Homozygosity for a mutation in the lipoprotein lipase gene (Gly139-->Ser) causes chylomicronaemia in a boy of Spanish descent.
The enzyme lipoprotein lipase (LPL) plays a crucial role in triglyceride metabolism through catalysis of triglyceride-rich chylomicrons and very low density lipoproteins. Primary LPL deficiency manifests with chylomicronaemia and is caused by mutations in the LPL gene. In this paper we report a novel molecular defect (G670-->A) in exon 4 of the LPL gene, resulting in a substitution of serine for glycine at position 139 in the mature protein. We identified homozygosity for this mutation in a boy of Spanish descent. In vitro mutagenesis provided formal proof that this missense mutation completely abolishes LPL function and therefore is the cause of LPL deficiency.
Bijvoet
S M
SM
Centre for Haemostasis, Thrombosis, Atherosclerosis and Inflammation Research, Academic Medical Centre, University of Amsterdam, The Netherlands.
Bruin
T
T
Tuzgöl
S
S
Bakker
H D
HD
Hayden
M R
MR
Kastelein
J J
JJ
D000293:Adolescent; D001483:Base Sequence; D002914:Chylomicrons / Q000097:blood*; D004247:DNA; D005260:Female; D005998:Glycine; D006720:Homozygote; D006801:Humans; D008071:Lipoprotein Lipase / Q000172:deficiency / Q000235:genetics* / Q000378:metabolism; D008297:Male; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010375:Pedigree; D012694:Serine; D013030:Spain / Q000208:ethnology
D002914:Chylomicrons; D012694:Serine; D004247:DNA; D008071:Lipoprotein Lipase; D005998:Glycine