Canagliflozin could improve the levels of renal oxygenation in newly diagnosed type 2 diabetes patients with normal renal function.

Objective: To evaluate the effects of canagliflozin on the renal oxygen level and blood perfusion in newly diagnosed type 2 diabetes mellitus (T2DM) patients with normal renal function.

Methods: We conducted a prospective, randomised, and drug-controlled trial to determine the reno-protective effect exerted by canagliflozin in newly diagnosed T2DM patients with normal renal function using blood oxygen level-dependent magnetic resonance imaging (BOLD-MRI) and arterial spin labelling MRI (ASL-MRI). This provides an experimental basis for a first-line of defence for the prevention of diabetic nephropathy.

A novel allosteric site in casein kinase 2α discovered using combining bioinformatics and biochemistry methods.

Casein kinase 2 (CK2) is a highly pleiotropic serine-threonine kinase, which catalyzed phosphorylation of more than 300 proteins that are implicated in regulation of many cellular functions, such as signal transduction, transcriptional control, apoptosis and the cell cycle. On the other hand, CK2 is abnormally elevated in a variety of tumors, and is considered as a promising therapeutic target. The currently available ATP-competitive CK2 inhibitors, however, lack selectivity, which has impeded their development in cancer therapy.

Annonaceous acetogenin mimic AA005 induces cancer cell death via apoptosis inducing factor through a caspase-3-independent mechanism.

Background: Annonaceous acetogenins are a family of natural products with antitumor activities. Annonaceous acetogenin mimic AA005 reportedly inhibits mammalian mitochondrial NADH-ubiquinone reductase (Complex I) and induces gastric cancer cell death. However, the mechanisms underlying its cell-death-inducing activity are unclear.

Phosphoproteomics study on the activated PKCδ-induced cell death.

The proteolytic activation of protein kinase Cδ (PKCδ) generates a catalytic fragment called PKCδ-CF, which induces cell death. However, the mechanisms underlying PKCδ-CF-mediated cell death are largely unknown. On the basis of an engineering leukemic cell line with inducible expression of PKCδ-CF, here we employ SILAC-based quantitative phosphoproteomics to systematically and dynamically investigate the overall phosphorylation events during cell death triggered by PKCδ-CF expression.

PKCδ enhances C/EBPα degradation via inducing its phosphorylation and cytoplasmic translocation.

Our previous study has shown that PKCδ stimulates proteasome-dependent degradation of C/EBPα, which partially contributes to PKCδ-mediated apoptosis. However, the molecular interrelationship between these two important proteins is still unknown. In this study, we reported that C/EBPα was phosphorylated by activated PKCδ on three serines, two of which were reported for the first time.

Proteomic identification of common SCF ubiquitin ligase FBXO6-interacting glycoproteins in three kinds of cells.

FBOX6 ubiquitin ligase complex is involved in the endoplasmic reticulum-associated degradation pathway by mediating the ubiquitination of glycoproteins. FBXO6 interacts with the chitobiose in unfolded N-glycoprotein, pointing glycoproteins toward E2 for ubiquitination. Although the glycoprotein-recognizing mechanism of FBXO6 is well documented, its bona fide interacting glycoproteins are largely unknown.