Apolipoprotein M: progress in understanding its regulation and metabolic functions

Publikation: Bidrag til tidsskriftTidsskriftartikelForskning

Standard

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 tidsskriftTidsskriftartikelForskning

Harvard

Christoffersen, C, Dahlbäck, B & Nielsen, LB 2006, 'Apolipoprotein M: progress in understanding its regulation and metabolic functions', Scandinavian Journal of Clinical & Laboratory Investigation, bind 66, nr. 7, s. 631-7. https://doi.org/10.1080/00365510600885500

APA

Christoffersen, C., Dahlbäck, B., & Nielsen, L. B. (2006). Apolipoprotein M: progress in understanding its regulation and metabolic functions. Scandinavian Journal of Clinical & Laboratory Investigation, 66(7), 631-7. https://doi.org/10.1080/00365510600885500

Vancouver

Christoffersen C, Dahlbäck B, Nielsen LB. Apolipoprotein M: progress in understanding its regulation and metabolic functions. Scandinavian Journal of Clinical & Laboratory Investigation. 2006;66(7):631-7. https://doi.org/10.1080/00365510600885500

Author

Christoffersen, Christina ; Dahlbäck, B ; Nielsen, L B. / Apolipoprotein M : progress in understanding its regulation and metabolic functions. I: Scandinavian Journal of Clinical & Laboratory Investigation. 2006 ; Bind 66, Nr. 7. s. 631-7.

Bibtex

@article{f1269abc810745a7b98fdd572818727f,
title = "Apolipoprotein M: progress in understanding its regulation and metabolic functions",
abstract = "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.",
keywords = "Animals, Apolipoproteins, Atherosclerosis, Chromosome Mapping, Gene Expression Regulation, Humans, Kidney, Lipocalins, Lipoproteins, Mice, Sequence Analysis, Protein",
author = "Christina Christoffersen and B Dahlb{\"a}ck and Nielsen, {L B}",
year = "2006",
doi = "10.1080/00365510600885500",
language = "English",
volume = "66",
pages = "631--7",
journal = "Scandinavian Journal of Clinical & Laboratory Investigation",
issn = "0036-5513",
publisher = "Taylor & Francis",
number = "7",

}

RIS

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