Jian Wu Li

Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is controlled by sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit IkappaB. A large multiprotein complex, the IkappaB kinase (IKK) signalsome, was purified from HeLa cells and found to contain a cytokine-inducible IkappaB kinase activity that phosphorylates IkappaB-alpha and IkappaB-beta. Two components of the IKK signalsome, IKK-1 and IKK-2, were identified as closely related protein serine kinases containing leucine zipper and helix-loop-helix protein interaction motifs. Mutant versions of IKK-2 had pronounced effects on RelA nuclear translocation and NF-kappaB-dependent reporter activity, consistent with a critical role for the IKK kinases in the NF-kappaB signaling pathway.

Activation of the transcription factor NF-kappaB is controlled by the sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit, IkappaB. We recently purified a large multiprotein complex, the IkappaB kinase (IKK) signalsome, which contains two regulated IkappaB kinases, IKK1 and IKK2, that can each phosphorylate IkappaBalpha and IkappaBbeta. The IKK signalsome contains several additional proteins presumably required for the regulation of the NFkappaB signal transduction cascade in vivo. In this report, we demonstrate reconstitution of IkappaB kinase activity in vitro by using purified recombinant IKK1 and IKK2. Recombinant IKK1 or IKK2 forms homo- or heterodimers, suggesting the possibility that similar IKK complexes exist in vivo. Indeed, in HeLa cells we identified two distinct IKK complexes, one containing IKK1-IKK2 heterodimers and the other containing IKK2 homodimers, which display differing levels of activation following tumor necrosis factor alpha stimulation. To better elucidate the nature of the IKK signalsome, we set out to identify IKK-associated proteins. To this end, we purified and cloned a novel component common to both complexes, named IKK-associated protein 1 (IKKAP1). In vitro, IKKAP1 associated specifically with IKK2 but not IKK1. Functional analyses revealed that binding to IKK2 requires sequences contained within the N-terminal domain of IKKAP1. Mutant versions of IKKAP1, which either lack the N-terminal IKK2-binding domain or contain only the IKK2-binding domain, disrupt the NF-kappaB signal transduction pathway. IKKAP1 therefore appears to mediate an essential step of the NF-kappaB signal transduction cascade. Heterogeneity of IKK complexes in vivo may provide a mechanism for differential regulation of NF-kappaB activation.

AIM: To determine the clinical characteristics of vulvovaginal candidiasis (VVC), the Candida species involved and the antifungal susceptibility of Candida species isolated from patients with VVC. METHODS: Candida organisms were cultured from samples obtained from patients who presented with VVC to the Gynecology Department, Peking University Shenzhen Hospital. Antifungal susceptibility testing was performed using a commercial agar diffusion test. RESULTS: Of the 1,070 cases of VVC reported in this study, 36.5% were uncomplicated VVC, and 63.5% were complicated VVC. Twenty-four patients were identified as having two species of Candida. Candid albicans alone was isolated from 89.5% of cases (n = 958). Candida glabrata was isolated from 85 cases (7.9%), Candida tropicalis from 10 (0.9%), Saccharomyces cerevisiae from eight (0.7%), Candida parapsilosis from six (0.6%), Candida famata from two (0.2%), and Candida krusei from one case (0.1%). All isolates of Candida albicans were susceptible to nystatin. The resistant rate of Candida albicans to azole agents was 0-4.9%. CONCLUSION: Candida albicans was the predominant Candida species isolated from this series of patients with VVC. Resistance of vaginal Candida albicans isolates to antifungal agents was infrequent.

Reflective heating polyester fiber is the fiber prepared by adding nanoparticle with reflecting infrared radiation into the polyester. The human body loses 60% of the total heat by heat radiation, but reflective heating fiber can reflect the body's infrared radiation back to the human body to minimize the loss of heat. In this paper, the purchased GTO powder is modified by silane coupling agent KH560, which is added into PET as a reflective heating powder, and PET fiber containing different content of GTO(0.3wt%,0.6wt%,0.9wt%) is prepared through adding masterbatch method. The particle size test shows that the average size of GTO powder modified by KH560 is about 180nm and the distribution is narrow, which meets the basic requirements of spinning. Through the SEM analysis of PET fibers cross-section, it is found that the GTO powder modified by KH560 were dispersed well in the PET substrate. The results of DSC and mechanical tests show that the fiber with 0.6wt% content of GTO powder have the improved elongation and the crystallinity degree. For the infrared thermal imaging and UV-VIS-NIR tests of the fabric, with the increase of the proportion of powder the infrared emissivity and reflectivity of the fabric increased, the warmth retention is also improved.