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The purpose of this paper is to optimize the course construction and teaching process of psychopharmacology， and analyze the problems in the course of teaching and assessment of psychopharmacology from many aspects. This article is to deeply excavate the space for improvement， and enrich the teaching links by using existing conditions， technology and personnel to enhance the teaching effect and improve the teaching quality， so as to provide references for the reform of similar course teaching.
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Objective:To assess the differences among the expressions of p38 mitogen activated protein kinases (MAPK),phospho-p38MAPK and nuclear factor kappa B (NF-κB)in oral lichen planus (OLP)and oral squamous cell carcinoma (OSCC ).Methods:In the study,53 cases of OLP,45 of OSCC,and 18 controls were obtained and 4-μm-thick histological sections were prepared from formalin-fixed paraffin-embedded tissue blocks.The expressions of p38MAPK,phospho-p38MAPK and NF-κB were detected by immunohistochemistry staining.Furthermore,the expressions of p38MAPK and phospho-p38MAPK were detected using Western blotting analyses in the fresh tissues from 1 1 cases of OLP,5 ca-ses of OSCC,and 7 cases of the controls.Results:p38MAPK was over-expressed in the lamina propria, but lowly expressed in the epithelium in OLP group.Phospho-p38MAPK was lower expressed in OLP group than in OSCC and control groups.NF-κB was found over-expressed in the lamina propria in OLP group.p38MAPK was found expressed in all the samples in the 3 groups.The expression of phospho-p38MAPK was observed in 8 (8/11)OLP samples,5 (5/5)OSCC samples and 4 (4/7)controls by Western blotting,but no significant differences were found within the 3 groups.Conclusion:p38MAPK can be detected in normal oral mucosa,OLP and OSCC.phospho-p38MAPK may be related to the onset and progression of OSCC.The role of p38MAPK in OLP is yet to be revealed.
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<p><b>OBJECTIVE</b>To explore the postburn adhesion properties of polymorphonuclear leukocyte (PMN) onto pulmonary vascular endothelial cells (PVEC) in burn patients with acute lung injury (ALI), so as to determine the role of C5a on PVEC-PMN adhesion.</p><p><b>METHODS</b>Microtubule sucking technique was employed to determine the PVEC-PMN adhesion. The myeloperoxidase (MPO) was also assayed to reflect the magnitude of PVEC-PMN adhesion.</p><p><b>RESULTS</b>The magnitude of PVEC-PMN adhesion increased and the adhesion force increased along with an increase in rh-C5a concentration. Simultaneously, the MPO activity was increased, which could be inhibited by anti-C5aR McAb in a concentration 1:104.</p><p><b>CONCLUSION</b>Both C5a and C5aR participated in PVEC-PMN adhesion, which might be important in the pathogenesis of ALI.</p>
Subject(s)
Humans , Acute Disease , Antibodies, Monoclonal , Pharmacology , Antigens, CD , Allergy and Immunology , Burns , Blood , Cell Adhesion , Cells, Cultured , Complement C5a , Pharmacology , Dose-Response Relationship, Drug , Endothelium, Vascular , Cell Biology , Fetus , Lung , Lung Diseases , Neutrophils , Cell Biology , Peroxidase , Metabolism , Receptor, Anaphylatoxin C5a , Receptors, Complement , Allergy and ImmunologyABSTRACT
Objective To get the antigen of CD7.Methods The extracellular domain of human CD7 was cloned from a plasmid containing the full length of human CD7 cDNA and expressed in pinpoint-xa3 prokaryotic system. Results Analysis with SDS-PAGE and Western-blotting showed that the expressed protein could bind to the anti-CD7 mAb specifically and is about 30 000 u in molecular weight. Conclusion These results paved the way for preparing anti-CD7 engineering antibody.
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Objective To construct staphylococcal enterotoxin D (SED) mutants expressed in Escherichia coli ( E. coli ). Methods The expected mutants were introduced into the SED DNA by megaprimer PCR method. The PCR products ligated to plasmid pTrcHis B were transformed into E. coli DH5? for IPTG induced expression. The target protein was purified by Ni NTA metal affinity chromatography and analyzed by SDS PAGE and immunoblotting. Results The sequencing results showed that mutant nucleic acids were successfully introduced at the expected sites of SED gene. SDS PAGE and immunoblotting confirmed that the proteins of SED mutants were obtained by Ni NTA metal affinity chromatography. The mutants were named as SEDN23A, SEDN23A/H26R, SEDF45A, SEDL59A, SEDN61A, SEDI92A, and SEDF203A, respectively. Conclusion Several SED mutants are successfully constructed, which lays a foundation for subsequent studies of immune recognition of SED.
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Experimental acute serum sickness was produced in 20 rabbits By a sensitizing injection with bovine serum albumin (BSA) through the auricular vein. Five days after the sensitization, ten of the 20 animals were given a total body irradiation of 300 r from a 60Co sourse. No radiation was given to the other 10 animals which served as controls. Blood samples were taken from the rabbits of both groups before and 2 , 4 , 6 , 8 , 10, 12, 14, and 16 days after antigen injection. After the sera were seperated, the concentrations of the circulating immune complexes were determined with the PEG complement consumption test. It was found that the dynamic curves of the concentrations of the circulating immune complexes of the two groups were essentially similar. This result strongly suggests that total body irradiation of gamma rays given five days after the sensitization of an antigen exerts no influence on the formation of the circulating immune complexes though acute radiation sickness is well established.