Apolipoprotein M: progress in understanding its regulation and metabolic functions
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Apolipoprotein M : progress in understanding its regulation and metabolic functions. / Christoffersen, Christina; Dahlbäck, B; Nielsen, L B.
I: Scandinavian Journal of Clinical & Laboratory Investigation, Bind 66, Nr. 7, 2006, s. 631-7.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning
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TY - JOUR
T1 - Apolipoprotein M
T2 - progress in understanding its regulation and metabolic functions
AU - Christoffersen, Christina
AU - Dahlbäck, B
AU - Nielsen, L B
PY - 2006
Y1 - 2006
N2 - ApoM is a novel apolipoprotein mainly present in high-density lipoprotein (HDL). It belongs to the lipocalin protein superfamily and may bind a small but so far unknown lipophilic ligand. It is secreted without cleavage of its hydrophobic signal peptide, which probably anchors apoM in the phospholipid moiety of plasma lipoproteins. Recent studies suggest that apoM may affect HDL metabolism and have anti-atherogenic functions. The subfraction of human HDL that contains apoM therefore protects LDL from oxidation and mediates cholesterol efflux more efficiently then HDL without apoM. In addition to hepatocytes, apoM is highly expressed in kidney proximal tubule cells. Recent data suggest that apoM is secreted into the pre-urine from the tubule cells but is normally taken up again in a megalin-dependent fashion. Further studies of mice with genetically modified apoM expression will be essential to unravel the potential roles of apoM in lipoprotein metabolism, atherosclerosis and kidney biology.
AB - ApoM is a novel apolipoprotein mainly present in high-density lipoprotein (HDL). It belongs to the lipocalin protein superfamily and may bind a small but so far unknown lipophilic ligand. It is secreted without cleavage of its hydrophobic signal peptide, which probably anchors apoM in the phospholipid moiety of plasma lipoproteins. Recent studies suggest that apoM may affect HDL metabolism and have anti-atherogenic functions. The subfraction of human HDL that contains apoM therefore protects LDL from oxidation and mediates cholesterol efflux more efficiently then HDL without apoM. In addition to hepatocytes, apoM is highly expressed in kidney proximal tubule cells. Recent data suggest that apoM is secreted into the pre-urine from the tubule cells but is normally taken up again in a megalin-dependent fashion. Further studies of mice with genetically modified apoM expression will be essential to unravel the potential roles of apoM in lipoprotein metabolism, atherosclerosis and kidney biology.
KW - Animals
KW - Apolipoproteins
KW - Atherosclerosis
KW - Chromosome Mapping
KW - Gene Expression Regulation
KW - Humans
KW - Kidney
KW - Lipocalins
KW - Lipoproteins
KW - Mice
KW - Sequence Analysis, Protein
U2 - 10.1080/00365510600885500
DO - 10.1080/00365510600885500
M3 - Journal article
C2 - 17101555
VL - 66
SP - 631
EP - 637
JO - Scandinavian Journal of Clinical & Laboratory Investigation
JF - Scandinavian Journal of Clinical & Laboratory Investigation
SN - 0036-5513
IS - 7
ER -
ID: 100888582