Division of Gastroenterology - Liver Research Center 















Miran Kim, Ph.D.

Assistant Professor of Medicine

Address:

Liver Research Center
55 Claverick Street, 4th Floor
Providence, RI 02903
phone: 401-444-4493
fax: 401-444-2939
E-mail:Miran_Kim@Brown.edu

Research Interests:

Beta-catenin is a multifunction protein. It plays an essential role in cell-cell adhesion through to directly associate with E-cadherin and to link via alpha-catenin the actin filament network. Besides, beta-catenin is associated with hepatocellular carcinoma as a component of the Wnt signaling pathway. In addition, insulin and IGF-1 can activate the beta-catenin pathway in hepatoma cells involving PI3K and GSK3b. We are focusing on how to cross talk between IGF/IRS-1 and Wnt signaling pathway. To approach this aim, we will use proteomic techniques to explore what kind of protein(s) are required to cross talk, how these proteins interact with each other. This work will provide to understand the molecular mechanism of hepatocarcinogenesis through Wnt signaling pathway.

Schematic representation of the Wnt/b-catenin pathway. Wnt/b-catenin signaling involves the regulation of multiprotein complex. Wnt stimulates Fz receptor, beta-catenin can translocate to the nucleus, turn on the transcription factors involved in cell migration and inhibition of apoptosis.

Selected Publications:

Lee HC, Kim M, Wands JR. Wnt/Frizzled signaling in hepatocellular carcinoma. Front Biosci. 2006 May 1;11:1901-15.

Merle P, Kim M, Herrmann M, Gupte A, Lefrancois L, Califano S, Trepo C, Tanaka S, Vitvitski L, de la Monte S, Wands JR.Oncogenic role of the frizzled-7/beta-catenin pathway in hepatocellular carcinoma. J Hepatol. 2005 Nov;43(5):854-62.

Merle P, de la Monte S, Kim M, Herrmann M, Tanaka S, Von Dem Bussche A, Kew MC, Trepo C, Wands JR. Functional consequences of frizzled-7 receptor overexpression in human hepatocellular carcinoma. Gastroenterology. 2004 Oct;127(4):1110-22.

Adinolfi E, Kim M, Young MT, Di Virgilio F, Surprenant A.Tyrosine phosphorylation of HSP90 within the P2X7 receptor complex negatively regulates P2X7 receptors. J Biol Chem. 2003 Sep 26;278(39):37344-51.

Jiang LH, Kim M, Spelta V, Bo X, Surprenant A, North RA.  Subunit arrangement in P2X receptors. J Neurosci. 2003 Oct 1;23(26):8903-10.

 

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