NDLI: A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity

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A missense mutation Pro157Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity

Content Provider	Scilit
Author	Bruin, Taco Kastelein, John J. P. Diermen, Denise E. Ma, Yuanhong Henderson, Howard E. Stuyt, Paul M. J. Stalenhoef, Anton F. H. Sturk, Augueste Brunzell, John D. Hayden, Michael R.
Copyright Year	1992
Description	Journal: Journal of Biological Inorganic Chemistry Here we report on the molecular defect that leads to a deficiency of lipoprotein lipase (LPL) activity in a proband of Dutch descent. Southern-blot analysis of the LPL gene from the patient did not reveal any major DNA rearrangements. Sequencing of polymerase-chain-reaction-amplified DNA revealed that the proband is a homozygote for G725C, resulting in a substitution of Pro157 for Arg. This substitution alters a restriction site for PvuII, which allowed rapid identification of the mutant allele in family members. Site-directed mutagenesis and transient expression of the mutant LPL in COS cells produced an enzymatically inactive protein, establishing the functional significance of this mutation. This naturally occurring mutation which alters the Pro157 adjacent to Asp156 of the proposed catalytic triad, indicates that this region of the protein is indeed crucial for LPL catalytic activit
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1992.tb17182.x/pdf
Ending Page	272
Page Count	6
Starting Page	267
ISSN	09498257
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1992.tb17182.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	208
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1992-09-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemistry and Molecular Biology Lipoprotein Lipase
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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