Bioengineered chinese hamster ovary cells with golgi-targeted 3-O-sulfotransferase-1 biosynthesize heparan sulfate with an antithrombin-binding site

Payel Datta; Guoyun Li; Bo Yang; Xue Zhao; Jong Youn Baik; Trent R. Gemmill; Susan T. Sharfstein; Robert J. Linhardt

doi:10.1074/jbc.M113.519033

Bioengineered chinese hamster ovary cells with golgi-targeted 3-O-sulfotransferase-1 biosynthesize heparan sulfate with an antithrombin-binding site

Payel Datta, Guoyun Li, Bo Yang, Xue Zhao, Jong Youn Baik, Trent R. Gemmill, Susan T. Sharfstein, Robert J. Linhardt

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

28 Scopus citations

Abstract

Background: CHO-S cells produce non-anticoagulant heparan sulfate (HS) even when transfected with HS3st1 and NDST2. Results: Golgi targeting of HS3st1 alone in bioengineered CHO-S cells afforded anticoagulant HS. Conclusion: Targeting of HS3st1 to the Golgi ensured its action in biosynthesis and modified the action of other biosynthetic enzymes. Significance: Engineering the production of HS and potentially heparin could provide a safer form of this important anticoagulant drug.

Original language	English
Pages (from-to)	37308-37318
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	52
DOIs	https://doi.org/10.1074/jbc.M113.519033
State	Published - 27 Dec 2013
Externally published	Yes

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title = "Bioengineered chinese hamster ovary cells with golgi-targeted 3-O-sulfotransferase-1 biosynthesize heparan sulfate with an antithrombin-binding site",

abstract = "Background: CHO-S cells produce non-anticoagulant heparan sulfate (HS) even when transfected with HS3st1 and NDST2. Results: Golgi targeting of HS3st1 alone in bioengineered CHO-S cells afforded anticoagulant HS. Conclusion: Targeting of HS3st1 to the Golgi ensured its action in biosynthesis and modified the action of other biosynthetic enzymes. Significance: Engineering the production of HS and potentially heparin could provide a safer form of this important anticoagulant drug.",

author = "Payel Datta and Guoyun Li and Bo Yang and Xue Zhao and Baik, {Jong Youn} and Gemmill, {Trent R.} and Sharfstein, {Susan T.} and Linhardt, {Robert J.}",

year = "2013",

month = dec,

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doi = "10.1074/jbc.M113.519033",

language = "English",

volume = "288",

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journal = "Journal of Biological Chemistry",

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T1 - Bioengineered chinese hamster ovary cells with golgi-targeted 3-O-sulfotransferase-1 biosynthesize heparan sulfate with an antithrombin-binding site

AU - Datta, Payel

AU - Li, Guoyun

AU - Yang, Bo

AU - Zhao, Xue

AU - Baik, Jong Youn

AU - Gemmill, Trent R.

AU - Sharfstein, Susan T.

AU - Linhardt, Robert J.

PY - 2013/12/27

Y1 - 2013/12/27

N2 - Background: CHO-S cells produce non-anticoagulant heparan sulfate (HS) even when transfected with HS3st1 and NDST2. Results: Golgi targeting of HS3st1 alone in bioengineered CHO-S cells afforded anticoagulant HS. Conclusion: Targeting of HS3st1 to the Golgi ensured its action in biosynthesis and modified the action of other biosynthetic enzymes. Significance: Engineering the production of HS and potentially heparin could provide a safer form of this important anticoagulant drug.

AB - Background: CHO-S cells produce non-anticoagulant heparan sulfate (HS) even when transfected with HS3st1 and NDST2. Results: Golgi targeting of HS3st1 alone in bioengineered CHO-S cells afforded anticoagulant HS. Conclusion: Targeting of HS3st1 to the Golgi ensured its action in biosynthesis and modified the action of other biosynthetic enzymes. Significance: Engineering the production of HS and potentially heparin could provide a safer form of this important anticoagulant drug.

UR - http://www.scopus.com/inward/record.url?scp=84891383477&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.519033

DO - 10.1074/jbc.M113.519033

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SN - 0021-9258

VL - 288

SP - 37308

EP - 37318

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 52

ER -

Bioengineered chinese hamster ovary cells with golgi-targeted 3-O-sulfotransferase-1 biosynthesize heparan sulfate with an antithrombin-binding site

Abstract

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