AMP-activated protein kinase (AMPK) positively regulates osteoblast differentiation via induction of Dlx5-dependent Runx2 expression in MC3T3E1 cells

Jang, Won Gu; Kim, Eun Jung; Lee, Kkot-Nim; Son, Hye-Ju; Koh, Jeong‐Tae

doi:10.1016/j.bbrc.2010.12.099

Cited by 84 publications

(67 citation statements)

References 38 publications

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“…The cells were cultured in ␣-minimal essential medium (Gibco-BRL, Grand Island, NY) supplemented with 10% fetal bovine serum (FBS; GIBCO-BRL) and antibiotics, and incubated at 37°C in a humidified atmosphere containing 5% CO 2 . Transient transfections were performed as described previously (28). For viral infection, the cells were treated with the indicated viruses at the designated multiplicity of infection (m.o.i.)…”

Section: Methodsmentioning

confidence: 99%

Cyclic AMP Response Element-binding Protein H (CREBH) Mediates the Inhibitory Actions of Tumor Necrosis Factor α in Osteoblast Differentiation by Stimulating Smad1 Degradation

Jang

Jeong²,

Kim³

et al. 2015

Journal of Biological Chemistry

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Background: Severe inflammatory reactions delay wound healing of bone. Results: Tumor necrosis factor ␣ (TNF␣) inhibition of osteoblast differentiation is associated with increased cAMP response element-binding protein H (CREBH) and Smurf1 expression. Conclusion: CREBH mediates the inhibitory actions of TNF␣ in bone regeneration. Significance: CREBH is identified as a new mediator of inflammation-dependent bone degradation and a potential therapeutic target.

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Section: Methodsmentioning

confidence: 99%

Cyclic AMP Response Element-binding Protein H (CREBH) Mediates the Inhibitory Actions of Tumor Necrosis Factor α in Osteoblast Differentiation by Stimulating Smad1 Degradation

Jang

Jeong²,

Kim³

et al. 2015

Journal of Biological Chemistry

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“…We previously reported that AMPK activation stimulated the differentiation and mineralization of osteoblasts by enhancing the expression of BMP-2 and endothelial nitric oxide synthase via the inhibition of mevalonate pathway [11][12][13]. Moreover, other researchers also reported that AMPK activation induced calcified nodule formation in primary osteoblasts, whereas AMPK inhibition suppressed the effects of AMPK and osteoblastic differentiation [69,70]. On the other hand, several studies showed that AMPK plays roles in osteoclastogenesis.…”

Section: The Association Between Osteocalcin and Glucose Metabolismmentioning

confidence: 98%

Interaction between bone and glucose metabolism [Review]

Kanazawa

2017

Endocr J

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Abstract.Accumulating evidence has shown that bone and glucose metabolism are closely associated with each other. Since the risk of osteoporotic fractures is increased in patients with diabetes mellitus (DM), osteoporosis is recently recognized as one of diabetic complications, called DM-induced bone fragility. Previous studies showed that collagen cross-links of advanced glycation end products (AGEs) and dysfunctions of osteoblast and osteocyte are involved in DMinduced bone fragility. Circulating levels of AGEs and homocysteine are increased in patients with DM, and they directly impair the functions of osteoblast and osteocyte, resulting in decreased bone formation and bone remodeling. On the other hand, bone is recently recognized as an endocrine organ. Previous studies based on in vitro and animal studies showed that osteocalcin, which is specifically expressed in osteoblasts and secreted into the circulation, may regulate glucose homeostasis. Although several clinical studies reported the relationship between osteocalcin and glucose metabolism, further large-scale and intervention studies are necessary to confirm the beneficial effects of osteocalcin on glucose metabolism in human. It has been shown that adenosine monophosphate-activated protein kinase (AMPK), an intracellular energy sensor, is involved in bone metabolism. Adiponectin and metformin stimulate osteocalcin expression and the differentiation of osteoblasts via AMPK activation. Also, AMPK activation protects against oxidative stress-induced apoptosis of osteocytes. These findings suggest that AMPK in osteoblasts and osteocytes may be a therapeutic target for DM-induced bone fragility.

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“…Regarding the roles of AMPK in osteoblasts, it has been revealed that the activation of AMPK stimulates collagen synthesis and the induction of Runt-related transcription factor 2 expression, and enhances mineralization (25,26). Additionally, AMPK has been reported to have an inhibitory role in palmitate-induced apoptosis (27).…”

Section: Discussionmentioning

confidence: 99%

Possible involvement of AMP-activated protein kinase in PGE1-induced synthesis of osteoprotegerin in osteoblasts

Kainuma

Otsuka

Kuroyanagi

et al. 2016

Experimental and Therapeutic Medicine

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Abstract. AMP-activated protein kinase (AMPK) is firmly established as a central regulator of cellular energy homeostasis. We have previously reported that prostaglandin E 1 (PGE 1 ) stimulates the synthesis of osteoprotegerin through p38 mitogen-activated protein (MAP) kinase and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in osteoblast-like MC3T3-E1 cells. The present study investigated the involvement of AMPK in PGE 1 -induced osteoprotegerin synthesis in MC3T3-E1 cells. The levels of osteoprotegerin were measured using an enzyme-linked immunosorbent assay, while the phosphorylation of AMPK, acetyl-CoA carboxylase, p38 MAP kinase and SAPK/JNK were analyzed by western blotting. In addition, the mRNA expression levels of osteoprotegerin were determined by a reverse transcription-quantitative polymerase chain reaction. It was revealed that PGE 1 significantly induced the phosphorylation of the α and β subunits of AMPK in a time-dependent manner (P<0.05). In addition, acetyl-CoA carboxylase, a direct substrate of AMPK, was significantly phosphorylated by PGE 1 (P<0.05). Compound C, an AMPK inhibitor, was revealed to suppress the phosphorylation of acetyl-CoA carboxylase, which significantly reduced the release and mRNA expression levels of PGE 1 -stimulated osteoprotegerin (P<0.05). However, the PGE 1 -induced phosphorylation of p38 MAP kinase and SAPK/JNK were not affected by compound C. The results of the present study indicated that AMPK may positively regulate PGE 1 -stimulated osteoprotegerin synthesis in osteoblasts; thus providing novel insight into the regulatory mechanisms underlying bone metabolism.

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AMP-activated protein kinase (AMPK) positively regulates osteoblast differentiation via induction of Dlx5-dependent Runx2 expression in MC3T3E1 cells

Cited by 84 publications

References 38 publications

Cyclic AMP Response Element-binding Protein H (CREBH) Mediates the Inhibitory Actions of Tumor Necrosis Factor α in Osteoblast Differentiation by Stimulating Smad1 Degradation

Cyclic AMP Response Element-binding Protein H (CREBH) Mediates the Inhibitory Actions of Tumor Necrosis Factor α in Osteoblast Differentiation by Stimulating Smad1 Degradation

Interaction between bone and glucose metabolism [Review]

Possible involvement of AMP-activated protein kinase in PGE1-induced synthesis of osteoprotegerin in osteoblasts

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