Arachidonic acid binds to apolipoprotein D: implications for the protein's function

FEBS Letters

Sawyer, Lindsay²  Morais Cabral, João H.²  López-Otin, Carlos¹  López-Boado, Yolanda S.¹  Sánchez, Luis M.¹  Atkins, Gordon L.² 

[1] Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain;Edinburgh Centre for Molecular Recognition and the Department of Biochemistry, University of Edinburgh, Hugh Robson Building, George Square, Edinburgh EH8 9XD, Scotland, UK

关键词: Apolipoprotein D;    Lipocalin;    Arachidonic acid;   

DOI  :  10.1016/0014-5793(95)00484-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The lipocalin apolipoprotein D (ApoD) is associated in human plasma with lecithin-cholesterol acyl transferase. It has also been found in high concentration in the fluid of gross cystic disease of the mammary gland. Using protein fluorescence quenching, it is shown that ApoD binds arachidonic acid (K _aof 1.6 × 10⁸M⁻¹) and as previously known progesterone (K _aof 2.5 × 10⁶M⁻¹), but neither cholesterol nor any of the other prostanoid molecules examined had measurable affinity. This specific binding of arachidonate, also observable directly, suggests a role for ApoD in the mobilisation of Arachidonic acid, and hence prostaglandin synthesis.

【 授权许可】

Unknown