Tumor Differentiation Factor (TDF) and its Receptor (TDF-R): Is TDF-R an Inducible Complex with Multiple Docking Sites?
|Urmi Roy, Izabela Sokolowska, Alisa G Woods and Costel C Darie*|
|Biochemistry and Proteomics Group, Department of Chemistry and Biomolecular Science, Clarkson University, USA|
|Corresponding Author :||Costel C Darie
Biochemistry and Proteomics Group
Department of Chemistry and Biomolecular Science
Clarkson University, 8 Clarkson Avenue
Potsdam, NY, 13699-5810, USA
E-mail: [email protected]clarkson.edu
|Received July 23, 2013; Accepted September 03, 2013; Published September 10, 2013|
|Citation: Roy U, Sokolowska I, Woods AG and Darie CC (2013) Tumor Differentiation Factor (TDF) and its Receptor (TDF-R): Is TDF-R an Inducible Complex with Multiple Docking Sites? Mod Chem appl 1:108. doi:10.4172/2329-6798.1000108|
|Copyright: © 2013 Roy U, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.|
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Tumor Differentiation Factor (TDF) is a protein produced by the pituitary and secreted into the blood stream. TDF targets breast and prostate and induces cell differentiation. However, the mechanism of cell differentiation, the TDF receptor and the TDF pathway have not been adequately investigated. Here, we provide some insights about the possible composition of the TDF-R. TDF-R may be a protein complex, composed of GRP78, HSP70 and HSP90 proteins, and all three protein subunits have a docking site for TDF-P1. The question of whether the TDF-R complex is a stable or transient/inducible complex is currently being investigated.