Ear Diseases ; congenital ; Ear, Middle ; abnormalities ; Humans

Twelve anaerobic fungal strains isolated from rumen and faeces of ruminants were screened for xylanase prodution. Isolate A4 strain identified as Neocallimastix had the highest xylanase activity among all isolates. With rice straw, corn straw , peanut straw and filter paper as fermentation substrates, the activities of xylanase by A4 were14.31 U/mL, 11.39 U/mL, 6.99 U/mL, 13.38 U/mL, respectively. The effect of cell-free rumen fluid and yeast extract on xylanase production was tested. The results showed that the concentration level of cell-free rumen fluid had no significant effect on xylanase production. However as yeast extract concentration decreased from 1.0 g/L to 0,5 g/L , the enzyme activity decreased significantly ( P

Measuring the content of soluble reducing sugar, total sugar, soluble protein, guanosine, alkaloids, and succinic acid of Pinellia ternata tuber were measured by anthrone-sulfuric acid colorimetric method, Coomassie brilliant blue method, RP-HPLC, reverse potentiometric titration, acid dye colorimetry, respectively. The result showed that yellow light could promote the growth and development of P. ternata and increase the content of soluble reducing sugar, total sugar, alkaloids, and succinic acid. Under blue light could promote the content of soluble protein and guanosine. Red and yellow light increased the content of chlorophyll a and chlorophyll b, contrastively blue light reduced the content of chlorophyll a and chlorophyll b. White film through the most uniform spectrum was most conducive to the synthesis of chlorophyll a. As single film, blue film, yellow film were more conducive to the synthesis of chlorophyll a, green film and red film had been relatively beneficial to the synthesis of chlorophyll b. Bulbil formed the largest number and the biggest propagation coefficient of P. ternata under red light showed that it could increase the production of P. ternata under red light.
Carbohydrate Metabolism ; radiation effects ; Chlorophyll ; metabolism ; Light ; Pinellia ; growth & development ; metabolism ; radiation effects ; Plant Leaves ; growth & development ; radiation effects ; Plant Proteins ; chemistry ; metabolism ; Quality Control ; Solubility

Adult ; Chemical and Drug Induced Liver Injury ; Dimethylformamide ; poisoning ; Humans ; Male

Adult ; Colonic Neoplasms ; genetics ; DNA, Neoplasm ; genetics ; Female ; Fluorescence ; Humans ; Male ; Microsatellite Instability ; Middle Aged ; Polymerase Chain Reaction ; methods ; Rectal Neoplasms ; genetics

AIM: To investigate the expression of EMMPRIN, MMP1, MMP9 and TIMP2 in retinoblastoma (RB) and normal retinal tissues and their clinicopathological significance and interrelationship.METHODS: Envision immunohistochemistry stainings of EMMPRIN, MMP1, MMP9 and TIMP2 were performed in 30 enucleated eyeballs with retinoblastoma and 15 specimens of normal retina tissue, which had been routinely imbedded with paraffin.RESULTS: Positive rate of EMMPRIN, MMP1, MMP9 expression was higher in RB tissue than in normal control (P<0.01), while TIMP2 expression was lower in RB than in normal retinal tissue (P<0.01). Samples from RB cases of clinical stage Ⅰ, differentiated type, and life span≥2 years had lower positive rate in expression of EMMPRIN, MMP1, MMP9 than those from RB cases of clinical stage Ⅲ, undifferentiated type, and life span<2 years (P<0.05 or P<0.01), while samples from RB cases of differentiated type, optic nerve unaffected, and life span≥2 years had markedly higher positive rate in expression of TIMP2 than those from RB cases of undifferentiated type, optic nerve involved and life span<2 years (P<0.05 or P<0.01). In RB tissues, EMMPRIN, MMP1, MMP9 expressions were highly consistent (P<0.05), whereas TIMP2 expression is highly inconsistent with EMMPRIN, MMP1, MMP9 expression levels (P<0.05).CONCLUSION: The expression level of EMMPRIN, MMP1, MMP9 and TIMP2 may be an important marker of RB progression, invasion and prognosis. There exist internally mutual regulation relations among them.

Lactic acid production and antagonistic property of five strains of LAB isolated from piglet intestine were investigated. The results showed that among all strains L5 exhibited the most rapid production and highest amount of lactic acid in the culture. Consequently, the pH in L5 culture showed the fast decline, with the final value significantly lower than those of other cultures. Strain L1 showed the least production of lactic acid and highest pH among all strains. Culture supernatants of the five strains showed different degrees of antagonistic effect against pathogenic E. coli K88, K99, 987P, O141, E1, and S. aureus. When taking out the effect of the acid, the culture supernatants still showed 22%～53% inhibitory effect, suggesting that the bacteria produced other inhibitory substances apart from lactic acid. The inhibitory effect of the culture supernatant was above 92% after heat treatment and above 85% when treated with proteases.

A 23-year-old man in remission from acute myeloblastic leukemia after allogeneic peripheral blood stem cell transplantation developed peripheral neuropathy presenting as sciatic and peroneal nerve deficits. Electrophysiological tests localized the lesions to the left sciatic and common peroneal nerve. Magnetic resonance imaging revealed nerve thickening and enhancement, while a positron emission tomography-computed tomography scan demonstrated increased fluorodeoxyglucose uptake tracking along the nerve, suggesting peripheral nerve infiltration. This report demonstrates an unusual presentation of acute leukemia relapse presenting as focal neuropathy

OBJECTIVETo observe the effect on infantile allergic cough with Minkeqing oral liquid (Minkeqing) and to study its cell molecular biologic mechanism.

METHODThe rat model was induced by inhalating ovalbumin; then the effects of Minkeqing on IL-6, IL-8, ET-1, TX-B2 in the blood and the bronchoalveolar lavage fluid (BALF) of the animal model were observed.

RESULTMinkeqing could reduce the levels of IL-6,IL-8,ET-1,Tx-B2 in the blood and BALF of the animal model.

CONCLUSIONMinkeqing has the significant function of inhibiting the release of inflammatory mediums.

Animals ; Bronchoalveolar Lavage Fluid ; chemistry ; Cough ; blood ; chemically induced ; metabolism ; Drug Combinations ; Drugs, Chinese Herbal ; isolation & purification ; pharmacology ; Endothelin-1 ; blood ; metabolism ; Hypersensitivity ; blood ; metabolism ; Interleukin-6 ; blood ; metabolism ; Interleukin-8 ; blood ; metabolism ; Male ; Ovalbumin ; Plants, Medicinal ; chemistry ; Random Allocation ; Rats ; Rats, Wistar ; Thromboxane B2 ; blood ; metabolism

Kindlin-2 belongs to a subfamily of FERM domain containing proteins, which plays key roles in activating integrin transmembrane receptors and mediating cell adhesion. Compared to conventional FERM domains, kindlin-2 FERM contains an inserted pleckstrin homology (PH) domain that specifically binds to phosphatidylinositol (3,4,5) trisphosphate (PIP3) and regulates the kindlin-2 function. We have determined the crystal structure of kindlin-2 PH domain at 1.9 Å resolution, which reveals a conserved PH domain fold with a highly charged and open binding pocket for PIP3 head group. Structural comparison with a previously reported solution structure of kindlin-2 PH domain bound to PIP3 head group reveals that upon PIP3 insertion, there is a significant conformational change of both the highly positively charged loop at the entry of the PIP3 binding pocket and the entire β barrel of the PH domain. We propose that such "induced-fit" type change is crucial for the tight binding of PIP3 to anchor kindlin-2 onto the membrane surface, thereby promoting its binding to integrins. Our results provide important structural insight into kindlin-2-mediated membrane anchoring and integrin activation.
Animals ; Crystallography, X-Ray ; Cytoskeletal Proteins ; chemistry ; metabolism ; Humans ; Integrins ; metabolism ; Membrane Proteins ; chemistry ; metabolism ; Mice ; Models, Molecular ; Muscle Proteins ; chemistry ; metabolism ; Neoplasm Proteins ; chemistry ; metabolism ; Protein Conformation