Familial lipoprotein lipase deficiency caused by known (G188E) and novel (W394X) LPL gene mutations

Amanda Hooper, G.M. Crawford, J.M. Brisbane, Kenneth Robertson, Gerald Watts, Frank Van Bockxmeer, John Burnett

Research output: Contribution to journalReview article

13 Citations (Scopus)

Abstract

Lipoprotein lipase (LPL) is the key enzyme in the catabolism of triglyceride-rich lipoproteins in the circulation. Familial LPL deficiency is characterized by hypertriglyceridaemia and absence of LPL activity. We report a case of LPL deficiency in a 43-year-old woman, who initially presented in childhood with chylomicronaemia syndrome. At that time, her plasma triglyceride concentration was similar to 30 mmol/L and post-heparin lipolytic activity was very low. In addition to having the known missense mutation LPL G188E, the patient was also found to have a novel nonsense mutation in exon 8, namely LPL W394X. The novel substitution in exon 8 (c.1262G > A) predicts a truncated protein product of 393 amino acids that lacks the carboxylterminal 12% of the mature LPL. Trp(394) is part of a cluster of exposed tryptophan residues in the carboxyl-terminal domain of LPL important for binding lipid substrate. Of 11 members from her three-generation family, three were heterozygotes for G188E (mean plasma triglyceride, 3.5 +/- 2.0 mmol/L), whereas six were heterozygotes for W394X (triglyceride, 4.3 +/- 1.8 mmol/L). In summary, we describe a case of familial LPL deficiency caused by compound heterozygosity for known (G188E) and novel (W394X) LPL gene mutations.
Original languageEnglish
Pages (from-to)102-105
JournalAnnals of Clinical Biochemistry
Volume45
DOIs
Publication statusPublished - 2008

Fingerprint Dive into the research topics of 'Familial lipoprotein lipase deficiency caused by known (G188E) and novel (W394X) LPL gene mutations'. Together they form a unique fingerprint.

Cite this