Characterization and optimization of vascular endothelial growth factor165 (rhVEGF165) expression in Escherichia coli

W. Kang; S. Kim; S. Lee; E. Jeon; Y. Lee; Y. R. Yun; C. K. Suh; H. W. Kim; J. H. Jang

doi:10.1016/j.pep.2012.10.004

Characterization and optimization of vascular endothelial growth factor₁₆₅ (rhVEGF₁₆₅) expression in Escherichia coli

W. Kang, S. Kim, S. Lee, E. Jeon, Y. Lee, Y. R. Yun, C. K. Suh, H. W. Kim, J. H. Jang

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

13 Scopus citations

Abstract

Vascular endothelial growth factors₁₆₅ (VEGF₁₆₅) is the most potent and widely used pro-angiogenic factor. Here we determined optimal culture condition of recombinant human VEGF₁₆₅ (rhVEGF₁₆₅) in Escherichia coli (E. coli). rhVEGF₁₆₅ expression was the highest in 0.25% of L-arabinose induction concentration, at 20 °C induction temperature, and for 5 h induction time under the control of araBAD promoter using pBADHisA vector. In biological activity test, rhVEGF₁₆₅ significantly increased the proliferative activity of CPAE cells (p < 0.001) and upregulated the expressions of endothelial cell growth-related genes, such as platelet endothelial cell adhesion molecule (PECAM-1), endothelial-specific receptor tyrosine kinase (TEK), kinase insert domain protein receptor (KDR), and tyrosine kinase with immunoglobulin-like and EGF-like domains 1 (TIE1) in calf pulmonary artery endothelial (CPAE) cells.

Original language	English
Pages (from-to)	55-60
Number of pages	6
Journal	Protein Expression and Purification
Volume	87
Issue number	2
DOIs	https://doi.org/10.1016/j.pep.2012.10.004
State	Published - Feb 2013

Keywords

Calf pulmonary artery endothelial cell
Cell proliferative activity
Gene expression
Protein expression
Vascular endothelial growth factor

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10.1016/j.pep.2012.10.004

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title = "Characterization and optimization of vascular endothelial growth factor165 (rhVEGF165) expression in Escherichia coli",

abstract = "Vascular endothelial growth factors165 (VEGF165) is the most potent and widely used pro-angiogenic factor. Here we determined optimal culture condition of recombinant human VEGF165 (rhVEGF165) in Escherichia coli (E. coli). rhVEGF165 expression was the highest in 0.25% of L-arabinose induction concentration, at 20 °C induction temperature, and for 5 h induction time under the control of araBAD promoter using pBADHisA vector. In biological activity test, rhVEGF165 significantly increased the proliferative activity of CPAE cells (p < 0.001) and upregulated the expressions of endothelial cell growth-related genes, such as platelet endothelial cell adhesion molecule (PECAM-1), endothelial-specific receptor tyrosine kinase (TEK), kinase insert domain protein receptor (KDR), and tyrosine kinase with immunoglobulin-like and EGF-like domains 1 (TIE1) in calf pulmonary artery endothelial (CPAE) cells.",

keywords = "Calf pulmonary artery endothelial cell, Cell proliferative activity, Gene expression, Protein expression, Vascular endothelial growth factor",

author = "W. Kang and S. Kim and S. Lee and E. Jeon and Y. Lee and Yun, {Y. R.} and Suh, {C. K.} and Kim, {H. W.} and Jang, {J. H.}",

note = "Publisher Copyright: {\textcopyright} 2012 Elsevier Inc.",

year = "2013",

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doi = "10.1016/j.pep.2012.10.004",

language = "English",

volume = "87",

pages = "55--60",

journal = "Protein Expression and Purification",

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T1 - Characterization and optimization of vascular endothelial growth factor165 (rhVEGF165) expression in Escherichia coli

AU - Kang, W.

AU - Kim, S.

AU - Lee, S.

AU - Jeon, E.

AU - Lee, Y.

AU - Yun, Y. R.

AU - Suh, C. K.

AU - Kim, H. W.

AU - Jang, J. H.

PY - 2013/2

Y1 - 2013/2

N2 - Vascular endothelial growth factors165 (VEGF165) is the most potent and widely used pro-angiogenic factor. Here we determined optimal culture condition of recombinant human VEGF165 (rhVEGF165) in Escherichia coli (E. coli). rhVEGF165 expression was the highest in 0.25% of L-arabinose induction concentration, at 20 °C induction temperature, and for 5 h induction time under the control of araBAD promoter using pBADHisA vector. In biological activity test, rhVEGF165 significantly increased the proliferative activity of CPAE cells (p < 0.001) and upregulated the expressions of endothelial cell growth-related genes, such as platelet endothelial cell adhesion molecule (PECAM-1), endothelial-specific receptor tyrosine kinase (TEK), kinase insert domain protein receptor (KDR), and tyrosine kinase with immunoglobulin-like and EGF-like domains 1 (TIE1) in calf pulmonary artery endothelial (CPAE) cells.

AB - Vascular endothelial growth factors165 (VEGF165) is the most potent and widely used pro-angiogenic factor. Here we determined optimal culture condition of recombinant human VEGF165 (rhVEGF165) in Escherichia coli (E. coli). rhVEGF165 expression was the highest in 0.25% of L-arabinose induction concentration, at 20 °C induction temperature, and for 5 h induction time under the control of araBAD promoter using pBADHisA vector. In biological activity test, rhVEGF165 significantly increased the proliferative activity of CPAE cells (p < 0.001) and upregulated the expressions of endothelial cell growth-related genes, such as platelet endothelial cell adhesion molecule (PECAM-1), endothelial-specific receptor tyrosine kinase (TEK), kinase insert domain protein receptor (KDR), and tyrosine kinase with immunoglobulin-like and EGF-like domains 1 (TIE1) in calf pulmonary artery endothelial (CPAE) cells.

KW - Calf pulmonary artery endothelial cell

KW - Cell proliferative activity

KW - Gene expression

KW - Protein expression

KW - Vascular endothelial growth factor

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SN - 1046-5928

VL - 87

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JO - Protein Expression and Purification

JF - Protein Expression and Purification

IS - 2

ER -

Characterization and optimization of vascular endothelial growth factor₁₆₅ (rhVEGF₁₆₅) expression in Escherichia coli

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Keywords

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