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- 저자 : William Hogan (검색결과 2 건)
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Mohsin Ilyas Malik,Mark Litzow,William Hogan,Mrinal Patnaik,Mohammad Hassan Murad,Larry J. Prokop,Jeffrey L. Winters,Shahrukh Hashmi 대한혈액학회 2014 Blood Research Vol.49 No.2
Background The safety of extracorporeal photopheresis (ECP) in steroid-refractory chronic graft-versus- host disease (SR-cGVHD) has been explored in multiple studies but reported response rates (RR) vary significantly across studies. Methods We conducted a meta-analysis to assess the efficacy of ECP for SR-cGVHD. A search of electronic databases for studies published between 1984 and 2012 was conducted. End points included RR: complete response (CR), overall response rates (ORR), and organ- specific RR. The initial search generated 312 studies, of which 18 met the selection criteria (N=595). A random effects model was used for pooled rates. Results Pooled CR rates and ORR were 29% (confidence interval [CI], 19‒42%) and 64% (CI, 65‒ 82%), respectively. One-year overall survival was available for 4 studies only and was 49% (CI, 29‒70%). The pooled RR for skin, liver, ocular, oral, lung, gastrointestinal and musculoskeletal SR-cGVHD was 74%, 68%, 60%, 72%, 48%, 53%, and 64%, respectively. There was a significant heterogeneity among studies due to differences in ECP schedules and duration. No significant differences in responses to ECP for pediatric and adult populations were found. Sensitivity analysis could not be undertaken due to a limited number of prospective studies. Conclusion ECP is an effective therapy for oral, skin, and liver SR-cGVHD, with modest activity in lung and gastrointestinal SR-cGVHD.
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Zeng, Zhi,Hincapie, Marina,Pitteri, Sharon J.,Hanash, Samir,Schalkwijk, Joost,Hogan, Jason M.,Wang, Hong,Hancock, William S. American Chemical Society 2011 ANALYTICAL CHEMISTRY - Vol.83 No.12
<P>The discovery of breast cancer associated plasma/serum biomarkers is important for early diagnosis, disease mechanism elucidation, and determination of treatment strategy for the disease. In this study of serum samples, a multidimensional fractionation platform combined with mass spectrometric analysis were used to achieve the identification of medium to lower abundance proteins, as well as to simultaneously detect glycan and abundance changes. Immuno-affinity depletion and multi-lectin chromatography (M-LAC) were integrated into an automated HPLC platform to remove high abundance protein and fractionate glycoproteins. The collected glycoproteomes were then subjected to isoelectric focusing (IEF) separation by a digital ProteomeChip (dPC), followed by in-gel digestion and LC–MS analysis using an Orbitrap mass spectrometer. As a result, the total number of identified proteins increased significantly when the IEF fractionation step was included as part of the platform. Relevant proteins with biological and disease significance were observed and the dynamic range of the serum proteome measurement was extended. In addition, potential glycan changes were indicated by comparing proteins in control and cancer samples in terms of their affinity to the multi-lectin column (M-LAC) and the p<I>I</I> profiles in IEF separation. In conclusion, a proteomics platform including high abundance protein depletion, lectin affinity fractionation, IEF separation, and LC–MS analysis has been applied to discover breast cancer-associated proteins. The following candidates, thrombospondin-1 and 5, alpha-1B-glycoprotein, serum amyloid P-component, and tenascin-X, were selected as promising examples of the use of this platform. They show potential abundance and glycan changes and will be further investigated in future studies.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancham/2011/ancham.2011.83.issue-12/ac2002802/production/images/medium/ac-2011-002802_0006.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/ac2002802'>ACS Electronic Supporting Info</A></P>
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