S100A12 Is Expressed Exclusively by Granulocytes and Acts Independently from MRP8 and MRP14

MRP8 AND MRP14 CONTROL MICROTUBULE REORGANIZATION DURING TRANSENDOTHELIAL MIGRATION OF PHAGOCYTES. running title: MRP8/MRP14 complexes and migration of phagocytes

Expression of MRP8 and MRP14 by macrophages is a marker for severe forms of glomerulonephritis.

Expression of two S100 proteins, myeloid related protein (MRP)8 and MRP14, as well as their complex formation indicate proinflammatory properties of macrophages. We analyzed if the different forms of glomerulonephritis (GN) are associated with the appearance of certain phenotypes of infiltrating macrophages characterized by expression of MRP8 and MRP14 as well as their complex formation. Immuno...

Implication of extracellular zinc exclusion by recombinant human calprotectin (MRP8 and MRP14) from target cells in its apoptosis-inducing activity.

BACKGROUND Calprotectin is a calcium-binding and zinc-binding protein complex that is abundant in the cytosol of neutrophils. This factor is composed of 8 and 14 kDa subunits, which have also been termed migration inhibitory factor-related proteins MRP8 and MRP14. We previously reported that rat calprotectin purified from inflammatory neutrophils induces apoptosis of various tumor cells or norm...

MRP8 and MRP14 control microtubule reorganization during transendothelial migration of phagocytes.

MRP14 (S100A9) is the major calcium-binding protein of neutrophils and monocytes. Targeted gene disruption reveals an essential role of this S100 protein for transendothelial migration of phagocytes. The underlying molecular mechanism comprises major alterations of cytoskeletal metabolism. MRP14, in complex with its binding partner MRP8 (S100A8), promotes polymerization of microtubules. MRP14 i...

MRP8/MRP14 impairs endothelial integrity and induces a caspase-dependent and -independent cell death program.

Activated phagocytes express considerable amounts of MRP8 and MRP14, 2 calcium-binding S100 proteins forming stable heterodimers that are specifically secreted at inflammatory sites in many diseases. We previously reported that treatment of human microvascular endothelial cells with purified MRP8/MRP14 leads to loss of endothelial cell contacts. In this study, we demonstrate that MRP8/MRP14 com...