Periimplant diseases : Etiopathogenesis and progression

Use of the implant-supported prosthesis has gained a strong foothold in oral rehabilitation in recent decades. The increasing number of implant restorations has necessitated their long-term maintenance for optimal health. The ubiquitous use of dental implants has been associated with the occurrence of implant failure, one of the most important causes being periimplant infections. Periimplant infection is a condition wherein clinical inflammation of periimplant soft tissue with or without periimplant bone loss is evident. Knowledge of etiology alone determines the treatment and long-term maintenance of implants and periimplant tissue. There is a spate of scientific data exploring the etiologic factors resulting in periimplant infection. In this article, an earnest effort is made to analyze and present contemporary research data

Properties of copper–stainless steel HIP joints before and after neutron irradiation

Protein ubiquitylation is a dynamic post-translational modification that can be reversed by deubiquitylating enzymes (DUBs). It is unclear how the small number of ∼100 DUBs present in mammalian cells regulates the thousands of different ubiquitylation events. Here we analysed annotated transcripts of human DUBs and find ∼300 ribosome-associated transcripts annotated as protein coding, which thus increase the total number of DUBs. Using USP35, a poorly studied DUB, as a case study we provide evidence that alternative isoforms contribute to the functional expansion of DUBs. We show the existence of two different USP35 isoforms that localise to different intracellular compartments and have distinct functions. Our results reveal that isoform 1 is an anti-apoptotic factor that inhibits staurosporine- and TNF-related apoptosis inducing ligand (TRAIL)-induced apoptosis. In contrast, USP35 isoform 2 is an integral membrane protein of the endoplasmic reticulum (ER) present also at lipid droplets. Manipulations of isoform 2 levels cause rapid ER stress likely through deregulation of lipid homeostasis and lead to cell death. Our work highlights how alternative isoforms provide functional expansion of DUBs and sets directions for future research.</jats:p