Human gC1q-R (p33, p32, C1qBP, TAP) is a ubiquitously expressed, multiligand-binding, multicompartmental cellular protein involved in various ligand-mediated cellular responses. Although expressed on the surface of cells, an intriguing feature of the membrane-associated form of gC1q-R is that its translated amino acid sequence does not predict the presence of either a sequence motif compatible with a transmembrane segment or a consensus site for a glycosylphosphatidylinositol anchor. Moreover, the N-terminal sequence of the pre-pro-protein gC1q-R contains a motif that targets the molecule to the mitochondria and as such was deemed unlikely to be expressed on the surface. However, several lines of experimental evidence clearly show that gC1q-R is present in all compartments of the cell, including the extracellular cell surface. First, surface labeling of B lymphocytes with the membrane-impermeable reagent sulfosuccinimidyl 6-(biotinamido)hexanoate shows specific biotin incorporation into the surface-expressed but not the intracellular form of gC1q-R. Second, FACS and confocal laser scanning microscopic analyses using anti-gC1q-R IgG mAb 60.11 or 74.5.2, and the fluorophore Alexa 488-conjugated F(ab')2 goat anti-mouse IgG as a probe, demonstrated specific staining of Raji cells (>95% viable). Three-dimensional analyses of the same cells by confocal microscopy showed staining distribution that was consistent with surface expression. Third, endothelial gC1q-R, which is associated with the urokinase plasminogen activator receptor, and cytokeratin 1 bind 125I-high molecular weight kininogen in a specific manner, and the binding is inhibited dose-dependently by mAb 74.5.2 recognizing gC1q-R residues 204-218. Fourth, native gC1q-R purified from Raji cell membranes but not intracellular gC1q-R is glycosylated, as evidenced by a positive periodic acid Schiff stain as well as sensitivity to digestion with endoglycosidase H and F. Finally, cross-linking experiments using C1q as a ligand indicate that both cC1q-R and gC1q-R are co-immunoprecipitated with anti-C1q. Taken together, the evidence accumulated to date supports the concept that in addition to its intracellular localization, gC1q-R is expressed on the cell surface and can serve as a binding site for plasma and microbial proteins, but also challenges the existing paradigm that mitochondrial proteins never leave their designated compartment. It is therefore proposed that gC1q-R belongs to a growing list of a class of proteins initially targeted to the mitochondria but then exported to different compartments of the cell through specific mechanisms which have yet to be identified. The designation 'multifunctional and multicompartmental cellular proteins' is proposed for this class of proteins.

Receptor-interacting protein kinase 3 (RIP3) is a member of the RIP Ser/Thr kinase family, plays an important role in regulating cell survival, cell apoptosis and cell necrosis. However, the role of RIP3 in the carcinogenesis of colorectal cancer is still poorly understood.We used quantitative PCR and Western blot analysis to examine RIP3 expression in primary colorectal cancer and paired normal colorectal mucosa. RIP3 clinicopathological significance was assessed by immunohistochemical staining in 112 cases of primary colorectal cancer paired with noncancerous tissues. The biological function of RIP3 overexpression was measured by CCK8 assay and plate colony formation assay. Dual staining with fluorescent Annexin V and propidium iodide (PI) was used to discriminate apoptotic or necrotic cell death.RIP3 expression was significantly lower in colorectal cancer and associated with T stage, M stage and AJCC stage. Cox proportional hazard models showed that RIP3 expression was an independent prognostic factor for overall survival and disease-free survival in patients with colorectal cancer. Overexpression of RIP3 significantly suppressed the proliferation of colorectal cancer cells in vitro.Our results suggest that RIP3 may function as a novel prognostic indicator after surgery and play a suppressive role in the colorectal carcinogenesis.

Al/LiF cathode/organic is known to form an excellent interface for electron injection into the organic active layer, resulting in excellent performing organic light-emitting diodes (OLEDs). Here, the chemical structure of the interface between the Al/LiF bilayer cathode and tris (8-hydroxyquinoline) aluminum (Alq) of working OLED devices was investigated by using x-ray photoelectron spectroscopy (XPS). Using a in situ peel-off technique, we are able to characterize the buried interface structure without disturbing the chemical states of each element probed. The data show that there are two types of F at the interface; one is attributed to LiF and the other to F attached to the Alq. This F-doped Alq layer could induce a downshift in molecular orbital levels and thus leads to a reduced electron injection barrier. XPS depth profile results show significant O diffusion through Al layer to the interface, and the diffusion of O ends abruptly at the Al/LiF interface.

To investigate the impact of the linker on the electronic and photophysical properties of diboryl compounds, three new diboryl compounds that contain two BMes2 groups (Mes = mesityl) have been synthesized, including a planar 1,6-(BMes2)2pyrene (1), a V-shaped bis(p-BMes2phenyl)diphenylsilane (4), and a U-shaped 1,8-bis(p-BMes2phenyl)naphthalene (5). For comparison, two previously known compounds, p-(BMes2)2benzene (3) and 1,8-bis(p-BMes2-biphenyl)naphthalene (6), were also investigated. The aromatic linkers in these molecules have been found to have a dramatic impact on the electron-accepting ability and Lewis acidity of the diboryl compounds through their distinct steric and electronic properties. Compound 1 has the most positive reduction potential (E 1/2 red1 = −1.81 V, relative to FeCp2 0/+), while 5 has the most negative reduction potential (E 1/2 red1 = −2.34 V). All compounds are blue emitters with considerable variation of emission energy and efficiencies (e.g., λem = 446, 402, 395 nm, Φ = ∼1.0, 0.17, ∼1.0 for 1, 4, and 5, respectively), and each displays a distinct and selective response toward fluoride ions. Upon addition of fluoride ions, compound 1 displays an unusual red shift and an on−off response in both absorption and fluorescent spectra. By comparing the behavior of 1 to that of the monoboryl compound 1-BMes2pyrene (2) and 3, and with TD-DFT computations on 1 and its fluoride adducts 1F and 1F 2 , it has been found that the peculiar response of 1 toward fluoride ions is caused by the dominance of pyrene π orbitals at the HOMO level of 1F and the relatively low-energy charge transfer from the pyrene ring to the three-coordinate boron center in 1F. The crystal structures of 2, 4, 1F 2 , and 5F 2 were determined by X-ray diffraction analyses. The potential use of compound 1 as either a blue emitter or a bifunctional emitter in OLEDs has been demonstrated by the successful fabrication of double- and triple-layer electroluminescent devices.