Matrix metalloproteinases: the most important pathway involved with periodontal destruction

Periodontitis is an infectious disease estimated to occur in approximately a third of adults over the age of 35, being the major cause of adult tooth loss. The tissue destruction seems to be regulated by four major pathways. Plasminogen-dependent, phagocytic, osteoclastic and matrix metalloproteinase pathway. The matrix metalloproteinases (MMPs) pathway seems to be the most relevant in periodontal disease. The purpose of the current study was to review the roles of MMPs on periodontal disease, with emphasis on periodontal ligament and alveolar bone destruction. Particular attention is given on the mechanisms that control MMPs genes transcription, the regulation of protein activity, and the influence of MMP genes polymorphisms in inflammatory diseases.

Identification and characterization of highly conserved antigenic determinants in the laminin molecule

1. Fragments P1 and E8, the results of two different enzymatic digestions of the laminin molecule, represent interaction sites of laminin with specific. By using negative and positive affinity purification of a rabbit antiserum against mouse laminin we have generated antibodies to these two fragments. 2. Antibodies against P1 were able to immunoprecipitate fragment E8 from elastase-digested laminin. By liquid phase competition experiments we demonstrated that the epitopes shared by P1 and E8 are a minor portion of the antigenic determinants of P1. When we checked for the presence of these shared epitopes in the human laminin molecule, they were the major fraction of the interspecies antigenic conservation. 3. A similar approach usisng polyclonal antibodies against human laminin has confirmed these reults. 4. The shared epitopes present in both mouse and human laminin molecules seem to be spatially determined, because antibodies against these sites did not bind to fully denatured laminin. 5. Since human and mouse laminin bind to cell receptors and to other extracellular matrix proteins from both species, we conclude that these antigenic determinants may represent the actual sites for at least some of these interactions