A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion

Biochem Biophys Res Commun. 1994 Nov 30;205(1):506-15. doi: 10.1006/bbrc.1994.2694.

Abstract

The patient was a 20-year-old male. His fasting plasma triglyceride and cholesterol levels were 1258 mg/dl and 138 mg/dl, respectively. The lipoprotein lipase (LPL) activity and mass from postheparin plasma of the patient were 0.00 mumol/ml/h (normal range: 5.51 +/- 1.12) and 23 ng/ml (normal range: 220 +/- 42), respectively. DNA sequence analysis of the LPL gene from the patient revealed a homozygous nucleotide change: a A-->G transition at nucleotide position 383, resulting in an amino acid substitution of Ser for Asn43, which is believed to be an N-linked glycosylation site of the LPL mature protein. Expression studies of this mutant LPL cDNA produced an inactive LPL protein which was not secreted into the media.

MeSH terms

  • Adult
  • Amino Acid Sequence
  • Asparagine / genetics*
  • Base Sequence
  • Codon*
  • DNA Mutational Analysis
  • DNA, Complementary
  • Glycosylation
  • Heparin
  • Humans
  • Lipoprotein Lipase / deficiency
  • Lipoprotein Lipase / genetics*
  • Lipoprotein Lipase / metabolism
  • Male
  • Molecular Sequence Data
  • Mutation*
  • Serine / genetics

Substances

  • Codon
  • DNA, Complementary
  • Serine
  • Asparagine
  • Heparin
  • Lipoprotein Lipase