Activation of lipoprotein lipase by apolipoprotein C-II is modulated by the COOH terminal region of apolipoprotein C-III.

Abstract:

:The in vitro effect of apolipoprotein C-II (apo C-II) on the apolipoprotein C-III (apo C-III) induced activation of bovine milk lipoprotein lipase (LPL) was studied in vitro using a synthetic substrate. Apo C-III effectively inhibited, in a dose-dependent manner, the activation of lipoprotein lipase induced by apo C-II. A 3-fold molar apo C-III excess decreased the lipoprotein lipase activity by 25%. Thrombin cleavage of apo C-III produced two fragments: only fragment 41-79 retained the inhibitory activity and was equipotent to native apo C-III1 on a molar basis. Neither displacement of apo C-II from the substrate, as determined using 125I-labeled apo C-II, nor the charge carried by sialic residues of apo C-III, as demonstrated in experiments performed after neuraminidase treatment, accounted for this effect. I speculate that apo C-III may act by inhibiting the apo C-II-LPL interaction.

journal_name

Chem Phys Lipids

authors

Catapano AL

doi

10.1016/0009-3084(87)90038-7

subject

Has Abstract

pub_date

1987-10-01 00:00:00

pages

39-47

issue

1

eissn

0009-3084

issn

1873-2941

pii

0009-3084(87)90038-7

journal_volume

45

pub_type

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