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Papers In Press, published online ahead of print April 21, 2004
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Clinical Biochemistry, KB3011, Rigshospitalet, University of Copenhagen, Copenhagen DK-2100
Corresponding Author: larsbo{at}rh.dk
A novel human apolipoprotein (apoM) was recently described and demonstrated to be a lipocalin. We have now examined apoM in wild-type mice and mice with genetically altered lipoprotein metabolism. Liver and kidney showed high mRNA expression, whereas spleen, heart, brain, and testis demonstrated low expression. ApoM gene expression was initiated on embryonic day 10. Western blotting analysis of plasma suggested that mouse apoM like its human counterpart is secreted with a retained signal peptide, but unlike human apoM it is not glycosylated. Gel filtration of plasma showed apoM to be associated with HDL-sized particles in wild type and apo-AI deficient mice, with HDL and LDL-sized particles in LDL-receptor deficient mice, whereas apoM was mainly found in VLDL-sized particles in high-fat, high-cholesterol-fed apo-E deficient mice. The plasma concentration of apoM was similar in wild type, LDL-receptor deficient, and apo-E deficient mice, but was reduced to 33 % in apoA-I deficient compared with wild type mice (P = 0.007). The data suggest that ApoM mainly associates with HDL in normal mice but also with the pathologically elevated lipoprotein fraction in genetically modified mice. The substantially decreased apoM levels in ApoA-I deficient mice suggest a connection between apoM and apoA-I metabolisms.
Revised on April 21, 2004
Accepted on April 9, 2004
Characterization of apoM in normal and genetically modified mice
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