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Papers In Press, published online ahead of print July 16, 2004
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Department of Pathology, Wake Forest University School of Medicine, Winston-Salem, NC 27157-1040
Corresponding Author: gshelnes{at}wfubmc.edu
To examine the role of apolipoprotein (apo) AIV in the intracellular trafficking and secretion of apoB, COS cells were cotransfected with microsomal triglyceride transfer protein (MTP), apoB41 (amino terminal 41% of apoB), and either native apoAIV or apoAIV modified with the C-terminal endoplasmic reticulum (ER) retention signal, KDEL (apoAIV-KDEL). As expected, apoAIV-KDEL was inefficiently secreted, relative to native apoAIV. Coexpression of apoB41 with apoAIV-KDEL reduced the secretion of apoB41 by ~80%. The apoAIV-KDEL effect was specific, as neither KDEL modified forms of human serum albumin or apoAI affected apoB41 secretion. Similar results were observed in McA-RH7777 rat hepatoma cells, which express endogenous MTP. The full inhibitory effect of apoAIV-KDEL on apoB secretion was observed only for forms of apoB containing a minimum of the amino terminal 25% of the protein (apoB25). However, apoAIV-KDEL inhibited the secretion of both lipid-associated and lipid-poor forms of apoB25. Dual label-immunofluorescence microscopy of cells transfected with native apoAIV and apoB25 revealed that both apolipoproteins were localized to the ER and Golgi, as expected. However, when apoAIV-KDEL was co-transfected with apoB25, both proteins localized primarily to the ER. These data suggest that apoAIV may physically interact with apoB in the secretory pathway, perhaps reflecting a role in modulating the process of triglyceride-rich lipoprotein assembly and secretion.
Revised on July 1, 2004
Accepted on July 4, 2004
Apolipoprotein AIV tagged with the C-terminal ER retention signal KDEL perturbs the intracellular trafficking and secretion of apolipoprotein B
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