Interactions and possible functional characteristics of Tag7-S100A4 protein complex.
Peptidoglycane-recognizing protein Tag7 formed a complex with S100A4 (a representative of S100 protein family), the apparent dissociation constants in the absence and presence of Ca2+ were 2 x l0(-8) M and 10(-9) M, respectively. Analysis of fluorescence spectra of hydrophobic fluorescent probe 2-toluidinyl naphthalene-6-sulfonate in the presence of S100A4 and Tag7 proteins showed that extensive area or several sites are involved into the complex formation between these proteins. The formation of Tag7-S100A4 complex had virtually no effect on the role of S100A4 in the regulation of intracellular Ca2+ metabolism. Removal of not only Tag7, but also S100A4 from neutrophil conditioned medium reduced lysis of E. coli cell, while addition of the Tag7-S100A4 complex to the medium restored antibacterial activity.
Dukhanina
E A
EA
Russian State Medical University, Moscow, Russia.
Romanova
E A
EA
Dukhanin
A S
AS
Kabanova
O D
OD
Lukyanova
T I
TI
Shatalov
Y V
YV
Yashin
D V
DV
Gnuchev
N V
NV
Sashchenko
L P
LP
D002478:Cells, Cultured; D017077:Culture Media, Conditioned; D016207:Cytokines / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D046912:Multiprotein Complexes / Q000378:metabolism*; D009504:Neutrophils / Q000166:cytology / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins / Q000235:genetics / Q000378:metabolism*
D017077:Culture Media, Conditioned; D016207:Cytokines; D046912:Multiprotein Complexes; C491878:PGLYRP1 protein, human; D011994:Recombinant Proteins; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins; C077591:S100A4 protein, human