We present a unified quantitative explanation of the temperature dependence of the drift mobilities of photoinjected electrons in naphthalene for all directions and temperatures. The theory proposed is based on a polaronic description of the charge carriers and the calculational scheme employs site-local states. Excellent agreement of the theory and experiment occurs for known and reasonable parameters. PACS numbers: 72.10.Di, 72,20.Dp, 72.80.Le In this Letter we present a resolution of a puzzle ^"^ in the transport of charges in organic solids that has existed for many years. This puzzle consists of the temperature behavior of the mobility of photoinjected electrons in naphthalene. The mobility is independent of temperature in the c' crystallographic direction over the temperature range 100 < T < 300 K and decreases rapidly v^ith an increase in temperature for 30 < T < 100 K. There is also a large anisotropy with respect to crystal orientation in both the magnitude and the temperature behavior of the mobility.While various specific aspects of these measurements have been interpreted qualitatively, no single theoretical model has succeeded in providing simultaneously a description of all of them. Moreover, several theories have been proposed which initially appeared to provide an explanation of the qualitative features present in the experimental observations, but, on closer scrutiny, have been found to be inapplicable. Indeed, it has been recently remarked^ that all theoretical attempts made so far in this direction have essentially failed. In this Letter, we present what we believe to be the first explanation of the behavior of these mobilities, which is internally consistent and compatible with known or estimable parameters.The various theoretical studies that have appeared in the literature include (i) Sumi's librational phonon theory,^ (ii) Reineker, Kenkre, and Kiihne's stochasticLiouville-equation approach,^ (iii) Silbey and Munn's formalism,^^ and (iv) a Boltzmann-equation treatment'' of scattering by acoustical phonons presented by Andersen, Duke, and Kenkre. All these theories have provided a qualitative or partial explanation of the measurements. Upon quantitative application to the data, however, they have been found to be inadequate. The analyses of Reineker, Kenkre, and Kiine^ and of Sumi^ predict the appropriate qualitative behavior but require a phonon frequency which is smaller than the lowest known libration in naphthalene. The Boltzmann-equation treatment,'' while it provides good fits with the data below 100 K in all crystallographic directions, is found to yield mean free paths that are less than a lattice constant for most of the data for the c' direction, and thus fails to be internally consistent. The Silbey-Munn theory'^ is found to result in perturbation parameters which are not consistent with the analysis of the low-temperature mobilities {T < 100 K). For the high-temperature mobilities, it is consistent with the data but requires phonon frequencies that are higher than that of the ...

BackgroundNew biomarkers that replace or are used in conjunction with the current ovarian cancer diagnostic antigen, CA125, are needed for detection of ovarian cancer in the presurgical setting, as well as for detection of disease recurrence. We previously demonstrated the upregulation of leucine-rich alpha-2-glycoprotein-1 (LRG1) in the sera of ovarian cancer patients compared to healthy women using quantitative mass spectrometry.MethodsLRG1 was quantified by ELISA in serum from two relatively large cohorts of women with ovarian cancer and benign gynecological disease. The expression of LRG1 in ovarian cancer tissues and cell lines was examined by gene microarray, reverse-transcriptase polymerase chain reaction (RT-PCR), Western blot, immunocytochemistry and mass spectrometry.ResultsMean serum LRG1 was higher in 58 ovarian cancer patients than in 56 healthy women (89.33 ± 77.90 vs. 42.99 ± 9.88 ug/ml; p = 0.0008) and was highest among stage III/IV patients. In a separate set of 193 pre-surgical samples, LRG1 was higher in patients with serous or clear cell ovarian cancer (145.82 ± 65.99 ug/ml) compared to patients with benign gynecological diseases (82.53 ± 76.67 ug/ml, p < 0.0001). CA125 and LRG1 levels were moderately correlated (r = 0.47, p < 0.0001). LRG1 mRNA levels were higher in ovarian cancer tissues and cell lines compared to their normal counterparts when analyzed by gene microarray and RT-PCR. LRG1 protein was detected in ovarian cancer tissue samples and cell lines by immunocytochemistry and Western blotting. Multiple iosforms of LRG1 were observed by Western blot and were shown to represent different glycosylation states by digestion with glycosidase. LRG1 protein was also detected in the conditioned media of ovarian cancer cell culture by ELISA, Western blotting, and mass spectrometry.ConclusionsSerum LRG1 was significantly elevated in women with ovarian cancer compared to healthy women and women with benign gynecological disease, and was only moderately correlated with CA125. Ovarian cancer cells secrete LRG1 and may contribute directly to the elevated levels of LRG1 observed in the serum of ovarian cancer patients. Future studies will determine whether LRG1 may serve as a biomarker for presurgical diagnosis, disease recurrence, and/or as a target for therapy.

Leucine-rich alpha-2-glycoprotein-1 (LRG) is a serum glycoprotein of unknown function that has shown promise based on qualitative assessments as a biomarker for certain diseases including microbial infections and cancer. However, the lack of a quantitative assay for LRG has limited its application. Here an indirect enzyme-linked immunosorbent assay (ELISA) for quantifying LRG in human serum is described in which cytochrome c is employed as the capturing ligand and a monoclonal antibody specific for LRG is used to detect the captured glycoprotein. Application of this assay in quantifying LRG in various patients' sera is demonstrated. The concentration of LRG in sera of control subjects as determined by this assay is approximately 50 microg/ml. Consistent with expectations from published reports, LRG was found to be significantly elevated in the sera of some patients with a bacterial infection (toxic shock syndrome, TSS). LRG was only slightly elevated in patients infected with the human immunodeficiency virus as compared to uninfected control subjects, while normal levels of LRG were observed in patients with non-infectious diseases (inflammatory arthritis and neurological disorders, primarily Parkinson's disease). Although LRG and C-reactive protein (CRP) are both produced by the liver and are classified as acute-phase proteins, there was no significant correlation between the levels of LRG and CRP in the sera of the patients. Thus, LRG and CRP measurements are non-redundant and indicate different physiological contexts. The ELISA described in this report should be useful to further assess serum LRG as a biomarker for clinical diagnostics.

Ovarian cancer is the fifth leading cause of cancer death for women in the U.S., yet survival rates are over 90% when it is diagnosed at an early stage, highlighting the need for biomarkers for early detection. To enhance the discovery of tumor-specific proteins which could represent novel serum biomarkers for ovarian cancer, we depleted serum of highly abundant proteins which can mask the detection of proteins present in serum at low concentrations. Three commercial immunoaffinity columns were used in parallel to deplete the highly abundant proteins in serum from 60 patients with serous ovarian carcinoma and 60 non-cancer controls. Medium and low abundance serum proteins from each serum pool were then evaluated by the quantitative proteomic technique of Differential-In-Gel-Electrophoresis (DIGE). The number of protein spots that were elevated in ovarian cancer sera by at least 2-fold ranged from 36 to 248, depending upon the depletion and separation methods. From the 33 spots picked for MS analysis, nine different proteins were identified, including the novel candidate ovarian cancer biomarkers leucine-rich alpha-2 glycoprotein-1 and ficolin 3. Western blotting validated the relative increases in serum protein levels for three of the proteins identified, demonstrating the utility of this approach for the identification of novel serum biomarkers for ovarian cancer.

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