Calcium-dependent interaction of monomeric S100P protein with serum albumin
| Autor: | Sergei E. Permyakov, Marina P. Shevelyova, Eugene A. Permyakov, Maria E. Permyakova, Ramis G. Ismailov, Ekaterina A. Litus, Alexei S. Kazakov |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Serum albumin chemistry.chemical_element Serum Albumin Human Calcium Biochemistry Protein–protein interaction 03 medical and health sciences Structural Biology medicine Humans Bovine serum albumin Protein Structure Quaternary Protein Dimerization Molecular Biology biology Chemistry Calcium-Binding Proteins General Medicine Human serum albumin Neoplasm Proteins body regions Dissociation constant 030104 developmental biology embryonic structures biology.protein Biophysics Protein G Protein Multimerization Protein Binding medicine.drug |
| Zdroj: | International Journal of Biological Macromolecules. 108:143-148 |
| ISSN: | 0141-8130 |
| Popis: | 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 25–50 nM, 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. |
| Databáze: | OpenAIRE |
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