Revealing novel telomere proteins using in vivo cross-linking, tandem affinity purification, and label-free quantitative LC-FTICR-MS.

Telomeres are DNA-protein structures that protect chromosome ends from the actions of the DNA repair machinery. When telomeric integrity is compromised, genomic instability ensues. Considerable effort has focused on identification of telomere-binding proteins and elucidation of their functions.

SCKs as nanoparticle carriers of doxorubicin: investigation of core composition on the loading, release and cytotoxicity profiles.

SCK nanoparticles having differing core thermal characteristics were designed and evaluated as thermoresponsive drug delivery systems of doxorubicin for the killing of cancerous cells.

Alternative lengthening of telomeres (ALT) and chromatin: is there a connection?

The acquisition of cellular immortality is a critical step in the tumorigenic process that requires stabilization of the telomeres, nucleoprotein structures at the termini of chromosomes. While the majority of human tumors stabilize their telomeres through activation of telomerase (hTERT), a significant portion (10-15%) utilize a poorly understood alternative mechanism of telomere maintenance referred to as ALT (Alternative Lengthening of Telomeres). Strikingly, the ALT mechanism is more prevalent in tumors arising from tissues of mesenchymal origin than in those of epithelial origin.

Nurse driven protocol for head injured patients on warfarin.

The trauma quality improvement committee at our facility identified a significant number of patients on warfarin presenting to the emergency center after minor head trauma that subsequently expired from their intracranial hemorrhage prior to appropriate intervention. An analysis of this patient population identified multiple areas of delay. A collaborative effort between the emergency center nurses and the trauma service personnel resulted in a formal protocol to address each component of delay and expedite the process.

Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin.

To elucidate the mechanisms of cuproprotein biosynthesis in the secretory pathway, a polyclonal antiserum was generated against hephaestin, a multicopper oxidase essential for enteric iron absorption. Immunoblot analysis and pulse-chase metabolic labeling revealed that hephaestin is synthesized as a single-chain polypeptide modified by N-linked glycosylation to a mature 161-kDa species. Cell surface biotinylation and immunofluorescent studies of polarized, differentiated colon carcinoma cells detected hephaestin on the basolateral surface under steady-state conditions.