Tissue-specific expression and subcellular localization of ALADIN, the absence of which causes human triple A syndrome

• Published in: Experimental & molecular medicine Vol. 41; no. 6; pp. 381 - 386
• Main Authors: Cho, A-Ri, Yang, Keum-Jin, Bae, Yoonsun, Bahk, Young Yil, Kim, Eunmin, Lee, Hyungnam, Kim, Jeong Ki, Park, Wonsang, Rhim, Hyanshuk, Choi, Soo Young, Imanaka, Tsuneo, Moon, Sungdae, Yoon, Jongbok, Yoon, Sungjoo Kim
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 30-06-2009; Springer Nature B.V; Korean Society of Medical Biochemistry and Molecular Biology; 생화학분자생물학회
• Subjects: Adrenal Insufficiency - genetics; Antibodies - immunology; Biomedical and Life Sciences; Biomedicine; Cloning, Molecular; DNA, Complementary - genetics; Esophageal Achalasia - genetics; Gene Expression Profiling; HeLa Cells; Humans; Lacrimal Apparatus Diseases - genetics; Medical Biochemistry; Molecular Medicine; Mutagenesis, Site-Directed; Nerve Tissue Proteins - analysis; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - immunology; Nuclear Pore - chemistry; Nuclear Pore Complex Proteins - analysis; Nuclear Pore Complex Proteins - genetics; Nuclear Pore Complex Proteins - immunology; Original; RNA, Messenger - analysis; RNA, Messenger - genetics; Stem Cells; Syndrome; Tissue Distribution; 생화학; protein transport; gene expression profiling; AAAS protein, human
• ISSN: 1226-3613; 2092-6413
• DOI: 10.3858/emm.2009.41.6.043

Triple A syndrome is a rare genetic disorder caused by mutations in the achalasia-addisonianism-alacrima syndrome (
AAAS
) gene which encodes a tryptophan aspartic acid (WD) repeat-containing protein named alacrima-achalasia-adrenal insufficiency neurologic disorder (ALADIN). Northern blot analysis shows that the 2.1 kb
AAAS
mRNA is expressed in various tissues with stronger expression in testis and pancreas. We show that human ALADIN is a protein with an apparent molecular weight of 60 kDa, and expressed in the adrenal gland, pituitary gland and pancreas. Furthermore, biochemical analysis using anti-ALADIN antibody supports the previous finding of the localization of ALADIN in the nuclear membrane. The mutations S544G and S544X show that alteration of S544 residue affects correct targeting of ALADIN to the nuclear membrane.