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Pancreatic Neoplasms: HELP
Articles by Donghwa Kim
Based on 3 articles published since 2009
(Why 3 articles?)
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Between 2009 and 2019, Donghwa Kim wrote the following 3 articles about Pancreatic Neoplasms.
 
+ Citations + Abstracts
1 Editorial MicroRNAs in pancreatic ductal adenocarcinoma. 2011

Park, Jong Y / Helm, James / Coppola, Domenico / Kim, Donghwa / Malafa, Mokenge / Kim, Seung Joon. · ·World J Gastroenterol · Pubmed #21412491.

ABSTRACT: Ductal adenocarcinoma of the pancreas is a lethal cancer for which the only chance of long-term survival belongs to the patient with localized disease in whom a potentially curative resection can be done. Therefore, biomarkers for early detection and new therapeutic strategies are urgently needed. miRNAs are a recently discovered class of small endogenous non-coding RNAs of about 22 nucleotides that have gained attention for their role in downregulation of mRNA expression at the post-transcriptional level. miRNAs regulate proteins involved in critical cellular processes such as differentiation, proliferation, and apoptosis. Evidence suggests that deregulated miRNA expression is involved in carcinogenesis at many sites, including the pancreas. Aberrant expression of miRNAs may upregulate the expression of oncogenes or downregulate the expression of tumor suppressor genes, as well as play a role in other mechanisms of carcinogenesis. The purpose of this review is to summarize our knowledge of deregulated miRNA expression in pancreatic cancer and discuss the implication for potential translation of this knowledge into clinical practice.

2 Article IκB Kinase ε expression in pancreatic ductal adenocarcinoma. 2011

Cheng, Anna / Guo, Jianping / Henderson-Jackson, Evita / Kim, Donghwa / Malafa, Mokenge / Coppola, Domenico. ·Anatomic Pathology, Moffitt Cancer Center, Tampa, FL 33612, USA. ·Am J Clin Pathol · Pubmed #21685032.

ABSTRACT: IκB kinase (IKKε) is a serine/threonine protein kinase that belongs to the IKK kinase family. Recent studies have shown that IKKε functions as a breast and ovarian cancer oncogene. We demonstrated frequent overexpression of IKKε in pancreatic ductal adenocarcinoma (PDA). We immunohistochemically evaluated 78 PDAs using the avidin-biotin-peroxidase method and the anti-IKKε rabbit polyclonal antibody. Elevated IKKε reactivity (immunohistochemical score, 4-9) was observed in 64% of PDAs (50/78), but in 0.0% of nonneoplastic pancreatic ductal epithelium (0/113; P < .001). Kaplan-Meier analysis of overall survival revealed that patients with high IKKε-immunohistochemical scores (4-9) had significantly shorter survival than did patients with low IKKε immunohistochemical scores (0-3; P = .023; log-rank test) independent of tumor stage or grade. These data indicate that deregulation of IKKε is a common event in PDA and might have an important role in the pathogenesis of this deadly disease. In addition, IKKε could serve as a prognostic marker and potential therapeutic target for PDA intervention.

3 Retraction A small molecule inhibits Akt through direct binding to Akt and preventing Akt membrane translocation. 2010

Kim, Donghwa / Sun, Mei / He, Lili / Zhou, Qing-Hua / Chen, Jun / Sun, Xia-Meng / Bepler, Gerold / Sebti, Said M / Cheng, Jin Q. ·Departments of Molecular Oncology, H Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33612, USA. ·J Biol Chem · Pubmed #20068047.

ABSTRACT: The Akt pathway is frequently hyperactivated in human cancer and functions as a cardinal nodal point for transducing extracellular and intracellular oncogenic signals and, thus, presents an exciting target for molecular therapeutics. Here we report the identification of a small molecule Akt/protein kinase B inhibitor, API-1. Although API-1 is neither an ATP competitor nor substrate mimetic, it binds to pleckstrin homology domain of Akt and blocks Akt membrane translocation. Furthermore, API-1 treatment of cancer cells results in inhibition of the kinase activities and phosphorylation levels of the three members of the Akt family. In contrast, API-1 had no effects on the activities of the upstream Akt activators, phosphatidylinositol 3-kinase, phosphatidylinositol-dependent kinase-1, and mTORC2. Notably, the kinase activity and phosphorylation (e.g. Thr(P)(308) and Ser(P)(473)) levels of constitutively active Akt, including a naturally occurring mutant AKT1-E17K, were inhibited by API-1. API-1 is selective for Akt and does not inhibit the activation of protein kinase C, serum and glucocorticoid-inducible kinase, protein kinase A, STAT3, ERK1/2, or JNK. The inhibition of Akt by API-1 resulted in induction of cell growth arrest and apoptosis selectively in human cancer cells that harbor constitutively activated Akt. Furthermore, API-1 inhibited tumor growth in nude mice of human cancer cells in which Akt is elevated but not of those cancer cells in which it is not. These data indicate that API-1 directly inhibits Akt through binding to the Akt pleckstrin homology domain and blocking Akt membrane translocation and that API-1 has anti-tumor activity in vitro and in vivo and could be a potential anti-cancer agent for patients whose tumors express hyperactivated Akt.