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Studies from University of Illinois Provide New Data on Biological Chemistry (Acidic domain in dentin phosphophoryn facilitates cellular uptake:...

July 15, 2014



Studies from University of Illinois Provide New Data on Biological Chemistry (Acidic domain in dentin phosphophoryn facilitates cellular uptake: implications in targeted protein delivery)

By a News Reporter-Staff News Editor at Life Science Weekly -- Researchers detail new data in Life Science Research. According to news reporting from Chicago, Illinois, by NewsRx journalists, research stated, "Dentin phosphophoryn is nature's most acidic protein found predominantly in the dentin extracellular matrix. Its unique amino acid composition containing Asp-Ser (DS)-rich repeats makes it highly anionic."

The news correspondents obtained a quote from the research from the University of Illinois, "It has a low isoelectric point (pI 1.1) and, therefore, tends to be negatively charged at physiological pH. Phosphophoryn is normally associated with matrix mineralization as it can bind avidly to Ca(2+). It is well known that several macromolecules present in the extracellular matrix can be internalized and localized to specific intracellular compartments. In this study we demonstrate that dentin phosphophoryn (DPP) is internalized by several cell types via a non-conventional endocytic process. Utilizing a DSS polypeptide derived from DPP, we demonstrate the repetitive DSS-rich domain facilitates that endocytosis. As a proof-of-concept, we further demonstrate the use of this polypeptide as a protein delivery vehicle by delivering the osteoblast transcription factor Runx2 to the nucleus of mesenchymal cells. The functionality of the endocytosed Runx2 protein was demonstrated by performing gene expression analysis of Runx2 target genes. Nuclear localization was also demonstrated with the fusion protein DSS-Runx2 conjugated to quantum dots in two-and three-dimensional culture models in vitro and in vivo."

According to the news reporters, the research concluded: "Overall, we demonstrate that the DSS domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo."

For more information on this research see: Acidic domain in dentin phosphophoryn facilitates cellular uptake: implications in targeted protein delivery. Journal of Biological Chemistry, 2013;288(22):16098-109. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)

Our news journalists report that additional information may be obtained by contacting S. Ravindran, Brodie Tooth Development Genetics and Regenerative Medicine Research Laboratory Dept. of Oral Biology, University of Illinois, Chicago, Illinois 60612, United States. Additional authors for this research include P.T. Snee, A. Ramachandran and A. George (see also Life Science Research).

Keywords for this news article include: Chicago, Illinois, United States, Life Science Research, North and Central America.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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