title: The lipocalin Xlcpl1 expressed in the neural plate of Xenopus laevis embryos is a secreted retinaldehyde binding protein.
abstract: The cellular and structural properties and binding capabilities of a lipocalin expressed in the early neural plate of Xenopus laevis embryos and the adult choroid plexus have been investigated. It was found that this lipocalin, termed Xlcpl1, binds retinal at a nanomolar concentration, retinoic acid in the micromolar range, but does not show binding to retinol. Furthermore, this protein also binds D/L thyroxine. The Xlcpl1 cDNA was expressed in cell culture using the vaccinia virus expression system. In AtT20 cells, Xlcpl1 was secreted via the constitutive secretory pathway. We therefore assume that cpl1 binds retinaldehyde during the transport through the compartments of the secretory pathway that are considered to be the storage compartments of retinoids. Therefore, cpl1-expressing cells will secrete the precursors of active retinoids such as retinoic acid isomers. These retinoids may enter the cytosol by diffusion or receptor-controlled mechanisms, as has been shown for exogenously applied retinoids. Based on these data, it is suggested that cpl1 is an integral member of the retinoid signaling pathway and, therefore, it plays a key role in pattern formation in early embryonic development.
authors.affiliation: Austrian Academy of Sciences, Institute of Molecular Biology, Salzburg, Austria. lepperd@oeaw.ac.at
authors.forename: G
authors.initials: G
authors.lastname: Lepperdinger
authors.forename: B
authors.initials: B
authors.lastname: Strobl
authors.forename: A
authors.initials: A
authors.lastname: Jilek
authors.forename: A
authors.initials: A
authors.lastname: Weber
authors.forename: J
authors.initials: J
authors.lastname: Thalhamer
authors.forename: H
authors.initials: H
authors.lastname: Flöckner
authors.forename: C
authors.initials: C
authors.lastname: Mollay
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D018507:Gene Expression Regulation, Developmental; D006367:HeLa Cells; D006801:Humans; D054834:Lipocalins; D008969:Molecular Sequence Data; D009420:Nervous System / Q000196:embryology*; D012172:Retinaldehyde / Q000378:metabolism*; D016415:Sequence Alignment; D014616:Vaccinia virus / Q000235:genetics; D029867:Xenopus Proteins; D014982:Xenopus laevis
chemical_list: C020932:11-cis-retinal-binding protein; D002352:Carrier Proteins; D054834:Lipocalins; C105000:PTGDS protein, Xenopus; D029867:Xenopus Proteins; D012172:Retinaldehyde