A NATURALLY-OCCURRING MUTATION AT THE 2ND 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

作者：KOBAYASHI J^*; INADERA H; FUJITA Y; TALLEY G; MORISAKI N; YOSHIDA S; SAITO Y; FOJO SS; BREWER HB

来源：Biochemical and Biophysical Research Communications, 1994, 205(1): 506-515.

DOI：10.1006/bbrc.1994.2694

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 mu mol/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 homozymous nucleotide change: a A --> G transition at nucleotide position 383, resulting in an amino acid substitution of Ser for Asn(43), 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.

• 出版日期1994-11-30