A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells

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URI http://shark.lib.kagawa-u.ac.jp/kuir/metadata/28490
Title
A quantitative study on splice variants of N-acylethanolamine acid amidase in human prostate cancer cells and other cells
File
Description

N-Acylethanolamine acid amidase (NAAA) is a lysosomal enzyme, hydrolyzing various bioactive N-acylethanolamines with a preference for palmitoylethanolamide. Human NAAA mRNA was previously reported to consist of multiple 3'-end splice variants. However, their tissue distributions and roles have not been examined yet. In the present study, we first identified four major splice variants (tentatively referred to as a1, a2, b2, and c2) in a human prostate cancer cell line LNCaP, which were composed of exons 1-11, exons 1-10 and 12, exons 1-9 and 12, and exons 1-8 and 12, respectively. We next developed quantitative polymerase chain reaction methods to individually quantify these NAAA variants as well as collectively measure all the variants. Among various human prostate cancer cells, the total levels of NAAA mRNAs in androgen-sensitive cells like LNCaP were higher than those in androgen-insensitive cells. In all of these prostate cells and other human cells, variants a1 and b2 showed the highest and lowest expression levels, respectively, among the four variants. Interestingly, ratios of the four variants were different by cell type. Variants a1 and a2 encoded the same full-length NAAA protein, which was catalytically active, while b2 and c2 were translated to C-terminally truncated proteins. As expressed in HEK293 cells these truncated forms were detected as catalytically inactive precursor proteins, but not as mature forms. These results revealed wide distribution of multiple variants of NAAA mRNA in various human cells and suggested that the proteins from some variants are catalytically inactive.

Author
著者 佐倉 雄馬
著者(ヨミ) サクラ ユウマ
著者(別表記) Sakura Yuma
Publication Title
Biochimica et Biophysica Acta
Volume
1861
Issue
12
Start Page
1951
End Page
1958
Publisher
Elsevier
Published Date
2016-10-05
ISSN
0006-3002
PMID
27693242
DOI
10.1016/j.bbalip.2016.09.018
Resource Type
Thesis or Dissertation
Language
eng
Relation
出版社版DOIリンク(URL) : https://doi.org/10.1016/j.bbalip.2016.09.018
Rights
Elsevier Japanより、機関リポジトリでの公開可能確認済み。エンバーゴ期間満了。 / From Elsevier Japan, publication possibility confirmed in an institutional repository. The embargo period has expired.
Text Version
ETD
Grant ID
博甲第656号
Grant Date
2017-03-24
Degree Name
博士(医学)
Grantor
香川大学
Set
香川大学
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