript. Thus, we considered this protein a human retina-specific amine oxidase (RAO). The RAO gene (AOC2) was mapped by fluorescence in situ hybridization to human chromosome 17q21. We propose that AOC2 may be a candidate gene for hereditary ocular diseases.
AB - In search of candidate genes for hereditary retinal disease, we have employed a subtractive and differential cDNA cloning strategy and isolated a novel retina-specific cDNA. Nucleotide sequence analysis revealed an open reading frame of 2187 bp, which encodes a 729-amino-acid protein with a calculated molecular mass of 80,644 Da. The putative protein contained a conserved domain of copper amine oxidase, which is found in various species from bacteria to mammals. It showed the highest homology to bovine serum amine oxidase, which is believed to control the level of serum biogenic amines. Northern blot analysis of human adult and fetal tissues revealed that the protein is expressed abundantly and specifically in retina as a 2.7-kb transcript. Thus, we considered this protein a human retina-specific amine oxidase (RAO). The RAO gene (AOC2) was mapped by fluorescence in situ hybridization to human chromosome 17q21. We propose that AOC2 may be a candidate gene for hereditary ocular diseases.
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U2 - 10.1006/geno.1996.4570
DO - 10.1006/geno.1996.4570
M3 - Article
C2 - 9119395
AN - SCOPUS:0031106170
VL - 40
SP - 277
EP - 283
JO - Genomics
JF - Genomics
SN - 0888-7543
IS - 2
ER -
