Molecular biology of PCSK9: its role in LDL metabolism

被引：470

作者：

Horton, Jay D.

Cohen, Jonathan C.

Hobbs, Helen H.

机构：

[1] Univ Texas, SW Med Ctr, Dept Internal Med, Dallas, TX 75390 USA

[2] Univ Texas, SW Med Ctr, Dept Mol Genet, Dallas, TX 75390 USA

[3] Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2007年 / 32卷 / 02期

关键词：

D O I：

10.1016/j.tibs.2006.12.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Proprotein convertase subtilisin-like kexin type 9 (PCSK9) is a newly discovered serine protease that destroys low density lipoprotein (LDL) receptors in liver and thereby controls the level of LDL in plasma. Mutations that increase PCSK9 activity cause hypercholesterolemia and coronary heart disease (CHD); mutations that inactivate PCSK9 have the opposite effect, lowering LDL levels and reducing CHD. Although the mechanism of PCSK9 action is not yet clear, the protease provides a new therapeutic target to lower plasma levels of LDL and prevent CHD.

引用

页码：71 / 77

页数：7

共 44 条

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