Description
Principle of the Assay: Matrix metalloproteinase 8 (MMP8) also called neutrophil collagenase. Neutrophil collagenase, a member of the family of matrix metalloproteinases, is distinct from the collagenase of skin fibroblasts and synovial cells in substrate specificity and immunologic crossreactivity. MMP8, an enzyme that degrades fibrillar collagens imparting strength to the fetal membranes, is expressed by leukocytes and chorionic cytotrophoblast cells. The human neutrophil collagenase (HNC) cDNA clone has been sequenced and shown to encode a 467-residue protein. Neutrophil collagenase has been found to possess 57% identity with the deduced protein sequence for fibroblast collagenase with 72% chemical similarity. Certain regions of the molecule, including the putative zinc-binding region, are highly conserved. When compared with the published sequence for fibroblast collagenase, neutrophil collagenase contains four additional sites for glycosylation.
Background: Matrix metalloproteinase 8 (MMP8) also called neutrophil collagenase. Neutrophil collagenase, a member of the family of matrix metalloproteinases, is distinct from the collagenase of skin fibroblasts and synovial cells in substrate specificity and immunologic crossreactivity. MMP8, an enzyme that degrades fibrillar collagens imparting strength to the fetal membranes, is expressed by leukocytes and chorionic cytotrophoblast cells. The human neutrophil collagenase (HNC) cDNA clone has been sequenced and shown to encode a 467-residue protein. Neutrophil collagenase has been found to possess 57% identity with the deduced protein sequence for fibroblast collagenase with 72% chemical similarity. Certain regions of the molecule, including the putative zinc-binding region, are highly conserved. When compared with the published sequence for fibroblast collagenase, neutrophil collagenase contains four additional sites for glycosylation