[HTML][HTML] The heterodimer of the Ca2+-binding proteins MRP8 and MRP14 binds arachidonic acid

M Klempt, H Melkonyan, W Nacken, D Wiesmann… - FEBS letters, 1997 - Elsevier
M Klempt, H Melkonyan, W Nacken, D Wiesmann, U Holtkemper, C Sorg
FEBS letters, 1997Elsevier
The S100 proteins MRP8 and MRP14 have been shown to be expressed by myeloid cells
during inflammatory reactions. Since the majority of S100 proteins exhibit their biological
activity when associated as complex it was investigated whether murine MRP8 and MRP14
form heterodimers and whether this complex may bind lipids of the cell membrane. This is of
particular importance since their anchoring into the plasma membrane is unclear although
upon calcium binding the proteins translocate from the cytoplasma to the cytoskeleton and …
The S100 proteins MRP8 and MRP14 have been shown to be expressed by myeloid cells during inflammatory reactions. Since the majority of S100 proteins exhibit their biological activity when associated as complex it was investigated whether murine MRP8 and MRP14 form heterodimers and whether this complex may bind lipids of the cell membrane. This is of particular importance since their anchoring into the plasma membrane is unclear although upon calcium binding the proteins translocate from the cytoplasma to the cytoskeleton and the plasma membrane. Using recombinant proteins we could show that not the monomers but only the heterodimers specifically bind arachidonic acid. This finding opens new perspectives for the role of MRP8 and MRP14 in acute and chronic inflammatory processes.
Elsevier