Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M

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Fältnamn	Indikatorer	Metadata
000		03530naa a2200397 4500
001		oai:lup.lub.lu.se:d6b5be0f-41d3-4236-b80e-39445ce5240e
003		SwePub
008		160401s2007 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://lup.lub.lu.se/record/6916722 URI
024	7	a https://doi.org/10.1194/jlr.M700103-JLR2002 DOI
040		a (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a art2 swepub-publicationtype
072	7	a ref2 swepub-contenttype
100	1	a Ahnström, Josefinu Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-jao
245	1 0	a Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M
264	1	c 2007
520		a Apolipoprotein M (apoM) is a plasma protein associated mainly with HDL. ApoM is suggested to be important for the formation of pre beta-HDL, but its mechanism of action is unknown. Homology modeling has suggested apoM to be a lipocalin. Lipocalins share a structurally conserved beta-barrel, which in many lipocalins bind hydrophobic ligands. The aim of this study was to test the ability of apoM to bind different hydrophobic substances. ApoM was produced both in Escherichia coli and in HEK 293 cells. Characterization of both variants with electrophoretic and immunological methods suggested apoM from E. coli to be correctly folded. Intrinsic tryptophan fluorescence of both apoM variants revealed that retinol, all-trans-retinoic acid, and 9-cis-retinoic acid bound ( dissociation constant 5 2-3 mu M), whereas other tested substances ( e.g., cholesterol, vitamin K, and arachidonic acid) did not. The intrinsic fluorescence of two apoM mutants carrying single tryptophans was quenched by retinol and retinoic acid to the same extent as wild-type apoM, indicating that the environment of both tryptophans was affected by the binding. In conclusion, the binding of retinol and retinoic acid supports the hypothesis that apoM is a lipocalin. The physiological relevance of this binding has yet to be elucidated.
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Läkemedelskemi0 (SwePub)301032 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Medicinal Chemistry0 (SwePub)301032 hsv//eng
653		a cholesterol
653		a signal peptide
653		a lipoprotein
653		a high density
653		a intrinsic fluorescence
653		a retinol
653		a retinoic acid
700	1	a Faber, Kirstenu Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-kfa
700	1	a Axler, Olofu Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-oax
700	1	a Dahlbäck, Björnu Lund University,Lunds universitet,Klinisk kemi, Malmö,Forskargrupper vid Lunds universitet,Clinical Chemistry, Malmö,Lund University Research Groups4 aut0 (Swepub:lu)klke-bda
710	2	a Klinisk kemi, Malmöb Forskargrupper vid Lunds universitet4 org
773	0	t Journal of Lipid Researchg 48:8, s. 1754-1762q 48:8<1754-1762x 1539-7262
856	4	u http://dx.doi.org/10.1194/jlr.M700103-JLR200y FULLTEXT
856	4 8	u https://lup.lub.lu.se/record/691672
856	4 8	u https://doi.org/10.1194/jlr.M700103-JLR200

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Av författaren/redakt...: Ahnström, Josefi ...; Faber, Kirsten; Axler, Olof; Dahlbäck, Björn

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MEDICIN OCH HÄLSOVETENSKAP: MEDICIN OCH HÄLS ...; och Medicinska och f ...; och Läkemedelskemi

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Av lärosätet: Lunds universitet

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