Ligand-Binding Properties of Annexin from Caenorhabditis elegans (Annexin XVI, Nex-1)
- 1 September 2000
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 128 (3) , 377-381
- https://doi.org/10.1093/oxfordjournals.jbchem.a022764
Abstract
Annexins are structurally related proteins that bind phospholipids in a calcium-dependent manner. Recently, we showed that annexins IV, V and VI also bind glycosaminoglycans in a calcium-dependent manner. Annexins are widely distributed from lower to higher eukaryotes, and the nematode Caenorhabditis elegans has been found to contain Nex-1, an annexin homologue. Here, we characterize the ligand-binding properties of Nex-1 using recombinant Nex-1. Nex-1 binds to liposomes containing phosphatidylsering. The apparent Kdwas calculated by Biacore to be 4.4 nM. Compared to mammalian annexins, the Nex-1 phospholipid-binding Specificities were similar whereas the K4 values were one order of magnitude larger. The Nex-1 glycosaminoglycan-binding specificities were investigated by affinity chromatography and solid-phase assays. Nex-1 binds to heparin, heparan sulfate, and chondroitin sulfate but not to chondroitin and chemically N-or O-desulfated heparin. Besides phospholipids, heparan sulfate andor chondroitin (sulfate), probably on perlecan, could be endogenous ligands of Nex-1Keywords
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