cathepsin-g and Pulpitis

Polymorphonuclear neutrophils (PMNs) are found in dental pulp secondary to carious exposures, periodontal disease, or trauma. Lysosomal degranulation of these cells liberates cellular proteases, including elastase (PMN-E) and cathepsin-G (PMN-CG), which produce connective tissue degradation. However, nonspecific pulpal tissue destruction can be modified by a naturally occurring serum protease inhibitor alpha 2-macroglobulin (A2-M). This study relates the concentrations of human PMN-E, PMN-CG, and A2-M in healthy and inflamed pulpal samples. Evaluation of 21 specimens yielded statistically significant differences between healthy and moderate to severely inflamed pulps for all groups (p < 0.05). No significant correlation was detected among human PMN-E, PMN-CG, and A2-M in the healthy tissues (P > 0.05). However, in the moderate to severely inflamed pulps, there was a significant correlation between PMN-CG and A2-M (p < 0.05).

Topics: alpha-Macroglobulins; Cathepsin G; Cathepsins; Dental Pulp; Humans; Leukocyte Elastase; Neutrophils; Pancreatic Elastase; Pulpitis; Reference Values; Serine Endopeptidases

Components of primary (azurophilic) granules of polymorphonuclear leukocytes (PMNs) have been implicated as important mediators in pulpal inflammation. This anatomical study used ultracryoimmunocytochemical techniques and characterized and contrasted the subcellular distributions of human PMN elastase (PMN-E), PMN cathepsin-G (PMN-CG), and alpha-2 macroglobulin (alpha-2M) in healthy and inflamed dental pulps. Inflamed pulpal tissue sections revealed an intense distribution of PMN-E in the extracellular domain throughout the collagen matrix. PMN-E was also localized in the perinuclear cytoplasm of PMNs and distributed in a random fashion. PMN-CG was localized intensely in the intracellular granules of PMNs and observed moderately within the extracellular matrix. Healthy pulpal tissues exposed to PMN-E and PMN-CG antibodies revealed no evidence of PMN infiltration and no specific labeling. alpha-2M, a natural serum inhibitor of PMN-E and PMN-CG, was distributed in an intense fashion within the intravascular compartments of both inflamed and healthy pulpal samples. Immunogold-labeling for alpha-2M was observed in moderate amounts within the extravascular domain of inflamed pulpal samples but only in mild amounts within the same area of healthy tissues. These results suggest that PMN-E and PMN-CG are released to the extracellular matrix of irreversibly inflamed teeth, enabling them to facilitate pulpal connective tissue destruction. Conversely, moderate extravascular labeling for alpha-2M within inflamed samples suggests a physiological attempt at inhibiting the pulpal connective tissue destruction mediated by human PMN-E and PMN-CG.

Topics: alpha-Macroglobulins; Brain Stem; Cathepsin G; Cathepsins; Collagen; Connective Tissue; Cytoplasm; Cytoplasmic Granules; Dental Pulp; Extracellular Matrix; Humans; Immunohistochemistry; Leukocyte Elastase; Microscopy, Electron; Neutrophils; Pancreatic Elastase; Pulpitis; Serine Endopeptidases

Lysosomal granules of polymorphonuclear leukocytes (PMN's) contain proteolytic enzymes and other components important in the regulation of inflammation and the elimination of bacteria or debris associated with pulp disease. However, PMN lysosomal degranulation is nonspecific and can result in destruction of healthy connective tissue adjacent to the areas of damaged or infected tissue. For this study a modified enzyme-linked immunosorbent assay was used to detect the human PMN lysosomal granule products: elastase, cathepsin G, and lactoferrin. Evaluation of 55 pulp samples yielded a statistically significant difference (p less than 0.05) among the levels of elastase and lactoferrin in normal and moderate to severely inflamed pulps. Although cathepsin G levels were increased, there was no statistical significance (p greater than 0.05) among groups. The results indicate that a modified enzyme-linked immunosorbent assay technique can be used to measure PMN lysosomal granule components in dental pulp tissues. Additionally, elastase and lactoferrin levels appear to be valid diagnostic markers of advanced dental pulp disease.

Topics: Biomarkers; Cathepsin G; Cathepsins; Dental Pulp; Enzyme-Linked Immunosorbent Assay; Humans; Lactoferrin; Lysosomes; Neutrophils; Pancreatic Elastase; Pulpitis; Serine Endopeptidases