ApoD Mediates Binding of HDL to LDL and to Growing T24 Carcinoma
Identifieur interne : 000422 ( Ncbi/Checkpoint ); précédent : 000421; suivant : 000423ApoD Mediates Binding of HDL to LDL and to Growing T24 Carcinoma
Auteurs : Sten Braesch-Andersen [Suède] ; Lena Beckman [Suède] ; Staffan Paulie [Suède] ; Makiko Kumagai-Braesch [Suède]Source :
- PLoS ONE [ 1932-6203 ] ; 2014.
Abstract
Apolipoprotein (Apo) D is an important protein produced in many parts of the body. It is necessary for the development and repair of the brain and protection from oxidative stress. The purpose of this study was to investigate the extent to which apoD interacts with lipoproteins in human plasma. By using detergent-free ELISA, we show that immobilized monoclonal antibodies against apoD very efficiently bind to low density lipoprotein (LDL) from plasma; this binding is as equally efficient as binding to an anti-apoB monoclonal antibody. Adding detergent to the plasma inhibited the binding, suggesting that the binding is dependent on the presence of intact lipoprotein particles. Reversing the system by using immobilized anti-apoB revealed that the affinity of apoD for LDL is rather low, suggesting that multiple bindings are needed for a durable connection. Biosensor experiments using purified lipoproteins also showed that purified apoD and high density lipoprotein 3 (HDL3), a lipoprotein fraction rich in apoD, were both able to bind LDL very efficiently, indicating that the HDL3-LDL interaction may be a physiological consequence of the affinity of apoD for LDL. Furthermore, we found that apoD increases the binding of HDL to actively growing T24 bladder carcinoma cells but not to quiescent, contact-inhibited, confluent T24 cells. This result is especially intriguing given that the T24 supernatant only contained detectable levels of apoD after growth inhibition, raising the possibility that alternating the expression of apoD and a putative apoD-receptor could give direction to the flow of lipids. In the current paper, we conclude that apoD mediates binding of HDL to LDL and to growing T24 carcinomas, thereby highlighting the importance of apoD in lipid metabolism.
Url:
DOI: 10.1371/journal.pone.0115180
PubMed: 25513803
PubMed Central: 4267786
Affiliations:
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PMC:4267786Le document en format XML
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<front><div type="abstract" xml:lang="en"><p>Apolipoprotein (Apo) D is an important protein produced in many parts of the body. It is necessary for the development and repair of the brain and protection from oxidative stress. The purpose of this study was to investigate the extent to which apoD interacts with lipoproteins in human plasma. By using detergent-free ELISA, we show that immobilized monoclonal antibodies against apoD very efficiently bind to low density lipoprotein (LDL) from plasma; this binding is as equally efficient as binding to an anti-apoB monoclonal antibody. Adding detergent to the plasma inhibited the binding, suggesting that the binding is dependent on the presence of intact lipoprotein particles. Reversing the system by using immobilized anti-apoB revealed that the affinity of apoD for LDL is rather low, suggesting that multiple bindings are needed for a durable connection. Biosensor experiments using purified lipoproteins also showed that purified apoD and high density lipoprotein 3 (HDL3), a lipoprotein fraction rich in apoD, were both able to bind LDL very efficiently, indicating that the HDL3-LDL interaction may be a physiological consequence of the affinity of apoD for LDL. Furthermore, we found that apoD increases the binding of HDL to actively growing T24 bladder carcinoma cells but not to quiescent, contact-inhibited, confluent T24 cells. This result is especially intriguing given that the T24 supernatant only contained detectable levels of apoD after growth inhibition, raising the possibility that alternating the expression of apoD and a putative apoD-receptor could give direction to the flow of lipids. In the current paper, we conclude that apoD mediates binding of HDL to LDL and to growing T24 carcinomas, thereby highlighting the importance of apoD in lipid metabolism.</p>
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<author><name sortKey="Garcia Centeno, Rm" uniqKey="Garcia Centeno R">RM Garcia-Centeno</name>
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<author><name sortKey="Garrote Adrados, Ja" uniqKey="Garrote Adrados J">JA Garrote-Adrados</name>
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</author>
<author><name sortKey="Carew, Te" uniqKey="Carew T">TE Carew</name>
</author>
<author><name sortKey="Koschinsky, T" uniqKey="Koschinsky T">T Koschinsky</name>
</author>
<author><name sortKey="Steinberg, D" uniqKey="Steinberg D">D Steinberg</name>
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<author><name sortKey="Canals, F" uniqKey="Canals F">F Canals</name>
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<author><name sortKey="Ray, Mj" uniqKey="Ray M">MJ Ray</name>
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</author>
<author><name sortKey="Aston, Ce" uniqKey="Aston C">CE Aston</name>
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<author><name sortKey="Hamman, Rf" uniqKey="Hamman R">RF Hamman</name>
</author>
<author><name sortKey="Kamboh, Mi" uniqKey="Kamboh M">MI Kamboh</name>
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</analytic>
</biblStruct>
<biblStruct><analytic><author><name sortKey="Yoshikawa, M" uniqKey="Yoshikawa M">M Yoshikawa</name>
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<author><name sortKey="Sakuma, N" uniqKey="Sakuma N">N Sakuma</name>
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<biblStruct><analytic><author><name sortKey="Shao, B" uniqKey="Shao B">B Shao</name>
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</TEI>
<affiliations><list><country><li>Suède</li>
</country>
<region><li>Svealand</li>
</region>
<settlement><li>Stockholm</li>
</settlement>
</list>
<tree><country name="Suède"><noRegion><name sortKey="Braesch Andersen, Sten" sort="Braesch Andersen, Sten" uniqKey="Braesch Andersen S" first="Sten" last="Braesch-Andersen">Sten Braesch-Andersen</name>
</noRegion>
<name sortKey="Beckman, Lena" sort="Beckman, Lena" uniqKey="Beckman L" first="Lena" last="Beckman">Lena Beckman</name>
<name sortKey="Beckman, Lena" sort="Beckman, Lena" uniqKey="Beckman L" first="Lena" last="Beckman">Lena Beckman</name>
<name sortKey="Kumagai Braesch, Makiko" sort="Kumagai Braesch, Makiko" uniqKey="Kumagai Braesch M" first="Makiko" last="Kumagai-Braesch">Makiko Kumagai-Braesch</name>
<name sortKey="Paulie, Staffan" sort="Paulie, Staffan" uniqKey="Paulie S" first="Staffan" last="Paulie">Staffan Paulie</name>
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</tree>
</affiliations>
</record>
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