Enhanced ridge preservation by bone mineral bound with collagen-binding synthetic oligopeptide: a clinical and histologic study in humans

Background: The ridge‐preservation technique has been applied with membrane alone or membrane plus graft. Synthetic peptides, mimicking bioactive growth factor or extracellular matrix protein, have been attempted to provide an active surface of the biomaterials in inducing bone formation while alleviating the limitations of whole protein such as short half‐life, immunologic responses. The aim of the present clinical study is to examine the osteogenic effect of synthetic oligopeptide–coated bone mineral compared to bone graft without peptide when applied with collagen membrane in a ridge‐preservation technique. Methods: Synthetic oligopeptide from the collagen‐binding domain of osteopontin was chemically synthesized and coated onto the surface of bone mineral particulates. Ridge preservations were performed at 44 extraction sites in 42 patients (20 males and 22 females). Analyses of clinical parameters and histomorphometric evaluations were conducted to compare the osteogenic effects of the grafts between baseline and 6 months. Results: In the bone grafts of the control group treated without synthetic peptide, new bone formation was only seen around borders and basal areas. However, new bone was observed broadly in the defects of the test group treated with synthetic peptide–coated bone mineral, as seen not only at peripheries but also in the central and coronal parts of bone cores in the defects. The average percentage of new bone formation was significantly higher in the test group (5.3% ± 8.3% versus 10.4% ± 4.6%). The contact percentages between the graft particles and the new bone were 8.2% ± 11.3% for the control group and 20.4% ± 7.5% for the test group (P <0.05). Conclusions: The ridge‐preservation approach using synthetic oligopeptide–coated bone mineral with collagen membrane effectively prevented the resorption of hard tissue with higher bone‐to‐graft contact, and the oligopeptide‐coated bone may be a choice for ridge‐preservation procedures while assuring new bone formation.     

Effect of Carbohydrate Source on Kanagawa-Type Hemolysis of Vibrio parahaemolyticus

Almost all strains of Vibrio parahaemolyticus produced Kanagawa-type hemolysis on media of high salt content in the presence of fermentable carbohydrates.     

Ionotropic glutamate receptor GluA4 and T‐type calcium channel Cav3.1 subunits control key aspects of synaptic transmission at the mouse L5B‐POm giant synapse

The properties and molecular determinants of synaptic transmission at giant synapses connecting layer 5B (L5B) neurons of the somatosensory cortex (S1) with relay neurons of the posteriomedial nucleus (POm) of the thalamus have not been investigated in mice. We addressed this by using direct electrical stimulation of fluorescently labelled single corticothalamic terminals combined with molecular perturbations and whole‐cell recordings from POm relay neurons. Consistent with their function as drivers, we found large‐amplitude excitatory postsynaptic currents (EPSCs) and multiple postsynaptic action potentials triggered by a single presynaptic action potential. To study the molecular basis of these two features, ionotropic glutamate receptors and low voltage‐gated T‐type calcium channels were probed by virus‐mediated genetic perturbation. Loss of GluA4 almost abolished the EPSC amplitude, strongly delaying the onset of action potential generation, but maintaining the number of action potentials generated per presynaptic action potential. In contrast, knockdown of the Ca_v3.1 subunit abrogated the driver function of the synapse at a typical resting membrane potential of ?70 mV. However, when depolarizing the membrane potential to ?60 mV, the synapse relayed single action potentials. Hence, GluA4 subunits are required to produce an EPSC sufficiently large to trigger postsynaptic action potentials within a defined time window after the presynaptic action potential, while Ca_v3.1 expression is essential to establish the driver function of L5B‐POm synapses at hyperpolarized membrane potentials.     

Dubin-Johnson综合征1例

Dubin-Johnson综合征是一种先天性非溶血性黄疸,在临床中较罕见,需与其他原因所导致的黄疸相鉴别.本文报告了我院1例Dubin- Johnson综合征的诊治情况,有助于加深对该病的认识.     

Effect of acidic fluoride solution on beta titanium alloy wire

The interaction between acidic fluoride solution and beta titanium alloy was investigated to explore the changes that occur in beta titanium alloy by fluoride-containing acetic acid solutions. For this, alloy crystal structure, tensile strength, and elements released from the alloy wires were determined using four solutions (0.05%/pH 6, 0.05%/pH 4, 0.2%/pH 6, and 0.2%/pH 4) for 1 or 3 days. The immersed wire did not form any identifiable new crystal structure compared with the as-received wire. The tensile strength of the immersed wires was significantly reduced compared to the as-received wires in the test solutions if the period of immersion increased from as-received to 3 days. The fractured area of the immersed wire was reduced compared to the as-received one. The dimple pattern at the inner part and a cup-cone morphology at the outer part of the fractured wires were similar in both as-received and immersed wires. After a 3-day immersion, the amount of the released Ti and Mo has much increased for higher NaF concentration and lower pH value. During the long-period orthodontic treatment, both patient and clinical doctor should carefully use the fluoride-containing products to minimize unexpected damage on orthodontic wires.     

Additive effect of TRAIL and p53 gene transfer on apoptosis of human lung cancer cell lines

TRAIL is a cytokine that can induce tumor-specific apoptosis through its specific death receptors (DR4 and DR5) and p53 has been proven to increase the expression of death receptors. To examine their interaction in tumor suppression, p53 and TRAIL genes were inserted in recombinant adenovirus vectors and transferred simultaneously into non-small cell lung cancer cell lines (NCI-H157, NCI-H358, NCI-H460 and A549). Western blot assay demonstrated production of TRAIL protein in NCI-H157 and A549 cell lines. Increased expressions of DR4 and DR5 of NCI-H157 and DR4 of A549 after p53 overexpression were confirmed by flow cytometry. p53 or TRAIL gene transfer increased sub-G1 fraction in cell cycle analysis and inhibited the tumor growth dose-dependently and the degree was potentiated by co-transfer. But isobologram analysis indicated an additive effect. Together, these data indicate that p53 and TRAIL interact additively on tumor apoptosis despite theoretical synergism.     

Translocation of cellular prion protein to non-lipid rafts protects human prion-mediated neuronal damage

Prions are the causative agents of transmissible spongiform encephalopathies, such as variant Creutzfeldt-Jakob disease in humans. Cellular prion proteins (PrPC) connect with cholesterol- and glycosphingolipid-rich lipid rafts through association of their glycosyl-phosphatidylinositol (GPI) anchor with saturated raft lipids and interaction of their N-terminal regions. Our previous study showed that cellular cholesterol enrichment prevented PrP(106-126)-induced neuronal death. We have now studied the influence of membrane cholesterol in PrP(106-126)-mediated neurotoxicity and identified membrane domains involved in this activity. We found that PrPC is normally distributed in lipid rafts, but high membrane cholesterol levels as a result of cholesterol treatment led to the translocation of PrPC from lipid rafts to non-lipid rafts. Moreover, cholesterol-mediated PrPC translocation protects PrP(106-126)-mediated apoptosis and p-38 activation and caspase-3 activation. In a mitochondrial functional assay including mitochondrial transmembrane potential, cholesterol treatment prevented the loss of mitochondrial potential, translocation of Bax and cytochrome c by prion protein fragment. Our results indicate that modulation of the PrPC location appears to protect against neuronal cell death caused by prion peptides. The results of this study suggest that regulation of membrane cholesterol affects the translocation of PrPC, which in turn regulates PrP(106-126)-induced mitochondrial dysfunction and neurotoxicity.