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Sökning: onr:"swepub:oai:DiVA.org:umu-30617" > Mutation of conserv...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003843naa a2200541 4500
001oai:DiVA.org:umu-30617
003SwePub
008100108s2010 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:120432974
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-306172 URI
0247 a https://doi.org/10.1194/jlr.M0027172 DOI
0247 a http://kipublications.ki.se/Default.aspx?queryparsed=id:1204329742 URI
040 a (SwePub)umud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Olivecrona, Gunillau Umeå universitet,Fysiologisk kemi4 aut0 (Swepub:umu)guol0002
2451 0a Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia
264 1a New York :b Rockefeller U.P.c 2010
338 a print2 rdacarrier
520 a We investigated a family from northern Sweden in which three of four siblings have congenital chylomicronemia. Lipoprotein lipase (LPL) activity and mass in pre- and post-heparin plasma were low, and LPL release into plasma after heparin injection was delayed. LPL activity and mass in adipose tissue biopsies appeared normal. [35S]Methionine incorporation studies on adipose tissue showed that newly synthesized LPL was normal in size and normally glycosylated. Breast milk from the affected female subjects contained normal to elevated LPL mass and activity levels. The milk had a lower than normal milk lipid content, and the fatty acid composition was compatible with the milk lipids being derived from de novo lipogenesis, rather than from the plasma lipoproteins. Given the delayed release of LPL into the plasma after heparin, we suspected that the chylomicronemia might be caused by mutations in GPIHBP1. Indeed, all three affected siblings were compound heterozygotes for missense mutations involving highly conserved cysteines in the Ly6 domain of GPIHBP1 (C65S and C68G). The mutant GPIHBP1 proteins reached the surface of transfected CHO cells but were defective in their ability to bind LPL (as judged by both cell-based and cell-free LPL binding assays). Thus, the conserved cysteines in the Ly6 domain are crucial for GPIHBP1 function.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a compound heterozygote
653 a lipoprotein lipase
653 a milk lipids
653 a mammary gland
653 a glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
653 a endothelial cells
7001 a Ehrenborg, Ewau Karolinska Institutet4 aut
7001 a Semb, Henriku Umeå universitet,Fysiologisk kemi4 aut
7001 a Makoveichuk, Elenau Umeå universitet,Fysiologisk kemi4 aut0 (Swepub:umu)elma0002
7001 a Lindberg, Annau Umeå universitet,Fysiologisk kemi4 aut
7001 a Hayden, Michael R4 aut
7001 a Gin, Peter4 aut
7001 a Davies, Brandon S J4 aut
7001 a Weinstein, Michael M4 aut
7001 a Fong, Loren G4 aut
7001 a Beigneux, Anne P4 aut
7001 a Young, Stephen G4 aut
7001 a Olivecrona, Thomasu Umeå universitet,Fysiologisk kemi4 aut0 (Swepub:umu)thol0003
7001 a Hernell, Olleu Umeå universitet,Pediatrik4 aut0 (Swepub:umu)olhe0002
7102 a Umeå universitetb Fysiologisk kemi4 org
7730 t Journal of Lipid Researchd New York : Rockefeller U.P.g 51:6, s. 1535-1545q 51:6<1535-1545x 0022-2275x 1539-7262
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-30617
8564 8u https://doi.org/10.1194/jlr.M002717
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:120432974

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