Ligand-binding properties of annexin from Caenorhabditis elegans (Annexin XVI, Nex-1)

Ayano Satoh, Miwa Hazuki, Kyoko Kojima, Jun Hirabayashi, Isamu Matsumoto

Research output: Contribution to journalArticlepeer-review

19 Citations (Scopus)


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 phosphatidylserine. The apparent K(d) was calculated by Biacore to be 4.4 nM. Compared to mammalian annexins, the Nex-1 phospholipid-binding specificities were similar whereas the K(d) 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 and/or chondroitin (sulfate), probably on perlecan, could be endogenous ligands of Nex-1.

Original languageEnglish
Pages (from-to)377-381
Number of pages5
JournalJournal of biochemistry
Issue number3
Publication statusPublished - Jan 1 2000
Externally publishedYes


  • Annexin
  • Glycosaminoglycan
  • Phospholipid

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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