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
; 205(1): 506-15, 1994 Nov 30.
Article
em En
| MEDLINE
| ID: mdl-7999071
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Asparagina
/
Códon
/
Lipase Lipoproteica
/
Mutação
Limite:
Adult
/
Humans
/
Male
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1994
Tipo de documento:
Article