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    Keywords: CANCER ; CELLS ; EXPRESSION ; tumor ; TUMOR-CELLS ; CELL ; Germany ; human ; GENE-EXPRESSION ; PROTEIN ; PROTEINS ; NF-KAPPA-B ; TUMOR-NECROSIS-FACTOR ; AP-1 ; CARCINOGENESIS ; COMPARATIVE GENOMIC HYBRIDIZATION ; SQUAMOUS-CELL CARCINOMA ; GLYCATION END-PRODUCTS ; RAGE ; NF-kappa B ; TUMOR CELLS ; inflammation ; CALCIUM-BINDING PROTEINS ; CALCIUM-BINDING PROTEIN ; HUMAN CANCER ; LEVEL ; TUMOR-CELL ; MICROVASCULAR ENDOTHELIAL-CELLS ; chronic inflammation ; CALCIUM-BINDING ; function ; S100 ; HUMAN CANCERS ; CANCERS ; MALIGNANCY-ASSOCIATED REGIONS ; TRANSENDOTHELIAL MIGRATION
    Abstract: Calprotectin (S100A8/A9), a heterodimer of the two calcium-binding proteins S100A8 and S100A9, was originally discovered as immunogenic protein expressed and secreted by neutrophils. Subsequently, it has emerged as important pro-inflammatory mediator in acute and chronic inflammation. More recently, increased S100A8 and S100A9 levels were also detected in various human cancers, presenting abundant expression in neoplastic tumor cells as well as infiltrating immune cells. Although, many possible functions have been proposed for S100A8/A9, its biological role still remains to be defined. Altogether, its expression and potential cytokine-like function in inflammation and in cancer suggests that S100A8/A9 may play a key role in inflammation-associated cancer. (c) 2006 Elsevier Inc. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16846592
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