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Hepatic epithelioid hemangioendothelioma (HEHE) is a rare category of vascular tumor with uncertain malignant potential. It commonly presents nonspecific and variable clinical manifestations, ranging from asymptomatic to hepatic failure. In addition, laboratory measurements and imaging features also lack specificity in the diagnosis of HEHE. The aim of the present study is to highlight the dilemma and challenges in the preoperative diagnosis of HEHE, and to enhance awareness of the range of hepatobiliary surgery available in patients with multiple hepatic nodular lesions on imaging. In these patients, HEHE should at least be considered in the differential diagnosis.

A new hydrophilic polyhydric corrole (1) and its Ga(III) complex (1-Ga) were synthesized and characterized. Corroles 1 and 1-Ga bind to calf thymus DNA externally and exhibit remarkable photonuclease-like activity. Singlet oxygen (1O2) was identified as the reactive oxygen species involved. These corroles also exhibit significant photocytotoxicity against HeLa, A549, BEL-7402 and HepG2 tumor cell lines. They mainly accumulated in the nuclei of tumor cells. ROS-mediated mitochondrial damage and intracellular DNA disintegration contributed to the observed photodynamic activity.

A water-soluble cationic gallium corrole, 5,10,15-tris(N-methyl-4-pyridyl)corrolatogallium(III) (3), was prepared and characterized. The photocytotoxicity of 3 was investigated using Hep G2 cancer cell line. Upon treatment with corrole 3 and irradiation, fragmentation of tumor cell nuclei was observed, which led to apoptosis. Flow cytometric analysis clearly showed the efficient induction of apoptotic cell death, and corrole 3 exhibited high photocytotoxicity towards Hep G2 cancer cells (IC50 = 60 nM). Furthermore, the binding behavior of corrole 3 with c-MYC G-quadruplex DNA, a potent target for antitumor drugs, was investigated using spectroscopic methods and molecular docking simulation. Copyright © 2015 John Wiley & Sons, Ltd.

The DNA binding of amphiphilic iron(III) 2,17-bis(sulfonato)-5,10,15-tris(pentafluorophenyl)corrole complex (Fe–SC) was studied using spectroscopic methods and viscosity measurements. Its nuclease-like activity was examined by using pBR322 DNA as a target. The interaction of Fe–SC with human serum albumin (HSA) in vitro was also examined using multispectroscopic techniques. Experimental results revealed that Fe–SC binds to ct-DNA via an outside binding mode with a binding constant of 1.25 × 104 M–1. This iron corrole also displays good activity during oxidative DNA cleavage by hydrogen peroxide or tert-butyl hydroperoxide oxidants, and high-valent (oxo)iron(V,VI) corrole intermediates may play an important role in DNA cleavage. Fe–SC exhibits much stronger binding affinity to site II than site I of HSA, indicating a selective binding tendency to HSA site II. The HSA conformational change induced by Fe–SC was confirmed by UV/Vis and CD spectroscopy. Copyright © 2015 John Wiley & Sons, Ltd.