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Contribution Of The Carboxy-terminal Domain Of Lipoprotein Lipase To Interaction With Heparin And Lipoproteins.

A. Lõokene, M. S. Nielsen, J. Gliemann, G. Olivecrona
Published 2000 · Chemistry, Medicine

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The C-terminal domain of lipoprotein lipase (LPL) is involved in several important interactions. To assess its contribution to the binding ability of full-length LPL we have determined kinetic constants using biosensor technique. The affinity of the C-terminal domain for heparin was about 500-fold lower than that of full-length LPL (K(d) = 1.3 microM compared to 3.1 nM). Replacement of Lys403, Arg405 and Lys407 by Ala abolished the heparin affinity, whereas replacement of Arg420 and Lys422 had little effect. The C-terminal domain increased binding of chylomicrons and VLDL to immobilized heparin relatively well, but was less than 10% efficient in binding of LDL compared to full-length LPL. Deletion of residues 390-393 (WSDW) did not change the affinity to heparin and only slightly decreased the affinity to lipoproteins. We conclude that the C-terminal folding domain contributes only moderately to the heparin affinity of full-length LPL, whereas the domain appears important for tethering triglyceride-rich lipoproteins to heparin-bound LPL.
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