The purpose of the study was to investigate expressions of nuclear factor-kappa B (NF-κB) and intercellular cell adhesion molecule-1 mRNA (ICAM-1 mRNA) in the nasal mucosa of allergic rhinitis (AR) patients. Expressions of NF-κB and ICAM-1 mRNA were studied using immunohistochemistry and reverse transcription-PCR (RT-PCR) in AR tissues and corresponding normal nasal mucosa. The correlation between NF-κB and ICAM-1 mRNA was studied using linear correlation analysis. The results of immunohistochemistry showed that expression of NF-κB was significantly up-regulated in the nasal mucosa of AR compared with that in normal tissue (P < 0.01), over-expression of NF-κB p50 was found in the cytoplasm and nucleus (P < 0.01), and NF-κB p65 was mainly expressed in the cytoplasm (P < 0.01). ICAM-1 mRNA was strongly expressed in the nasal mucosa of AR compared with that in normal tissue as shown by RT-PCR (P < 0.01). Up-regulation of ICAM-1 mRNA was significantly correlated with over-expressions of NF-κB p50 and NF-κB p65 (r = 0.8995, P < 0.01; r = 0.7601, P < 0.01). In conclusion, NF-κB plays a key role in AR. Excessively activated NF-κB promotes the transcription of ICAM-1 mRNA. ICAM-1 is related to the pathogenesis and development of AR.

Vitamin A is an essential nutrient element in animal and human growth, which is usually produced by partially acetylating and transforming retinyl diol. The lipase-catalyzed mono-acetylation can obtain pure monoacetate compared with the classical chemistry process. In the current work, the synthesis of vitamin A precursor of Candida antarctica lipase B catalyzed by regioselective monoacetylation of primary hydroxyl of diol in n-hexane was studied. The reaction rate could be described in terms of the Michaelis-Menten equation with a Ping-Pong Bi-Bi mechanism and competitive inhibition by both substrates. A kinetic model was developed, and the apparent kinetic parameters were calculated as: Vmax =8.45 mmol/ (L•h); K m, vinyl =0.997 mmol/L; K m, diol =161.28 mmol/L; K i, diol =287.32 mmol/L; K i, monoacetate=18.13 mmol/L; and K I, diol =427.40 mmol/L. The current study indicates a competitive enzyme inhibition of highly concentrated diol during lipase-catalyzed acetylation reaction. When the diol concentration in the medium was low, there was a good conformity between the experimental and simulated values with 4.73% average relative error.