O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2

Sun Hee Kim; Yun Hee Kim; Minseok Song; Sang Hee An; Ha Young Byun; Kyun Heo; Seyoung Lim; Young Seok Oh; Sung Ho Ryu; Pann Ghill Suh

doi:10.1016/j.bbrc.2007.07.149

O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2

Sun Hee Kim, Yun Hee Kim, Minseok Song, Sang Hee An, Ha Young Byun, Kyun Heo, Seyoung Lim, Young Seok Oh, Sung Ho Ryu, Pann Ghill Suh

Department of Brain Sciences

Research output: Contribution to journal › Article › peer-review

36 Scopus citations

Abstract

O-Linked β-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction. Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation. Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts. In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin. By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc. Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin. Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.

Original language	English
Pages (from-to)	325-329
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	362
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2007.07.149
State	Published - 19 Oct 2007

Bibliographical note

Funding Information:
We thank Dr. Franceschi at University of Michigan and Dr. Bae at Chungbuk National University for providing plasmids and Dr. Gerald Hart at Johns Hopkins University School of Medicine for the kind gift of CTD 110.6 antibody. This work was supported by the Next Generation New Technology Development Program (10027891) funded by Ministry of Commerce, Industry and Energy (MOCIE) of South Korea.

Keywords

O-GlcNAc
OSE2
Osteoblast
Osteocalcin
Runx2

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10.1016/j.bbrc.2007.07.149

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title = "O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2",

abstract = "O-Linked β-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction. Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation. Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts. In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin. By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc. Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin. Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.",

keywords = "O-GlcNAc, OSE2, Osteoblast, Osteocalcin, Runx2",

author = "Kim, {Sun Hee} and Kim, {Yun Hee} and Minseok Song and An, {Sang Hee} and Byun, {Ha Young} and Kyun Heo and Seyoung Lim and Oh, {Young Seok} and Ryu, {Sung Ho} and Suh, {Pann Ghill}",

note = "Funding Information: We thank Dr. Franceschi at University of Michigan and Dr. Bae at Chungbuk National University for providing plasmids and Dr. Gerald Hart at Johns Hopkins University School of Medicine for the kind gift of CTD 110.6 antibody. This work was supported by the Next Generation New Technology Development Program (10027891) funded by Ministry of Commerce, Industry and Energy (MOCIE) of South Korea.",

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AU - Kim, Sun Hee

AU - Kim, Yun Hee

AU - Song, Minseok

AU - An, Sang Hee

AU - Byun, Ha Young

AU - Heo, Kyun

AU - Lim, Seyoung

AU - Oh, Young Seok

AU - Ryu, Sung Ho

AU - Suh, Pann Ghill

N1 - Funding Information: We thank Dr. Franceschi at University of Michigan and Dr. Bae at Chungbuk National University for providing plasmids and Dr. Gerald Hart at Johns Hopkins University School of Medicine for the kind gift of CTD 110.6 antibody. This work was supported by the Next Generation New Technology Development Program (10027891) funded by Ministry of Commerce, Industry and Energy (MOCIE) of South Korea.

PY - 2007/10/19

Y1 - 2007/10/19

N2 - O-Linked β-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction. Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation. Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts. In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin. By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc. Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin. Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.

AB - O-Linked β-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction. Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation. Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts. In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin. By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc. Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin. Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.

KW - O-GlcNAc

KW - OSE2

KW - Osteoblast

KW - Osteocalcin

KW - Runx2

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IS - 2

ER -

O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2

Abstract

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Keywords

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