Matrix metalloproteinase -2, -8, -9, and -13 in gingival crevicular fluid of short root anomaly patients.

Abstract

The aim of the present observational study was to identify and characterize matrix metalloproteinase (MMP) -2, -8, -9, and -13 in gingival crevicular fluid (GCF) of patients with short root anomaly (SRA). GCF samples collected from affected maxillary central incisors and premolars of five SRA patients and five systemically and periodontally healthy controls were analysed using the zymographic technique for gelatinase A and B (MMP-2 and -9) and by Western blot for collagenase -2 and -3 (MMP-8 and -13). SRA GCF revealed MMP-9 (30 per cent of the total gelatinolytic activity), of which 18 per cent was in 90 kDa proform and 12 per cent in 71-82 kDa active form. Moreover, high-molecular weight complexes (37 per cent) and low-molecular size fragmented (33 per cent) gelatinolytic enzymes were detectable. No MMP-8 or -13 immunoreactivities existed. These results may suggest that activation and complex formation of MMP-9 is characteristic of SRA GCF. From the findings it may be assumed that the GCF of SRA teeth has low collagenolytic resorptive or pathological activity.