[Clinical significance of serum carbohydrate antigen 125 in acute exacerbation of chronic obstructive pulmonary disease].

OBJECTIVE: To study the serum level of carbohydrate antigen 125 (CA125) in patients with acute exacerbation of chronic obstructive pulmonary disease (AECOPD) and its relation with pulmonary hypertension. METHODS: Forty-six patients with AECOPD complicated by pulmonary hypertension, 46 with AECOPD and 38 healthy control subjects were examined for their clinical data, pulmonary function, echocardiographic findings, and serum levels of lung tumor markers and brain natriuretic peptide (BNP). RESULTS: Compared with the healthy control group, COPD patients with or without pulmonary hypertension showed significantly decreased pulmonary function (P<0.05), especially in those with AECOPD and concurrent pulmonary hypertension (P<0.05). Serum CA125 level was obviously higher in AECOPD group than in the healthy control group, and further increased in AECOPD patients with pulmonary hypertension (P<0.05). The levels of lung tumor markers (CEA, NSE, CYFRA and PROGRP) were similar among the 3 groups (P>0.05). The serum level of BNP in patients with AECOPD and concurrent pulmonary hypertension was significantly higher than that in patients with AECOPD (P<0.05). Pearson linear correlation analysis showed that serum CA125 was positively correlated with pulmonary artery systolic pressure and BNP in AECOPD patients with pulmonary hypertension (P<0.01). CONCLUSION: Serum CA125 may serve as a serological index to identify AECOPD patients with pulmonary hypertension.

Modulation of homochiral Dy(III) complexes: single-molecule magnets with ferroelectric properties.

Homochiral Dy(III) complexes: by changing the ligand-to-metal ratio, enantiomeric pairs of a Dy(III) complex of different nuclearity could be obtained. The mono- and dinuclear complexes exhibit characteristics of single-molecule magnets and different slow magnetic relaxation processes. In addition, the dinuclear complexes exhibit ferroelectric behavior, thus representing the first chiral polynuclear lanthanide-based single-molecule magnets with ferroelectric properties.

Two mono- and dinuclear Eu(III) enantiomeric pairs based on chiral bis-bidentate bridging ligands: synthesis, structures, luminescent and ferroelectric properties.

Using the enantiomeric bis-bidentate bridging ligands (+)/(-)-2,5-bis(4,5-pinene-2-pyridyl)pyrazine (L(S)/L(R)) and depending on the ratio control of reactants, two mono- and dinuclear Eu(III)-based enantiomeric pairs with the formulae Eu(dbm)(3)L(R/S)·2H(2)O (L(R) in R-1, L(S) in S-1 and dbm = dibenzoylmethanato) and Eu(2)(dbm)(6)L(R/S)·H(2)O (L(R) in R-2 and L(S) in S-2) have been stereoselectively synthesized and structurally characterized. The circular dichroic (CD) spectra confirmed their chiroptical activities and enantiomeric natures. The homochiral dinuclear species represents the first example of a polynuclear lanthanide ß-diketonate complexes with circular dichroic and crystallographic evidences. The photoluminescent properties studies revealed that both mono- and dinuclear Eu(iii) complexes exhibited the characteristic red emissions of Eu(III) ions in the solid state (at 77 K and 300 K) and CH(2)Cl(2) solution. Notably, the photophysical properties of the mononuclear enantiomers were superior to the dinuclear species. Interestingly, R-2 displayed a ferroelectric property at room temperature, which was not observed for R-1 due to the lack of crystalline polarity. R/S-2 are the first examples of homochiral polynuclear lanthanide complexes with luminescence and ferroelectric properties, being potential multifunctional materials.

[Construction and identification of the expression library of album pollen allergens cDNA].

AIM: To construct and identify the express library of album pollen allergens cDNA. METHODS: Total RNA were extracted from the album pollen with TRIzol reagent and the mRNA was isolate for the amplify followed. A double stranded cDNA (ds cDNA) was synthesized using primers containing Xho I and Poly(dT) sequence by ZAP Express®cDNA synthesis kit. The ds cDNA was modified and purified by gel chromatography, and then the cDNA fragment with the length of more than 400 bp containing sticky ends was obtained. The cDNA fragment was ligated with Uni-ZAP XR vector and subsequently treated with in vitro packaging using phage by ZAP-cDNA express GigapackIII Gold cloning kit. The express library of album pollen cDNA was constructed by in vitro packaging. The recombination rate and the lengths of fragments inserted of the cDNA library were detected by polymerase chain reaction. RESULTS: The titer and the recombination rate of cDNA expression library constructed were 9.7×10(5) and 100%, respectively. The capacity of the library was 4.85 Pfu. The average length of cDNA fragments inserted was about 1.0 kb. CONCLUSION: Based on the capacity of cDNA expression library constructed and the length of cDNA insertion fragments, the cDNA expression library constructed is qualified to screening target cDNA clone, laying the foundation for preparation of gene recombinant allergen pollen vaccine.

[Analysis of the allergenicity and immunogenicity of Psilogramma menephron allergen].

OBJECTIVE: To analyze the allergenicity and immunogenicity of Psilogramma menephron allergen so as to provide the basis for preparing recombinant and standardized allergen vaccines of Psilgramma menephorn. METHODS: The extracts of Psilgramma menephorn were analyzed by SDS-PAGE, and the allergenicity and immunogenicity of the extracts were tested with 9 sera from allergic patients by means of immunoblotting. RESULTS: More than 20 allergen proteins were separated from the extract of Psilgramma menephorn by SDS-PAGE, with the relative molecular weight ranging from 12,000 to 128,000. The relative molecular weight of the allergenic proteins were 74,000 (88.9%), 66,000 (22.2%), 49,000 (22.2%), 36,000 (77.8%), or 25,000 (33.3%), and those of the immunogenic proteins were 79,000 (33.3%), 74,000 (66.7%), 66,000 (22.2%), 49,000 (22.2%), 36,000 (44.4%), or 25,000 (55.6%). CONCLUSION: The relative molecular weight of the major allergenic proteins of Psilgramma menephorn are 74,000 and 36,000, and 74,000 and 25,000 for the major immunogenic proteins. These proteins constitute the major allergenic components for diagnosis and specific treatment of Psilgramma menephorn allergy.

[Purification and analysis of the immunoactivity of humulus pollen allergen].

OBJECTIVE: To purify the humulus pollen allergen and study the allergenicity and immunogenicity of it. METHODS: Crude humulus pollen extracts were purified by gel filtration with Sephadex G-75 and Sephacryl S-200HR. Various fractions of the allergen protein were collected respectively. The molecular weights of protein were confirmed by SDS-PAGE. The inhibition rate and reaction rate with sIgG and sIgE of patient's serum were determined by ELISA inhibition test and western blotting. RESULTS: Two peaks were obtained from crude humulus pollen extracts by gel filtration of Sephadex G-75. The first peak contained most of protein while the second peak contained little protein and lots of pigments. So the second peak was thrown away. P solution which contained the first peak and valley fraction were purified by gel filtration of Sephacryl S-200HR and four components that included the 1st peak, the valley, the 2nd peak and the end fraction were obtained. The results of electrophoresis demonstrated that purified humulus pollen contained more than 20 kinds of protein with the molecular weights ranged from 5.0 x 10(3) to 97.4 x 10(3). The fraction of the 1st peak contained protein with the molecular weights ranged from 43 x 10(3) to 97.4 x 10(3), and the fraction of the valley and the 2nd peak contained protein with the molecular weights ranged from 5.0 x 10(3) to 43 x 10(3). The fraction of the end contained protein with the molecular weights lower than 5.0 x 10(3). The results of ELISA inhibition test showed that the inhibition rate of the 1st peak, the valley, the 2nd peak and the end fraction to sIgG were 68%, 70%, 95%, 5% respectively, and those to sIgE were 25%, 64%, 71%, 11% respectively. The results of western blotting demonstrated that the reaction rate of the 1st peak, the valley, the 2nd peak and the end fraction with sIgG of patients' serum were 65.63%, 78.13%, 87.50%, 6.25% respectively, and those with patients' sIgE were 25.00%, 71. 88%, 84.38%, 15.63% respectively. CONCLUSION: Humulus pollen contained more than 20 kinds of protein. The proteins with molecular weights ranged from 5.0 x 10(3) to 43 x 10(3) were the major allergen with strong allergenicity and immunogenicity. The proteins with molecular weights ranged from 43 x 10(3) to 97.4 x 10(3) were subordinated allergen with strong immunogenicity and weak allergenicity.

[Cloning, screening and sequence analysis of the major allergens of Psilgramma menephorn].

OBJECTIVE: To identify and isolate the genes encoding the allergens of Psilgramma menephorn by screening the cDNA expression library. METHODS: The cDNA expression library of Psilgramma menephorn was constructed in lambdaZAPIIphage, and the library was screened using the sera from the patients allergic to Psilgramma menephorn and those from the rabbits immunized with Psilgramma menephorn extracts. The positive clones were subcloned into pBluescript plas, and the cDNA in the positive clones were amplified with PCR and sequenced. RESULTS AND CONCLUSION: Five positive clones were obtained by immunological screening of 5 x 10(4) recombinants. Sequence analysis showed that the positive clones contained the new genes of Psilgramma menephorn allergens. This success in isolating these genes may facilitate the development of specific immunotherapy against Psilgramma menephorn allergy and further research of allergic diseases.