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Using protein fluorescence quenching, it is shown that ApoD binds arachidonic acid (<jats:italic>K<\/jats:italic>\n<jats:sub>a<\/jats:sub>of 1.6 \u00d7 10<jats:sup>8<\/jats:sup>M<jats:sup>\u22121<\/jats:sup>) and as previously known progesterone (<jats:italic>K<\/jats:italic>\n<jats:sub>a<\/jats:sub>of 2.5 \u00d7 10<jats:sup>6<\/jats:sup>M<jats:sup>\u22121<\/jats:sup>), 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.<\/jats:p>","DOI":"10.1016\/0014-5793(95)00484-q","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T01:45:07Z","timestamp":1027647907000},"page":"53-56","source":"Crossref","is-referenced-by-count":107,"title":["Arachidonic acid binds to apolipoprotein D: implications for the protein's function"],"prefix":"10.1002","volume":"366","author":[{"given":"Jo\u00e3o H.","family":"Morais Cabral","sequence":"first","affiliation":[]},{"given":"Gordon L.","family":"Atkins","sequence":"additional","affiliation":[]},{"given":"Luis M.","family":"S\u00e1nchez","sequence":"additional","affiliation":[]},{"given":"Yolanda S.","family":"L\u00f3pez-Boado","sequence":"additional","affiliation":[]},{"given":"Carlos","family":"L\u00f3pez-Otin","sequence":"additional","affiliation":[]},{"given":"Lindsay","family":"Sawyer","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2000,3,7]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)66599-8"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.1.3.3622999"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560020507"},{"key":"e_1_2_1_5_1","first-page":"3327","volume-title":"Proc. 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