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

1995/06/05 by João H. Morais‐Cabral, Gordon L. Atkins, Luis Sánchez‐Pulido +3 · 19 citations
Biochemistry, Genetics and Molecular Biology · Medicine · Chemistry · #Protein Interaction Studies and Fluorescence Analysis #Drug Transport and Resistance Mechanisms #S100 Proteins and Annexins #Arachidonic acid #Lipocalin #Apolipoprotein B #Chemistry #Cholesterol #Prostaglandin #Biochemistry #Lecithin #Internal medicine #Endocrinology #Biology #Enzyme #Medicine

paper · doi:10.1016/0014-5793(95)00484-q

openalex publication_date 1995/06/05 · openalex created_date 2025/10/10 · openalex updated_date 2026/06/23

Abstract

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 (Ka of 1.6 x 10(8) M-1) and as previously known progesterone (Ka of 2.5 x 10(6) M-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.

Citations

• Binding properties of Progesterone-Binding Cyst Protein, PBCP
• Apolipoprotein D transcription occurs specifically in nonproliferating quiescent and senescent fibroblast cultures

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