Arthur A. Decarlo

TL;DR: The present review discusses in detail the primary structures and the overlapping yet distinct substrate specificities of MMPs as well as the mode of activation of the unique MMP precursors.

TL;DR: It is demonstrated that a proteinase isolated from the periodontopathogen Porphyromonas gingivalis can activate MMP-1, MMPs-3, and M MP-9 and can catalyze the superactivation of Mmp-1 by MMP to describe a mode of virulence that involves activation of host-degradative enzymes.

TL;DR: Cysteine proteinases from P. gingivalis appear to be multidomain proteins with functions for hemagglutination, erythrocyte lysis, proteolysis, and heme binding, as demonstrated here.

TL;DR: It is demonstrated that in the presence or absence of serum, gingipains were able to hydrolyze IL- 12 and reduce the IL-12-induced IFN-γ production from CD4+ T cells, however, the induction ofIL-12 receptors on T cells by gedipains did not correlate with the enhancement of IFN -γ production.

TL;DR: It is suggested that chitosan scaffolds containing plasmid DNA encoding VEGF189 and perlecan domain I have the potential to induce angiogenesis and wound healing.