Leukotriene-C4 synthase, a critical enzyme in the activation of store-independent Orai1/Orai3 channels, is required for neointimal hyperplasia

Wei Zhang, Xuexin Zhang, José C. González-Cobos, Judith A. Stolwijk, Khalid Matrougui, Mohamed Trebak

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Background: LTC4S is required for Orai1/Orai3 LRC channel activation. However, the role of LTC4S in neointimal hyperplasia is unknown. Results: LTC4S knockdown inhibited neointimal hyperplasia. Akt phosphorylation was decreased in injured arteries, and knockdown of Orai3 or LTC4S restored Akt phosphorylation. Conclusion: LTC4S is required for neointimal hyperplasia. Significance: LTC4S is a potential therapeutic target for vascular occlusive diseases.

Original languageEnglish (US)
Pages (from-to)5015-5027
Number of pages13
JournalJournal of Biological Chemistry
Volume290
Issue number8
DOIs
StatePublished - Feb 20 2015

Fingerprint

Phosphorylation
Enzyme Activation
Hyperplasia
Chemical activation
Enzymes
Vascular Diseases
Arteries
leukotriene-C4 synthase
Therapeutics

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{2b15a7e646404112965692158fff9d15,
title = "Leukotriene-C4 synthase, a critical enzyme in the activation of store-independent Orai1/Orai3 channels, is required for neointimal hyperplasia",
abstract = "Background: LTC4S is required for Orai1/Orai3 LRC channel activation. However, the role of LTC4S in neointimal hyperplasia is unknown. Results: LTC4S knockdown inhibited neointimal hyperplasia. Akt phosphorylation was decreased in injured arteries, and knockdown of Orai3 or LTC4S restored Akt phosphorylation. Conclusion: LTC4S is required for neointimal hyperplasia. Significance: LTC4S is a potential therapeutic target for vascular occlusive diseases.",
author = "Wei Zhang and Xuexin Zhang and Gonz{\'a}lez-Cobos, {Jos{\'e} C.} and Stolwijk, {Judith A.} and Khalid Matrougui and Mohamed Trebak",
year = "2015",
month = "2",
day = "20",
doi = "10.1074/jbc.M114.625822",
language = "English (US)",
volume = "290",
pages = "5015--5027",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "8",

}

Leukotriene-C4 synthase, a critical enzyme in the activation of store-independent Orai1/Orai3 channels, is required for neointimal hyperplasia. / Zhang, Wei; Zhang, Xuexin; González-Cobos, José C.; Stolwijk, Judith A.; Matrougui, Khalid; Trebak, Mohamed.

In: Journal of Biological Chemistry, Vol. 290, No. 8, 20.02.2015, p. 5015-5027.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Leukotriene-C4 synthase, a critical enzyme in the activation of store-independent Orai1/Orai3 channels, is required for neointimal hyperplasia

AU - Zhang, Wei

AU - Zhang, Xuexin

AU - González-Cobos, José C.

AU - Stolwijk, Judith A.

AU - Matrougui, Khalid

AU - Trebak, Mohamed

PY - 2015/2/20

Y1 - 2015/2/20

N2 - Background: LTC4S is required for Orai1/Orai3 LRC channel activation. However, the role of LTC4S in neointimal hyperplasia is unknown. Results: LTC4S knockdown inhibited neointimal hyperplasia. Akt phosphorylation was decreased in injured arteries, and knockdown of Orai3 or LTC4S restored Akt phosphorylation. Conclusion: LTC4S is required for neointimal hyperplasia. Significance: LTC4S is a potential therapeutic target for vascular occlusive diseases.

AB - Background: LTC4S is required for Orai1/Orai3 LRC channel activation. However, the role of LTC4S in neointimal hyperplasia is unknown. Results: LTC4S knockdown inhibited neointimal hyperplasia. Akt phosphorylation was decreased in injured arteries, and knockdown of Orai3 or LTC4S restored Akt phosphorylation. Conclusion: LTC4S is required for neointimal hyperplasia. Significance: LTC4S is a potential therapeutic target for vascular occlusive diseases.

UR - http://www.scopus.com/inward/record.url?scp=84929119504&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84929119504&partnerID=8YFLogxK

U2 - 10.1074/jbc.M114.625822

DO - 10.1074/jbc.M114.625822

M3 - Article

C2 - 25540197

AN - SCOPUS:84929119504

VL - 290

SP - 5015

EP - 5027

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 8

ER -