Bis{1-[(1H-benzimidazol-1-yl)methyl-κN 3]-1H-1,2,3,4-tetra­zole}silver(I) nitrate

In the title salt, [Ag(C9H8N6)2]NO3, the central AgI atom is linearly coordinated by the N atoms [171.97 (8)°] from two 1-[(benzimidazol-1-yl)meth­yl]-1H-1,2,3,4-tetra­zole ligands. The benzimidazole rings in adjacent mol­ecules are parallel with an average inter­planar distance of 3.461 Å; adjacent mol­ecules are linked through N—H⋯O hydrogen bonds into a linear chain along the b-axis direction

Gastric adenocarcinoma of the fundic gland: A review of clinicopathological characteristics, treatment and prognosis

Gastric adenocarcinoma of the fundic gland is a rare, well-differentiated gastric cancer entity, and very few patients transition to poorly differentiated tubular adenocarcinoma during progression. Gastric adenocarcinoma of the fundic gland originates from the mucosa of the gastric fundic gland, usually without chronic gastritis or intestinal metaplasia. Histologically, the tumor cells are closely arranged to form anastomosing tubular glands, and more than 95% of tumor cells differentiate towards chief cells. Most gastric adenocarcinoma of the fundic gland cases are characterized by submucosal involvement, but the tumor volume is usually small, with lymphatic and vascular invasion rarely observed. Therefore, endoscopic submucosal dissection can be an ideal treatment, leading to a favorable prognosis, and recurrence and metastasis of the disease are uncommon

Tetra­aqua­{1-[(1H-1,2,3-benzotriazol-1-yl)meth­yl]-1H-1,2,4-triazole}sulfato­zinc(II) dihydrate

In the title complex, [Zn(SO4)(C9H8N6)(H2O)4]·2H2O, the ZnII ion is six-coordinated by one N atom from a 1-[(1H-1,2,3-benzotriazol-1-yl)meth­yl]-1H-1,2,4-triazole ligand and five O atoms from one monodentate sulfate anion and four water mol­ecules in a distorted octa­hedral geometry. The sulfate tetra­hedron is rotationally disordered over two positions in a 0.618 (19):0.382 (19) ratio. In the crystal, adjacent mol­ecules are linked through O—H⋯O and O—H⋯N hydrogen bonds involving the cation, the anion, and the coordinated and uncoordinated water mol­ecules into a three-dimensional network

Diaqua­[5,5′-dicarb­oxy-2,2′-(propane-1,3-di­yl)bis­(1H-imidazole-4-carboxyl­ato)]manganese(II)

The complex mol­ecule of the title compound, [Mn(C13H10N4O8)(H2O)2] or [Mn(H4pbidc)(H2O)2] (H6pbidc = 2,2′-(propane-1,3-di­yl)bis­(1H-imidazole-4,5-dicarb­oxy­lic acid), has 2 symmetry with the twofold rotation axis running through the Mn2+ cation and the central C atom of the propanediyl unit. The cation is six-coordinated by two N atoms and two O atoms from one H4pbidc2− anion and two water O atoms in a considerably distorted octa­hedral coordination. In the crystal, adjacent mol­ecules are linked through O—H⋯O and N—H⋯O hydrogen bonds into a three-dimensional network

catena-Poly[[(acetato-κ2 O,O′)(methanol-κO)cadmium(II)]-μ-[1,2-bis­(1H-benzimid­azol-2-yl)ethane]-κ2 N 3:N 3′-[(acetato-κ2 O,O′)(methanol-κO)cadmium(II)]-di-μ-chlorido]

In the title complex, [Cd2(CH3COO)2Cl2(C16H14N4)(CH3OH)2]n, the CdII atom is six-coordinated by one N atom from a centrosymmetric bridging 1,2-bis­(2,2′-1H-benzimidazol-2-yl)ethane (bbe) ligand, two O atoms from a chelating acetate ligand, one O atom from a methanol mol­ecule and two bridging Cl atoms in a distorted octa­hedral geometry. The CdII atoms are connected alternately by the Cl atoms and bbe ligands, leading to a chain along [001]. These chains are further linked by O—H⋯O hydrogen bonds. Intra­chain N—H⋯O hydrogen bonds are observed

A new AgI complex based on 1-[(1H-benzimidazol-1-yl)meth­yl]-1H-1,2,4-triazole

In the title complex, bis­{μ-1-[(1H-benzimidazol-1-yl)meth­yl]-1H-1,2,4-triazole}disilver(I) dinitrate, [Ag2(C10H9N5)2](NO3)2, the AgI ion is nearly linearly coordinated [N—Ag—N angle is 155.72 (14)°] by two 1-[(1H-benzimidazole-1-yl)meth­yl]-1H-1,2,4-triazole (bmt) ligands. In addition, two bmt ligands link two AgI ions, forming a dinuclear unit with an Ag⋯Ag distance of 5.0179 (15) Å. The whole complex is generated by an inversion centre. The dinuclear units and the NO3 − counter-ions are connected by N—H⋯O hydrogen bonds and weak Ag⋯O inter­actions [2.831 (5), 2.887 (5) and 2.908 (5) Å], leading to a three-dimensional structure

Acetato­chlorido[2,2′-(ethane-1,2-di­yl)di-1H-benzimidazole]­copper(II) monohydrate

In the title complex, [Cu(CH3COO)Cl(C16H14N4)]·H2O, the CuII ion is five-coordinated by two N atoms from a 2,2′-(ethane-1,2-di­yl)di-1H-benzimidazole ligand, two O atoms from a chelating acetate ligand and one terminal monodentate Cl atom in a distorted square-pyramidal geometry. In the crystal, adjacent mol­ecules are linked through O—H⋯Cl, N—H⋯Cl, N—H⋯O and O—H⋯O hydrogen bonds into a three-dimensional network

Autophagy and its therapeutic potential in diabetic nephropathy

Diabetic nephropathy (DN), the leading cause of end-stage renal disease, is the most significant microvascular complication of diabetes and poses a severe public health concern due to a lack of effective clinical treatments. Autophagy is a lysosomal process that degrades damaged proteins and organelles to preserve cellular homeostasis. Emerging studies have shown that disorder in autophagy results in the accumulation of damaged proteins and organelles in diabetic renal cells and promotes the development of DN. Autophagy is regulated by nutrient-sensing pathways including AMPK, mTOR, and Sirt1, and several intracellular stress signaling pathways such as oxidative stress and endoplasmic reticulum stress. An abnormal nutritional status and excess cellular stresses caused by diabetes-related metabolic disorders disturb the autophagic flux, leading to cellular dysfunction and DN. Here, we summarized the role of autophagy in DN focusing on signaling pathways to modulate autophagy and therapeutic interferences of autophagy in DN

Interferon regulatory factor-1 together with reactive oxygen species promotes the acceleration of cell cycle progression by up-regulating the cyclin E and CDK2 genes during high glucose-induced proliferation of vascular smooth muscle cells

BACKGROUND: The high glucose-induced proliferation of vascular smooth muscle cells (VSMCs) plays an important role in the development of diabetic vascular diseases. In a previous study, we confirmed that Interferon regulatory factor-1 (Irf-1) is a positive regulator of the high glucose-induced proliferation of VSMCs. However, the mechanisms remain to be determined. METHODS: The levels of cyclin/CDK expression in two cell models involving Irf-1 knockdown and overexpression were quantified to explore the relationship between Irf-1 and its downstream effectors under normal or high glucose conditions. Subsequently, cells were treated with high glucose/NAC, normal glucose/H(2)O(2), high glucose/U0126 or normal glucose/H(2)O(2)/U0126 during an incubation period. Then proliferation, cyclin/CDK expression and cell cycle distribution assays were performed to determine whether ROS/Erk1/2 signaling pathway was involved in the Irf-1-induced regulation of VSMC growth under high glucose conditions. RESULTS: We found that Irf-1 overexpression led to down-regulation of cyclin D1/CDK4 and inhibited cell cycle progression in VSMCs under normal glucose conditions. In high glucose conditions, Irf-1 overexpression led to an up-regulation of cyclin E/CDK2 and an acceleration of cell cycle progression, whereas silencing of Irf-1 suppressed the expression of both proteins and inhibited the cell cycle during the high glucose-induced proliferation of VSMCs. Treatment of VSMCs with antioxidants prevented the Irf-1 overexpression-induced proliferation of VSMCs, the up-regulation of cyclin E/CDK2 and the acceleration of cell cycle progression in high glucose conditions. In contrast, under normal glucose conditions, H(2)O(2) stimulation and Irf-1 overexpression induced cell proliferation, up-regulated cyclin E/CDK2 expression and promoted cell cycle acceleration. In addition, overexpression of Irf-1 promoted the activation of Erk1/2 and when VSMCs overexpressing Irf-1 were treated with U0126, the specific Erk1/2 inhibitor abolished the proliferation of VSMCs, the up-regulation of cyclin E/CDK2 and the acceleration of cell cycle progression under high glucose or normal glucose/H(2)O(2) conditions. CONCLUSIONS: These results demonstrate that the downstream effectors of Irf-1 are cyclin E/CDK2 during the high glucose-induced proliferation of VSMCs, whereas they are cyclin D1/CDK4 in normal glucose conditions. The Irf-1 overexpression-induced proliferation of VSMCs, the up-regulation of cyclin E/CDK2 and the acceleration of cell cycle progression are associated with ROS/Erk1/2 signaling pathway under high glucose conditions

Inhibition of GABAergic Neurons and Excitation of Glutamatergic Neurons in the Ventrolateral Periaqueductal Gray Participate in Electroacupuncture Analgesia Mediated by Cannabinoid Receptor

Although electroacupuncture (EA) has become a worldwide practice, little is understood about its precise target in the central nervous system (CNS) and the cell type-specific analgesia mechanism. In the present study, we found that EA has significant antinociceptive effects both in inflammatory and neuropathic pain models. Chemogenetic inhibition of GABAergic neurons in the ventrolateral periaqueductal gray (vlPAG) replicated the effects of EA, whereas the combination of chemogenetic activation of GABAergic neurons and chemogenetic inhibition of glutamatergic neurons in the vlPAG was needed to reverse the effects of EA. Specifically knocking out CB1 receptors on GABAergic neurons in the vlPAG abolished the EA effect on pain hypersensitivity, while specifically knocking out CB1 receptors on glutamatergic neurons attenuated only a small portion of the EA effect. EA synchronously inhibits GABAergic neurons and activates glutamatergic neurons in the vlPAG through CB1 receptors to produce EA-induced analgesia. The CB1 receptors on GABAergic neurons localized in the vlPAG was the basis of the EA effect on pain hypersensitivity. This study provides new experimental evidence that EA can bidirectionally regulate GABAergic neurons and glutamatergic neurons via the CB1 receptors of the vlPAG to produce analgesia effects