Matrix metalloproteinases (MMPs) are thought to play important roles during enamel and dentin biomineralization. Previously, membrane type-1 matrix metalloproteinase (MT1-MMP) was localized to the plasma membranes of ameloblasts and odontoblasts of the developing tooth. The best-characterized function of MT1-MMP is to initiate the activation of gelatinase A (MMP-2). Thus, we hypothesized that gelatinase A may also be expressed by developing tooth tissues. A full-length porcine gelatinase A mRNA was isolated by RT-PCR homology cloning of an enamel-organ-specific cDNA library. Northern blot and in situ hybridization analyses demonstrated gelatinase A expression in developing tooth tissues. Immunohistochemical analysis localized gelatinase A close to the plasma membrane of these tissues. Furthermore, recombinant gelatinase A was demonstrated to cleave recombinant amelogenin into several fragments of differing molecular masses. Thus, gelatinase A is expressed by developing tooth tissues along with its activator MT1-MMP and may, therefore, play an important role during tooth development.
Despite good internal consistency of the questionnaire and the recognized validity of the test, people's perception of their masticatory efficiency does not reflect objective efficiency as measured using a clinical test.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.