Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
Structure and Characterization of AAT-1 Isoforms
Eiko MatsudaRay IshizakiTakahiro TairaSanae M. M. Iguchi-ArigaHiroyoshi Ariga
ジャーナル フリー

2005 年 28 巻 5 号 p. 898-901


A novel protein, AAT-1, was identified as a AMY-1-binding protein and three splicing variants of AAT-1, AAT-1α, -β and -γ were identified. The function of AAT-1 is thought to be related to spermatogenesis. In this study, we further identified other splicing isoforms of AAT-1, AAT-1L, AAT-1M and AAT-1S, consisting of 767, 603 and 252 amino acids, respectively. These isoforms were found to use a promoter different from that used by AAT-1α, -β and -γ in the aat-1 gene, which contains 20 exons. Only 60 amino acids in the C-terminal portion of AAT-1 derived from exons 15—17 are common among AAT-1L, AAT-1M, AAT-1S and AAT-1α. While AAT-1α is specifically expressed in the testis, AAT-1L, AAT-1M, AAT-1S were found to be differentially expressed in human tissues. All of the isoforms of AAT-1 were found to bind to and colocalized with AMY-1 in human cells. While AAT-1L and AAT-1M were found to be localized diffusely in the cytoplasm, AAT-1S, like AAT-1α, was found to be localized in the mitochondria-like structure, suggesting different roles of AAT-1 isoforms in cells.

© 2005 The Pharmaceutical Society of Japan
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