Calcium-dependent interaction of monomeric S100P protein with serum albumin.
Int J Biol Macromol
; 108: 143-148, 2018 Mar.
Article
in En
| MEDLINE
| ID: mdl-29175526
ABSTRACT
S100 proteins are multifunctional (intra/extra)cellular mostly dimeric calcium-binding proteins engaged into numerous diseases. We have found that monomeric recombinant human S100P protein interacts with intact human serum albumin (HSA) in excess of calcium ions with equilibrium dissociation constant of 25-50nM, as evidenced by surface plasmon resonance spectroscopy and fluorescent titration by HSA of S100P labelled by fluorescein isothiocyanate. Calcium removal or S100P dimerization abolish the S100P-HSA interaction. The interaction is selective, since S100P does not bind bovine serum albumin and monomeric human S100B lacks interaction with HSA. In vitro glycation of HSA disables its binding to S100P. The revealed selective and highly specific conformation-dependent interaction between S100P and HSA shows that functional properties of monomeric and dimeric forms of S100 proteins are different, and raises concerns on validity of cell-based assays and animal models used for studies of (patho)physiological roles of extracellular S100 proteins.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Calcium-Binding Proteins
/
Calcium
/
Serum Albumin, Human
/
Neoplasm Proteins
Type of study:
Prognostic_studies
Limits:
Humans
Language:
En
Journal:
Int J Biol Macromol
Year:
2018
Document type:
Article