S100A9

(redirected from MRP14)

S100A9

A gene on chromosome 1q21 that encodes a member of the S100 family of proteins, which contain 2 EF-hand calcium-binding motifs and as a group regulate cell cycle progression and differentiation and other cellular processes. S100A9 has antimicrobial activity against bacteria and fungi and provides resistance to invasion by pathogenic bacteria, and it upregulates transcription of genes under the control of NF-kappa-B; it is linked to the endotoxic shock response to bacterial lipopolysaccharide. S100A9 promotes tubulin polymerisation and macrophage and granulocyte migration and infiltration into wound sites; it is a pro-inflammatory mediator and upregulates IL8 release and cell surface expression of ICAM1. Extracellular S100A9 (calprotectin) binds to target cells and promotes apoptosis.
 
Molecular pathology
Altered expression of S100A9 is linked to cystic fibrosis.
References in periodicals archive ?
These proteins include (i) calcium-binding protein MRP14 implicated in several types of cancer; (ii) CD59 overexpressed on tumour cells that enables them to escape from complement-dependent and antibody-mediated immune responses; (iii) Profilin 1, a protein involved in several signaling pathways with cytoplasmic and nuclear ligands, generally secreted into tumour microenvironments during the early progressive stage of tumorigenesis; and (iv) catalase, a member of the enzymatic antioxidative system, whose level is elevated in many human tumours and involved in carcinogenesis and tumour progression (109).
Fales (National Institutes of Health), contributing to an article on the phosphorylation site analysis of MRP14 purified from granulocytes, commenting on proteome analysis, and discussing the analysis of single cells and molecules.
Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 are confirmed by electrospray ionization-mass analysis.
2+]-binding proteins MRP8, MRP14 and their heterodimeric form MRP8/14 in Crohn's disease.
S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14.
Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry.
Fales (National Institutes of Health, Maryland), contributing to an article on the phosphorylation site analysis of MRP14 purified from granulocytes, commenting on proteome analysis, and discussing the analysis of single cells and molecules.
Increased coexpression of CFTR and S100 calcium binding proteins MRP8 and MRP14 mRNAs in cystic fibrosis human tracheal gland cells.
Thus, MRP8 or MRP14 and their heterodimeric complex, MRP8/14, seem to be key proteins in cell-cycle regulation and cell activation with calcium to motivate phagocytosis (14-16).
1), on the other hand, reported that neither MRP8 or MRP14 was detectable in resident macrophages in sections of healthy human tissue, but in acutely inflamed tissue, such as in gingivitis, psoriasis, neurodermatitis, and erythrodermia, MRP14 was present in macrophages of the perivascular infiltrate in 15 of 32 cases analyzed, whereas MRP8 was always absent.
In addition, MRP8 and MRP14 proteins were purified electrophoretically.
The MRP8, MRP14, and MRP8/14 proteins, which were electrophoretically purified from 15% gels by SDS-PAGE in the absence of 2-ME, were used (see Fig.