Multidisciplinary Approach to Complicated Crown-root Fracture Treatment: A Case Report.

Treatment of complicated crown-root fractures is one of the most challenging within the various types of dental trauma and requires a multidisciplinary approach. This paper reports the complicated crown-root fracture of a maxillary right central incisor, in which there was esthetic, functional, and biologic (endodontic and biologic width invasion) involvement. A 15-year-old male patient presented to the dental clinic one month after suffering trauma with a complicated crown-root fracture on tooth 8. The patient had previously undergone endodontic treatment and was sent to have periodontal surgery to reestablish the biological width on the palatal surface. Following the surgery, a fiberglass post was cemented, and the fragment was reattached. This approach allows the exposure of the cervical margin, adequate isolation, and subsequent fragment reattachment in the same clinical appointment. Fragment reattachment is a viable approach as it is a simple and conservative procedure that restores the natural esthetic of the tooth and has superior resistance compared to a composite restoration. The patient's cooperation in understanding the limitations of the treatment and maintaining adequate oral hygiene are very important to achieving a good prognosis of the case. After a 2-year clinical and radiographic follow-up period, the clinical protocol was found to be successful, and the tooth remained functional, esthetically favorable and asymptomatic.

A serine proteinase inhibitor isolated from Tamarindus indica seeds and its effects on the release of human neutrophil elastase.

Proteinaceous inhibitors with high inhibitory activities against human neutrophil elastase (HNE) were found in seeds of the Tamarind tree (Tamarindus indica). A serine proteinase inhibitor denoted PG50 was purified using ammonium sulphate and acetone precipitation followed by Sephacryl S-300 and Sephadex G-50 gel filtration chromatographies. Inhibitor PG50 showed a Mr of 14.9 K on Sephadex G-50 calibrated column and a Mr of 11.6 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. PG50 had selective activity while cysteine proteinases (papain and bromelain) and serine proteinases (porcine pancreatic elastase and bovine chymotrypsin) were not inhibited, it was strongly effective against serine proteinases such as bovine trypsin and isolated human neutrophil elastase. The IC50 value was determined to be 55.96 microg.mL-1. PG50 showed neither cytotoxic nor haemolytic activity on human blood cells. After pre-incubation of PG50 with cytochalasin B, the exocytosis of elastase was initiated using PAF and fMLP. PG50 exhibited different inhibition on elastase release by PAF, at 44.6% and on release by fMLP, at 28.4%. These results showed that PG50 preferentially affected elastase release by PAF stimuli and this may indicate selective inhibition on PAF receptors.