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Papers In Press, published online ahead of print May 1, 2008
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Journal of Lipid Research, Vol. 49, 1103-1112, May 2008
Copyright © 2008 by American Society for Biochemistry and Molecular Biology

Children's Hospital Oakland Research Institute, Oakland, CA 94609
* This work was supported in part by grants from Philip Morris, Inc., and Philip Morris International to V.S. and by Grant HL-070583 from the National Institutes of Health to F.A.K.
The online version of this article (available at http://www.jlr.org) contains Supplementary data in form of two figures.
Published, JLR Papers in Press, February 11, 2008.
1 To whom correspondence should be addressed. e-mail: esoupene{at}chori.org
Human acyl-coenzyme A binding domain-containing member 6 (ACBD6) is a modular protein that carries an acyl-CoA binding domain at its N terminus and two ankyrin motifs at its C terminus. ACBD6 binds long-chain acyl-CoAs with a strong preference for unsaturated, C18:1-CoA and C20:4-CoA, over saturated, C16:0-CoA, acyl species. Deletion of the C terminus, which is not conserved among the members of this family, did not affect the binding capacity or the substrate specificity of the protein. ACBD6 is not a ubiquitous protein, and its expression is restricted to tissues and progenitor cells with functions in blood and vessel development. ACBD6 was detected in bone marrow, spleen, placenta, cord blood, circulating CD34+ progenitors, and embryonic-like stem cells derived from placenta. In placenta, the protein was only detected in CD34+ progenitor cells present in blood and in CD31+ endothelial cells surrounding the blood vessels. These cells were also positive for the marker CD133, and they probably constitute hemangiogenic stem cells, precursors of both blood and vessels. We propose that human ACBD6 represents a cellular marker for primitive progenitor cells with functions in hematopoiesis and vascular endothelium development.
Supplementary key words placenta endothelial cells vascular development stem cells
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