title: Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins.
abstract: The transfer of lipids in aqueous environments such as serum has been attributed to a recently characterized class of proteins. Abnormal regulation of serum lipids by these proteins is thought to be a key event in the pathophysiology of cardiovascular diseases. Lipopolysaccharide (endotoxin) binding protein (LBP) was identified by virtue of its ability to bind bacterial lipid A. We have analyzed the exon-intron organization of the LBP gene and the nucleotide sequence of its approximately 20 kb spanning 5'- and 3'-untranslated regions. When comparing the genomic organization of LBP with that of two other genes coding for lipid transfer proteins, significant homologies were found. The LBP gene includes 15 exons, and the 2-kb promoter contains recognition elements of acute phase-typical reactants and a repetitive 12-mer motif with an as yet unknown protein-binding property. Detailed sequence comparison revealed a closer relatedness of LBP with PLTP than with CETP as demonstrated by an almost identical intron positioning. This high degree of similarity supports functional studies by others suggesting that like LBP, PLTP may also be able to bind and transport bacterial lipopolysaccharide.
authors.affiliation: Molecular Sepesis Research Laboratory, Max-Delbrück Center for Molecular Medicine (MDC), University Hospital Charité, Humboldt University, Berlin, Germany.
authors.forename: C J
authors.initials: CJ
authors.lastname: Kirschning
authors.forename: J
authors.initials: J
authors.lastname: Au-Young
authors.forename: N
authors.initials: N
authors.lastname: Lamping
authors.forename: D
authors.initials: D
authors.lastname: Reuter
authors.forename: D
authors.initials: D
authors.lastname: Pfeil
authors.forename: J J
authors.initials: JJ
authors.lastname: Seilhamer
authors.forename: R R
authors.initials: RR
authors.lastname: Schumann
mesh_terms: D000209:Acute-Phase Proteins; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D053480:Cholesterol Ester Transfer Proteins; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006023:Glycoproteins; D006801:Humans; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D049294:Phospholipid Transfer Proteins; D014176:Protein Biosynthesis; D014407:Tumor Cells, Cultured; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D002352:Carrier Proteins; D053480:Cholesterol Ester Transfer Proteins; D018076:DNA, Complementary; D006023:Glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D049294:Phospholipid Transfer Proteins; D000099231:Lipopolysaccharide-Binding Protein; C506642:CETP protein, human