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Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells

Glycerophospholipids have important structural and functional roles in cells and are the main components of cellular membranes. Glycerophospholipids are formed via the de novo pathway (Kennedy pathway) and are subsequently matured in the remodeling pathway (Lands’ cycle). Lands’ cycle consists of tw...

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Autores principales: Tabe, Shirou, Hikiji, Hisako, Ariyoshi, Wataru, Hashidate-Yoshida, Tomomi, Shindou, Hideo, Shimizu, Takao, Okinaga, Toshinori, Seta, Yuji, Tominaga, Kazuhiro, Nishihara, Tatsuji
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5711957/
https://www.ncbi.nlm.nih.gov/pubmed/29196633
http://dx.doi.org/10.1038/s41598-017-16902-4
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author Tabe, Shirou
Hikiji, Hisako
Ariyoshi, Wataru
Hashidate-Yoshida, Tomomi
Shindou, Hideo
Shimizu, Takao
Okinaga, Toshinori
Seta, Yuji
Tominaga, Kazuhiro
Nishihara, Tatsuji
author_facet Tabe, Shirou
Hikiji, Hisako
Ariyoshi, Wataru
Hashidate-Yoshida, Tomomi
Shindou, Hideo
Shimizu, Takao
Okinaga, Toshinori
Seta, Yuji
Tominaga, Kazuhiro
Nishihara, Tatsuji
author_sort Tabe, Shirou
collection PubMed
description Glycerophospholipids have important structural and functional roles in cells and are the main components of cellular membranes. Glycerophospholipids are formed via the de novo pathway (Kennedy pathway) and are subsequently matured in the remodeling pathway (Lands’ cycle). Lands’ cycle consists of two steps: deacylation of phospholipids by phospholipases A(2) and reacylation of lysophospholipids by lysophospholipid acyltransferases (LPLATs). LPLATs play key roles in the maturation and maintenance of the fatty acid composition of biomembranes, and cell differentiation. We examined whether LPLATs are involved in chondrogenic differentiation of ATDC5 cells, which can differentiate into chondrocytes. Lysophosphatidylcholine acyltransferase 4 (LPCAT4) mRNA expression and LPCAT enzymatic activity towards 18:1-, 18:2-, 20:4-, and 22:6-CoA increased in the late stage of chondrogenic differentiation, when mineralization occurred. LPCAT4 knockdown decreased mRNA and protein levels of chondrogenic markers as well as Alcian blue staining intensity and alkaline phosphatase activity in ATDC5 cells. These results suggest that LPCAT4 plays important roles during the transition of chondrocytes into hypertrophic chondrocytes and/or a mineralized phenotype.
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spelling pubmed-57119572017-12-06 Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells Tabe, Shirou Hikiji, Hisako Ariyoshi, Wataru Hashidate-Yoshida, Tomomi Shindou, Hideo Shimizu, Takao Okinaga, Toshinori Seta, Yuji Tominaga, Kazuhiro Nishihara, Tatsuji Sci Rep Article Glycerophospholipids have important structural and functional roles in cells and are the main components of cellular membranes. Glycerophospholipids are formed via the de novo pathway (Kennedy pathway) and are subsequently matured in the remodeling pathway (Lands’ cycle). Lands’ cycle consists of two steps: deacylation of phospholipids by phospholipases A(2) and reacylation of lysophospholipids by lysophospholipid acyltransferases (LPLATs). LPLATs play key roles in the maturation and maintenance of the fatty acid composition of biomembranes, and cell differentiation. We examined whether LPLATs are involved in chondrogenic differentiation of ATDC5 cells, which can differentiate into chondrocytes. Lysophosphatidylcholine acyltransferase 4 (LPCAT4) mRNA expression and LPCAT enzymatic activity towards 18:1-, 18:2-, 20:4-, and 22:6-CoA increased in the late stage of chondrogenic differentiation, when mineralization occurred. LPCAT4 knockdown decreased mRNA and protein levels of chondrogenic markers as well as Alcian blue staining intensity and alkaline phosphatase activity in ATDC5 cells. These results suggest that LPCAT4 plays important roles during the transition of chondrocytes into hypertrophic chondrocytes and/or a mineralized phenotype. Nature Publishing Group UK 2017-12-01 /pmc/articles/PMC5711957/ /pubmed/29196633 http://dx.doi.org/10.1038/s41598-017-16902-4 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Tabe, Shirou
Hikiji, Hisako
Ariyoshi, Wataru
Hashidate-Yoshida, Tomomi
Shindou, Hideo
Shimizu, Takao
Okinaga, Toshinori
Seta, Yuji
Tominaga, Kazuhiro
Nishihara, Tatsuji
Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title_full Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title_fullStr Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title_full_unstemmed Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title_short Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of ATDC5 cells
title_sort lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic differentiation of atdc5 cells
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5711957/
https://www.ncbi.nlm.nih.gov/pubmed/29196633
http://dx.doi.org/10.1038/s41598-017-16902-4
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