Biochemical Analysis of the Lipoprotein Lipase Truncation Variant, LPL^S447X, Reveals Increased Lipoprotein Uptake.

ABSTRACT: Lipoprotein lipase (LPL) is responsible for the hydrolysis of triglycerides from circulating lipoproteins. Whereas most identified mutations in the LPL gene are deleterious, one mutation, LPL^S447X, causes a gain of function. This mutation truncates two amino acids from LPL's C-terminus. Carriers of LPL^S447X have decreased VLDL levels and increased HDL levels, a cardioprotective phenotype. LPL^S447X is used in Alipogene tiparvovec, the gene therapy product for individuals with familial LPL deficiency. It is unclear why LPL^S447X results in a serum lipid profile more favorable than that of LPL. In vitro reports vary as to whether LPL^S447X is more active than LPL. We report a comprehensive, biochemical comparison of purified LPL^S447X</

SUBMITTER: Hayne CK 

PROVIDER: S-EPMC5848218 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature