Acupuncture Therapy ; Adult ; Female ; Humans ; Laryngitis ; therapy

Allostasis ; physiology ; Chronic Disease ; General Adaptation Syndrome ; physiopathology ; Humans ; Stress, Psychological ; physiopathology

Acupuncture Therapy ; Aged ; Feeding and Eating Disorders ; therapy ; Humans ; Male

As a tumor suppressor, p53 is activated by numerous cellular and environmental signals, and plays a criticalrole in the cell cycle regulation, cell apoptosis and senenscence. The murine double minute (MDM)2 and double minute mu?rine 4 (MDMX) are two important regulators. MDMX is a p53 binding protein with strong sequence homology to MDM2, but lacks ubiquitin ligase activity, and which is unable to target p53 for proteasomal degradation. MDMX regulates p53 activity through its binding with p53 and its postranscriptional modification. MDMX in the closed and open structure binds to p53 to regulate its activity. As the main partner of MDMX, casein kinase 1 alpha (CK1α) disrupts the intramolecular binding in MD?MX in the cooperation to regulate p53 activity. The process of MDMX and CK1αin the regulation of p53 is multi-step and complicated. In this paper the mechanism of MDMX and CK1αin the regulation of p53 protein was reviewed.

OBJECTIVETo investigate the effect of midazolam on human ether-a-go-go (hERG) K+ channels exogenously expressed in human embryonic kidney cells (HEK-293) and the underlying molecular mechanisms.

METHODSWhole-cell patch clamp technique was used to record WT, Y652A and F656C hERG K+ current expressed in HEK-293 cells.

RESULTSMidazolam inhibited hERG K+ current in a concentration-dependent manner, the half-maximum block concentrations (IC50) values were (1.31 ± 0.32) µmol/L. The half-activation voltage (V1/2) were (2.32 ± 0.38) mV for the control and (-1.96 ± 0.83) mV for 1.0 µmol/L midazolam. The half-inactivation voltage (V1/2) was slightly shifted towards negative voltages from (-49.25 ± 0.69) mV in control to (-57.53 ± 0.53) mV after 1.0 µmol/L midazolam (P < 0.05). Mutations in drug-binding sites (Y652A or F656C) of the hERG channel significantly attenuated the hERG current blockade by midazolam.

CONCLUSIONMidazolam can block hERG K+ channel and cause the speed of inactivation faster. Mutations in the drug-binding sites (Y652 or F656) of the hERG channel were found to attenuate hERG current blockage by midazolam.

Dose-Response Relationship, Drug ; Ether-A-Go-Go Potassium Channels ; drug effects ; HEK293 Cells ; Humans ; Midazolam ; pharmacology ; Mutation ; Patch-Clamp Techniques ; Potassium Channel Blockers ; pharmacology

Acupuncture Points ; Acupuncture Therapy ; Adult ; Facial Pain ; therapy ; Female ; Headache ; therapy ; Humans ; Male ; Middle Aged ; Toes

BACKGROUND:Deep venous thrombosis is one of the most common and dangerous complication. There wil be serious consequences for failing to prevent deep venous thrombosis in advance, so we need to evaluate the risk factors of deep venous thrombosis. OBJECTIVE:To evaluate the clinical risk factors for lower limb deep vein thrombosis after total hip arthroplasty. METHODS:Data of 162 patients who were treated from January 2010 to February 2013 in Department of Bone and Joint Surgery, Shenzhen Hospital of Peking University for total hip arthroplasty were analyzed retrospectively. Al patients received ultrasonography on deep veins of lower limb preoperatively and postoperatively 3 and 7 days. Risk factors of deep venous thrombosis were analyzed using Logistic regression analysis in patients undergoing total hip arthroplasty. RESULTS AND CONCLUSION:The selected factors for Logistic regression model contained bone cement prosthesis, age distribution, body mass index, and general anesthesia. Their OR values were 9.215, 11.247, 3.842, 4.825, respectively. They were risk factors for the occurrence of deep venous thrombosis. Above results indicated that use of bone cement prosthesis, age, body mass index>25 kg/m2 and general anesthesia are risk factors for deep venous thrombosis after total hip replacement, so they should cause clinical attention and we should take active measures to prevent them.

Animals ; Cerebral Cortex ; metabolism ; Disease Models, Animal ; Male ; Mice ; Mice, Inbred Strains ; Morphine Dependence ; metabolism ; Neurotrophin 3 ; metabolism ; Prosencephalon ; metabolism

By Silica gel, Sephadex LH-20 and other materials for isolation and purification and by physicochemical methods and spectral analysis for structural identification, 23 compounds were isolated and identified from ethyl acetate portion of alcohol extract solution of Osmanthus fragrans fruits. Their structures were identified as nicotinamide (1), D-allitol (2), 5-hydroxymethyl-2-furancarboxaldehyde (3), acetyloleanolic acid (4), benzoic acid (5), ergosta-7,22-dien-3-one (6), beta-sitosterol (7), borreriagenin (8), cerevistero (9), c-veratroylglycol (10), methyl-2-O-beta-glucopyranosylbenzoate (11), 3', 7-dihydroxy-4'-methoxyisoflavon (12), umbelliferone (13), caffeic acid methyl ester (14), oleanolic acid (15), (-) -chicanine (16), dillapiol (17), 3beta,5alpha, 9alpha-trihydroxyergosta-7-22-dien-6-one (18), 2alpha-hydroxy-oleanolic acid (19), betulinic acid (20), betulin (21), 3, 3'-bisdemethylpinoresinol (22), and lupeol (23). All compounds were isolated from the osmanthus fruit for the first time. Except for compounds 4, 7, 15, 19, 23, the rest ones were isolated from the this plant for the first time.
Drugs, Chinese Herbal ; chemistry ; Fruit ; chemistry ; Oleaceae ; chemistry

Adult ; Aluminum Silicates ; toxicity ; Humans ; Middle Aged ; Mining ; Occupational Exposure ; Prevalence ; Silicosis ; epidemiology