TY - JOUR
T1 - Molecular cloning of the human ATP-Binding cassette transporter 1 (hABC1)
T2 - Evidence for sterol-dependent regulation in macrophages
AU - Langmann, Thomas
AU - Klucken, Jochen
AU - Reil, Markus
AU - Liebisch, Gerhard
AU - Luciani, Marie Françoise
AU - Chimini, Giovanna
AU - Kaminski, Wolfgang E.
AU - Schmitz, Gerd
N1 - Funding Information:
The authors thank Dr. Christa Buechler and Renate Glätzl for technical assistance and valuable discussions. This work was supported by a grant from the Deutsche Forschungsgemein-schaft within the Forschergruppe “Molekulare Grundlagen der Differenzierung und Aktivierung mononukleärer Phagozyten” (AN 111/6-1).
PY - 1999/4/2
Y1 - 1999/4/2
N2 - We have cloned the full-length cDNA for the human ATP binding cassette transporter 1 (hABC1). The 6603-bp open reading frame encodes a polypeptide of 2201 amino acids resulting in a deduced molecular weight of 220 kDa. The hABC1 cDNA is highly homologous (62%) to the human rim ABC transporter (ABCR). hABC1 is expressed in a variety of human tissues with highest expression levels found in placenta, liver, lung, adrenal glands, and fetal tissues. We demonstrate that the hABC1 expression is induced during differentiation of human monocytes into macrophages in vitro. In macrophages, both the hABC1 mRNA and protein expression are upregulated in the presence of acetylated low-density lipoprotein (AcLDL). The AcLDL-induced increase in hABC1 expression is reversed by cholesterol depletion mediated by the addition of high-density lipoprotein (HDL3). Our data, demonstrating sterol-dependent regulation of hABC1 in human monocytes/macrophages, suggest a novel role for this transporter molecule in membrane lipid transport.
AB - We have cloned the full-length cDNA for the human ATP binding cassette transporter 1 (hABC1). The 6603-bp open reading frame encodes a polypeptide of 2201 amino acids resulting in a deduced molecular weight of 220 kDa. The hABC1 cDNA is highly homologous (62%) to the human rim ABC transporter (ABCR). hABC1 is expressed in a variety of human tissues with highest expression levels found in placenta, liver, lung, adrenal glands, and fetal tissues. We demonstrate that the hABC1 expression is induced during differentiation of human monocytes into macrophages in vitro. In macrophages, both the hABC1 mRNA and protein expression are upregulated in the presence of acetylated low-density lipoprotein (AcLDL). The AcLDL-induced increase in hABC1 expression is reversed by cholesterol depletion mediated by the addition of high-density lipoprotein (HDL3). Our data, demonstrating sterol-dependent regulation of hABC1 in human monocytes/macrophages, suggest a novel role for this transporter molecule in membrane lipid transport.
UR - http://www.scopus.com/inward/record.url?scp=0033515841&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1999.0406
DO - 10.1006/bbrc.1999.0406
M3 - Article
C2 - 10092505
AN - SCOPUS:0033515841
SN - 0006-291X
VL - 257
SP - 29
EP - 33
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -