PMID- 15355353
OWN - NLM
STAT- MEDLINE
DCOM- 20041018
LR  - 20161017
IS  - 0014-2956 (Print)
IS  - 0014-2956 (Linking)
VI  - 271
IP  - 18
DP  - 2004 Sep
TI  - Identification of intracellular target proteins of the calcium-signaling protein 
      S100A12.
PG  - 3765-75
AB  - In this report, we have focused our attention on identifying intracellular 
      mammalian proteins that bind S100A12 in a Ca2+-dependent manner. Using S100A12 
      affinity chromatography, we have identified cytosolic NADP+-dependent isocitrate 
      dehydrogenase (IDH), fructose-1,6-bisphosphate aldolase A (aldolase), 
      glyceraldehyde-3-phosphate dehydrogenese (GAPDH), annexin V, S100A9, and S100A12 
      itself as S100A12-binding proteins. Immunoprecipitation experiments indicated the 
      formation of stable complexes between S100A12 and IDH, aldolase, GAPDH, annexin V 
      and S100A9 in vivo. Surface plasmon resonance analysis showed that the binding to 
      S100A12, of S100A12, S100A9 and annexin V, was strictly Ca2+-dependent, whereas 
      that of GAPDH and IDH was only weakly Ca2+-dependent. To localize the site of 
      S100A12 interaction, we examined the binding of a series of C-terminal truncation 
      mutants to the S100A12-immobilized sensor chip. The results indicated that the 
      S100A12-binding site on S100A12 itself is located at the C-terminus (residues 
      87-92). However, cross-linking experiments with the truncation mutants indicated 
      that residues 87-92 were not essential for S100A12 dimerization. Thus, the 
      interaction between S100A12 and S100A9 or immobilized S100A12 should not be 
      viewed as a typical S100 homo- or heterodimerization model. Ca2+-dependent 
      affinity chromatography revealed that C-terminal residues 75-92 are not necessary 
      for the interaction of S100A12 with IDH, aldolase, GAPDH and annexin V. To 
      analyze the functional properties of S100A12, we studied its action in protein 
      folding reactions in vitro. The thermal aggregation of IDH or GAPDH was 
      facilitated by S100A12 in the absence of Ca2+, whereas in the presence of Ca2+ 
      the protein suppressed the aggregation of aldolase to less than 50%. These 
      results suggest that S100A12 may have a chaperone/antichaperone-like function 
      which is Ca2+-dependent.
CI  - Copyright 2004 FEBS
FAU - Hatakeyama, Takashi
AU  - Hatakeyama T
AD  - Department of Signal Transduction Sciences, Kagawa University Faculty of 
      Medicine, Japan.
FAU - Okada, Miki
AU  - Okada M
FAU - Shimamoto, Seiko
AU  - Shimamoto S
FAU - Kubota, Yasuo
AU  - Kubota Y
FAU - Kobayashi, Ryoji
AU  - Kobayashi R
LA  - eng
PT  - Journal Article
PL  - England
TA  - Eur J Biochem
JT  - European journal of biochemistry
JID - 0107600
RN  - 0 (Annexin A5)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Recombinant Proteins)
RN  - 0 (S100 Proteins)
RN  - EC 1.1.1.41 (Isocitrate Dehydrogenase)
RN  - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Annexin A5/metabolism
MH  - Binding Sites
MH  - Blotting, Western
MH  - Calcium Signaling
MH  - Calcium-Binding Proteins/*metabolism
MH  - Cattle
MH  - Chromatography, Affinity
MH  - Cross-Linking Reagents
MH  - Dimerization
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Escherichia coli/genetics
MH  - Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism
MH  - Humans
MH  - Isocitrate Dehydrogenase/metabolism
MH  - Lung/chemistry
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Precipitin Tests
MH  - Protein Folding
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - S100 Proteins/*chemistry/genetics/*metabolism
MH  - Sequence Analysis, Protein
MH  - Sequence Homology, Amino Acid
MH  - Surface Plasmon Resonance
EDAT- 2004/09/10 05:00
MHDA- 2004/10/19 09:00
CRDT- 2004/09/10 05:00
PHST- 2004/09/10 05:00 [pubmed]
PHST- 2004/10/19 09:00 [medline]
PHST- 2004/09/10 05:00 [entrez]
AID - EJB4318 [pii]
AID - 10.1111/j.1432-1033.2004.04318.x [doi]
PST - ppublish
SO  - Eur J Biochem. 2004 Sep;271(18):3765-75. doi: 10.1111/j.1432-1033.2004.04318.x.