Paper Report for: Kobayashi_1994_Biochem.Biophys.Res.Commun_205_506
Reference
Title: 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 Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB, Jr. Ref: Biochemical & Biophysical Research Communications, 205:506, 1994 : PubMed
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.
Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB, Jr. (1994) 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 Biochemical & Biophysical Research Communications205: 506-15
Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB, Jr. (1994) Biochemical & Biophysical Research Communications205: 506-15