Articles by Adam Benjamin

In JoVE (1)

一种实用的新的方法来提取基因组DNA保存血浆蛋白从血液采集套件

Other Publications (1)

The American Journal of Pathology

Articles by Adam Benjamin in JoVE

Biology

一种实用的新的方法来提取基因组DNA保存血浆蛋白从血液采集套件 Jon Waters¹, Vishal Dhere¹, Adam Benjamin¹, Arvind Sekar¹, Archana Kumar¹, Sampath Prahalad², David T. Okou¹, Subra Kugathasan¹ ¹Division of Gastroenterology, Hepatology and Nutrition, Department of Pediatrics, Emory University School of Medicine and Children's Health Care of Atlanta, ²Division of Rheumatology, Department of Pediatrics, Emory University School of Medicine and Children's Health Care of Atlanta 我们所描述的从全血收集的血浆/血清中分离基因组DNA的新方法。血浆采集后，压实血通常是被丢弃。我们的新方法较现有方法相比，一个显着的改善，使得DNA，不要求额外的血液和血浆可以从一个单一的集合。

Other articles by Adam Benjamin on PubMed

Fusion Tyrosine Kinase NPM-ALK Deregulates MSH2 and Suppresses DNA Mismatch Repair Function Novel Insights into a Potent Oncoprotein The American Journal of Pathology. Jul, 2011 | Pubmed ID: 21703420 The fusion tyrosine kinase NPM-ALK is central to the pathogenesis of ALK-positive anaplastic large cell lymphoma (ALK(+)ALCL). We recently identified that MSH2, a key DNA mismatch repair (MMR) protein integral to the suppression of tumorigenesis, is an NPM-ALK-interacting protein. In this study, we found in vitro evidence that enforced expression of NPM-ALK in HEK293 cells suppressed MMR function. Correlating with these findings, six of nine ALK(+)ALCL tumors displayed evidence of microsatellite instability, as opposed to none of the eight normal DNA control samples (P = 0.007, Student's t-test). Using co-immunoprecipitation, we found that increasing levels of NPM-ALK expression in HEK293 cells resulted in decreased levels of MSH6 bound to MSH2, whereas MSH2Â·NPM-ALK binding was increased. The NPM-ALKÂ·MSH2 interaction was dependent on the activation/autophosphorylation of NPM-ALK, and the Y191 residue of NPM-ALK was a crucial site for this interaction and NPM-ALK-mediated MMR suppression. MSH2 was found to be tyrosine phosphorylated in the presence of NPM-ALK. Finally, NPM-ALK impeded the expected DNA damage-induced translocation of MSH2 out of the cytoplasm. To conclude, our data support a model in which the suppression of MMR by NPM-ALK is attributed to its ability to interfere with normal MSH2 biochemistry and function.

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