Carboxylesterase3 (Ces3) Interacts with Bone Morphogenetic Protein 11 and Promotes Differentiation of Osteoblasts via Smad1/5/9 Pathway
Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking study to understand the various interacting proteins involved in bone-adipose axis could provide novel targets for drug development. We explored...
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| Published in | Biotechnology and bioprocess engineering Vol. 27; no. 1; pp. 1 - 16 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Seoul
The Korean Society for Biotechnology and Bioengineering
01.02.2022
한국생물공학회 |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking study to understand the various interacting proteins involved in bone-adipose axis could provide novel targets for drug development. We explored the functional role of Ces3 in osteoblasts and mesenchymal stem cells differentiating into osteoblast lineage using
in vitro
models. We also investigated the physiological functions of Ces3 by stable gene knockdown of
Ces3
and exogenous Ces3 induction, and examined the interacting proteins by Co-IP and
in-silico
analysis. Data from our study suggests that
Ces3
is highly expressed in osteoblasts and promotes proliferation of the cells by increasing the expressions of osteogenic marker proteins and genes. For the first time, our mechanistic studies revealed that Ces3 interacts with BMP11 protein for regulation of osteoblast differentiation and activates the ALK2 and BMP type II receptors via Smad 1/5/9 signaling pathways. In addition, we identified the various partner proteins linked to Ces3 and BMP11 which are also involved in the metabolic network of osteoblasts.
In silico
analysis revealed a direct and strong interaction between Ces3 and BMP11 which influences the growth and regulation of osteoblasts. Current data unveiled a hitherto unknown mechanism of Ces3 and BMP11 in the bone-adipose axis, shedding light on Ces3 as a pharmacotherapeutic target to treat metabolic disorders. |
|---|---|
| AbstractList | Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking study to understand the various interacting proteins involved in bone-adipose axis could provide novel targets for drug development. We explored the functional role of Ces3 in osteoblasts and mesenchymal stem cells differentiating into osteoblast lineage using
in vitro
models. We also investigated the physiological functions of Ces3 by stable gene knockdown of
Ces3
and exogenous Ces3 induction, and examined the interacting proteins by Co-IP and
in-silico
analysis. Data from our study suggests that
Ces3
is highly expressed in osteoblasts and promotes proliferation of the cells by increasing the expressions of osteogenic marker proteins and genes. For the first time, our mechanistic studies revealed that Ces3 interacts with BMP11 protein for regulation of osteoblast differentiation and activates the ALK2 and BMP type II receptors via Smad 1/5/9 signaling pathways. In addition, we identified the various partner proteins linked to Ces3 and BMP11 which are also involved in the metabolic network of osteoblasts.
In silico
analysis revealed a direct and strong interaction between Ces3 and BMP11 which influences the growth and regulation of osteoblasts. Current data unveiled a hitherto unknown mechanism of Ces3 and BMP11 in the bone-adipose axis, shedding light on Ces3 as a pharmacotherapeutic target to treat metabolic disorders. Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking study to understand the various interacting proteins involved in bone-adipose axis could provide novel targets for drug development. We explored the functional role of Ces3 in osteoblasts and mesenchymal stem cells differentiating into osteoblast lineage using in vitro models. We also investigated the physiological functions of Ces3 by stable gene knockdown of Ces3 and exogenous Ces3 induction, and examined the interacting proteins by Co-IP and insilico analysis. Data from our study suggests that Ces3 is highly expressed in osteoblasts and promotes proliferation of the cells by increasing the expressions of osteogenic marker proteins and genes. For the first time, our mechanistic studies revealed that Ces3 interacts with BMP11 protein for regulation of osteoblast differentiation and activates the ALK2 and BMP type II receptors via Smad 1/5/9 signaling pathways. In addition, we identified the various partner proteins linked to Ces3 and BMP11 which are also involved in the metabolic network of osteoblasts. In silico analysis revealed a direct and strong interaction between Ces3 and BMP11 which influences the growth and regulation of osteoblasts. Current data unveiled a hitherto unknown mechanism of Ces3 and BMP11 in the bone-adipose axis, shedding light on Ces3 as a pharmacotherapeutic target to treat metabolic disorders. KCI Citation Count: 0 Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking study to understand the various interacting proteins involved in bone-adipose axis could provide novel targets for drug development. We explored the functional role of Ces3 in osteoblasts and mesenchymal stem cells differentiating into osteoblast lineage using in vitro models. We also investigated the physiological functions of Ces3 by stable gene knockdown of Ces3 and exogenous Ces3 induction, and examined the interacting proteins by Co-IP and in-silico analysis. Data from our study suggests that Ces3 is highly expressed in osteoblasts and promotes proliferation of the cells by increasing the expressions of osteogenic marker proteins and genes. For the first time, our mechanistic studies revealed that Ces3 interacts with BMP11 protein for regulation of osteoblast differentiation and activates the ALK2 and BMP type II receptors via Smad 1/5/9 signaling pathways. In addition, we identified the various partner proteins linked to Ces3 and BMP11 which are also involved in the metabolic network of osteoblasts. In silico analysis revealed a direct and strong interaction between Ces3 and BMP11 which influences the growth and regulation of osteoblasts. Current data unveiled a hitherto unknown mechanism of Ces3 and BMP11 in the bone-adipose axis, shedding light on Ces3 as a pharmacotherapeutic target to treat metabolic disorders. |
| Author | Park, Jong Pil Yun, Jong Won Mukherjee, Sulagna |
| Author_xml | – sequence: 1 givenname: Sulagna surname: Mukherjee fullname: Mukherjee, Sulagna organization: Department of Biotechnology, Daegu University – sequence: 2 givenname: Jong Pil surname: Park fullname: Park, Jong Pil organization: Department of Food Science and Technology, Chung-Ang University – sequence: 3 givenname: Jong Won surname: Yun fullname: Yun, Jong Won email: jwyun@daegu.ac.kr organization: Department of Biotechnology, Daegu University |
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| Snippet | Ces3 is a lipolytic enzyme predominantly present in liver and adipocytes, with recent reports of its presence in skeletal muscles, as well. A cross-linking... |
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| SubjectTerms | adipocytes biochemical pathways bioprocessing Biotechnology bone formation bone morphogenetic proteins Chemistry Chemistry and Materials Science computer simulation crosslinking drug development enzymes gene targeting Industrial and Production Engineering liver osteoblasts Research Paper 생물공학 |
| Title | Carboxylesterase3 (Ces3) Interacts with Bone Morphogenetic Protein 11 and Promotes Differentiation of Osteoblasts via Smad1/5/9 Pathway |
| URI | https://link.springer.com/article/10.1007/s12257-021-0133-y https://www.proquest.com/docview/2648856701 https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART002818562 |
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| ispartofPNX | Biotechnology and Bioprocess Engineering, 2022, 27(1), , pp.1-16 |
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