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 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 language | English |
|---|---|
| Pages (from-to) | 377-381 |
| Number of pages | 5 |
| Journal | Journal of Biochemistry |
| Volume | 128 |
| Issue number | 3 |
| Publication status | Published - 2000 |
| Externally published | Yes |
Fingerprint
Keywords
- Annexin
- Glycosaminoglycan
- Phospholipid
ASJC Scopus subject areas
- Biochemistry
Cite this
Ligand-binding properties of annexin from Caenorhabditis elegans (Annexin XVI, Nex-1). / Satoh, Ayano; Hazuki, M.; Kojima, K.; Hirabayashi, J.; Matsumoto, I.
In: Journal of Biochemistry, Vol. 128, No. 3, 2000, p. 377-381.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ligand-binding properties of annexin from Caenorhabditis elegans (Annexin XVI, Nex-1)
AU - Satoh, Ayano
AU - Hazuki, M.
AU - Kojima, K.
AU - Hirabayashi, J.
AU - Matsumoto, I.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
KW - Annexin
KW - Glycosaminoglycan
KW - Phospholipid
UR - http://www.scopus.com/inward/record.url?scp=0033809287&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033809287&partnerID=8YFLogxK
M3 - Article
C2 - 10965035
AN - SCOPUS:0033809287
VL - 128
SP - 377
EP - 381
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 3
ER -