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大学・研究所にある論文を検索できる 「Transforming growth factor-β1で誘導されるActin alpha2, smooth muscleは、Smad2/3経路を介してヒト歯根膜細胞のコラーゲン産生を制御する」の論文概要。リケラボ論文検索は、全国の大学リポジトリにある学位論文・教授論文を一括検索できる論文検索サービスです。

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Transforming growth factor-β1で誘導されるActin alpha2, smooth muscleは、Smad2/3経路を介してヒト歯根膜細胞のコラーゲン産生を制御する

ファカタバ, ナーティ FAKATAVA, NAATI 九州大学

2023.03.20

概要

九州大学学術情報リポジトリ
Kyushu University Institutional Repository

Actin alpha 2, smooth muscle, a transforming
growth factor-β1-induced factor, regulates
collagen production in human periodontal
ligament cells via Smad2/3 pathway
ファカタバ, ナーティ

https://hdl.handle.net/2324/6787530
出版情報:九州大学, 2022, 博士(歯学), 課程博士
バージョン:
権利関係:(c)2022 Association for Dental Sciences of the Republic of China. Publishing
services by Elsevier B.V. This is an open access article under the CC BY-NC-ND license.

(様式3)





:Fakatava Naati

論 文 名 :Actin alpha 2, smooth muscle, a transforming growth factor-β1-induced factor,
regulates collagen production in human periodontal ligament cells via Smad2/3 pathway
( Transforming growth factor-β1 で誘導される Actin alpha2, smooth muscle は、
Smad2/3 経路を介してヒト歯根膜細胞のコラーゲン産生を制御する )





:甲















Actin alpha 2, smooth muscle (ACTA2) is an actin isoform that forms the cytoskeleton. Actin
plays a crucial role in numerous cellular functions. ACTA2 is a marker of functional
periodontal ligament (PDL) fibroblasts and is upregulated by transforming growth factor-β1
(TGF-β1); however, the underlying function of ACTA2 in PDL tissue is unknown. We aimed to
examine the localization and potential function of ACTA2 in PDL tissues and cells.
In

this

research,

RNA expression

was

determined

using

semi-quantitative

reverse

transcription–polymerase chain reaction (RT-PCR) and quantitative RT-PCR. Protein
expression was determined using immunofluorescence staining and western blot analysis.
Small interfering RNA (siRNA) was used for knockdown assay to examine the effect of ACTA2
in human periodontal ligament cells. Cell proliferation was determined using WST-1 assay and
migration was determined using cell migration assay. Soluble and insoluble collagen
production was examined using the Sircol collagen assay and picrosirius red staining,
respectively.
From the results, ACTA2 expression was observed in human primary PDL cells and PDL cell
line, 2-23 cells. 2-23 cells treated with scramble siRNA exhibited a fibroblast-like morphology
with a spindle-shaped cell form, while 2-23 cells treated with ACTA2 siRNA showed round
appearance. ACTA2 knockdown also significantly suppressed the proliferation and migration
of 2-23 cells. TGF-β1 upregulated ACTA2, collagen type I alpha1 chain (COL1A1), periostin
(POSTN), and fibrillin-I (FBN1) expression and soluble and insoluble collagen production in
2-23 cells. However, ACTA2 depletion by siRNA strongly suppressed PDL-related gene
expression

and

soluble

and

insoluble

collagen

production

compared

with

those

of

TGF-β1–stimulated control cells. Furthermore, ACTA2 knockdown significantly suppressed
the phosphorylation of Smad2 and Smad3.
In summary, ACTA2 is involved in the cell morphology, proliferation, and migration process in
PDL cell. ACTA2 also plays a crucial role in PDL-related marker expression and collagen
production via Smad2/3 phosphorylation. These results suggest that ACTA2 may be a critical
factor involved in homeostatic maintenance of PDL tissue.

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