Functional expression of the guinea pig 11b-hydroxylase in cos-1 cells

Hannes E. Bülow; Katharina Möbius; Volker Bähr; Rita Bernhardt

doi:10.1080/07435809609043734

Functional expression of the guinea pig 11b-hydroxylase in cos-1 cells

Hannes E. Bülow, Katharina Möbius, Volker Bähr, Rita Bernhardt

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

2 Scopus citations

Abstract

We expressed a guinea pig 11β-hydroxylase cDNA (1) in COS-1 cells. In order to find the optimal expression system we compared three expression plasmids, each driven by a different promoter. Although promoters exhibited different transcriptional activities this did not result in different enzymatic activities. Upon cotransfection with bovine adrenodoxin a 5-fold increase of enzyme activity was achieved. A comparison with the bovine 11β- hydroxylase clearly demonstrated that the guinea pig enzyme was not able to produce significant amounts of 18-hydroxylated and 18-oxidized products from deoxycorticosterone under the experimental conditions used.

Original language	English (US)
Pages (from-to)	479-484
Number of pages	6
Journal	Endocrine Research
Volume	22
Issue number	4
DOIs	https://doi.org/10.1080/07435809609043734
State	Published - 1996
Externally published	Yes

ASJC Scopus subject areas

Endocrinology

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10.1080/07435809609043734

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title = "Functional expression of the guinea pig 11b-hydroxylase in cos-1 cells",

abstract = "We expressed a guinea pig 11β-hydroxylase cDNA (1) in COS-1 cells. In order to find the optimal expression system we compared three expression plasmids, each driven by a different promoter. Although promoters exhibited different transcriptional activities this did not result in different enzymatic activities. Upon cotransfection with bovine adrenodoxin a 5-fold increase of enzyme activity was achieved. A comparison with the bovine 11β- hydroxylase clearly demonstrated that the guinea pig enzyme was not able to produce significant amounts of 18-hydroxylated and 18-oxidized products from deoxycorticosterone under the experimental conditions used.",

author = "B{\"u}low, {Hannes E.} and Katharina M{\"o}bius and Volker B{\"a}hr and Rita Bernhardt",

note = "Funding Information: We thank Dr. K. Denner and B. Bijttner for helphl discussions and valuable advice. The expression plasmid pBAdx 4 was kindly provided by Dr. M. R. Waterman. This work was supported by the DFG grant Be 134316-1,",

year = "1996",

doi = "10.1080/07435809609043734",

language = "English (US)",

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T1 - Functional expression of the guinea pig 11b-hydroxylase in cos-1 cells

AU - Bülow, Hannes E.

AU - Möbius, Katharina

AU - Bähr, Volker

AU - Bernhardt, Rita

N1 - Funding Information: We thank Dr. K. Denner and B. Bijttner for helphl discussions and valuable advice. The expression plasmid pBAdx 4 was kindly provided by Dr. M. R. Waterman. This work was supported by the DFG grant Be 134316-1,

PY - 1996

Y1 - 1996

N2 - We expressed a guinea pig 11β-hydroxylase cDNA (1) in COS-1 cells. In order to find the optimal expression system we compared three expression plasmids, each driven by a different promoter. Although promoters exhibited different transcriptional activities this did not result in different enzymatic activities. Upon cotransfection with bovine adrenodoxin a 5-fold increase of enzyme activity was achieved. A comparison with the bovine 11β- hydroxylase clearly demonstrated that the guinea pig enzyme was not able to produce significant amounts of 18-hydroxylated and 18-oxidized products from deoxycorticosterone under the experimental conditions used.

AB - We expressed a guinea pig 11β-hydroxylase cDNA (1) in COS-1 cells. In order to find the optimal expression system we compared three expression plasmids, each driven by a different promoter. Although promoters exhibited different transcriptional activities this did not result in different enzymatic activities. Upon cotransfection with bovine adrenodoxin a 5-fold increase of enzyme activity was achieved. A comparison with the bovine 11β- hydroxylase clearly demonstrated that the guinea pig enzyme was not able to produce significant amounts of 18-hydroxylated and 18-oxidized products from deoxycorticosterone under the experimental conditions used.

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Functional expression of the guinea pig 11b-hydroxylase in cos-1 cells

Abstract

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