Interaction of lipoprotein lipase with heparin.
The hydrolysis of triglyceride-rich plasma lipoproteins is initiated by lipoprotein lipase (LPL) located at the luminal surface of endothelial cells. We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate. We and others recently isolated LPL cDNAs from various animals. The deduced amino acid sequence from cDNA sequence is highly conserved among animal species. The structural analysis revealed two regions rich in basic amino acid residues at the carboxyl-terminal region that may interact with the anionic heparin-like molecules. Amino acid residues 292 to 300 of bovine LPL are extremely similar to the reported heparin binding sites on apolipoproteins B-100 (amino acid residues 3359-3367) and E (amino acid residues 142-150).
Oka
K
K
Department of Medicine, Mount Sinai School of Medicine, New York, New York 10029.
Wang-Iverson
P
P
Paterniti
J R
JR
Brown
W V
WV
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D002478:Cells, Cultured; D004247:DNA / Q000235:genetics; D004730:Endothelium, Vascular / Q000187:drug effects / Q000201:enzymology; D006168:Guinea Pigs; D006493:Heparin / Q000378:metabolism* / Q000494:pharmacology; D006497:Heparan Sulfate / Q000494:pharmacology; D006801:Humans; D008071:Lipoprotein Lipase / Q000235:genetics / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000032:analysis; D051379:Mice; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D015345:Oligonucleotide Probes; D012333:RNA, Messenger / Q000235:genetics; D014471:Umbilical Veins
D004247:DNA; D006493:Heparin; D006497:Heparan Sulfate; D008071:Lipoprotein Lipase; D015345:Oligonucleotide Probes; D012333:RNA, Messenger