alexa Characterization of Human Serum Albumin-Facilitated Lip
ISSN: 2157-7013

Journal of Cell Science & Therapy
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Research Article

Characterization of Human Serum Albumin-Facilitated Lipofection Gene Delivery Strategy

Robert W Arpke1,2 and Pi-Wan Cheng1,2,3,4*
1Omaha Western Iowa Health System, VA Service, Department of Veterans Affairs Medical Center, Omaha, NE
2Department of Biochemistry and Molecular Biology, College of Medicine
3Eppley Institute for Research in Cancer and Allied Diseases
4Department of Pharmaceutical Sciences, College of Pharmacy, University of Nebraska Medical Center, Omaha, NE
Corresponding Author : Pi-Wan Cheng, PhD
Professor, Department of Biochemistry and Molecular
Biology, 985870 Nebraska Medical Center
Omaha, NE 68198-5870, USA
Tel: (402) 559-5776
Fax: (402) 559-6650
E-mail: [email protected]
Received October 01, 2011; Accepted October 22, 2011; Published October 24, 2011
Citation: Arpke RW, Cheng PW (2011) Characterization of Human Serum Albumin-Facilitated Lipofection Gene Delivery Strategy. J Cell Sci Ther 2:108. doi: 10.4172/2157-7013.1000108
Copyright: © 2011 Arpke RW, 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.
 

Abstract

We report the characterization of a facilitated lipofection strategy, which employs a formulation prepared with human serum albumin, DMRIE-C and pCMV?. The transfection complexes in the lipofection formulation containing albumin were characterized for size by light scattering, intracellular trafficking by confocal microscopy, and uptake mechanism by inhibitors. Supplementation of the formulation of DMRIE-C plus pCMV? with albumin enhances lipofection efficiency 8-9 fold and the size of the complexes 2-2.5 fold as measured by light scattering. Analysis of intracellular trafficking of the transfection complexes by confocal microscopy reveals colocalization of DNA and albumin in the cytoplasm and the nucleus. Pretreatment of the cells with chlorpromazine or excess albumin, cytochalasin B or filipin complexes results in inhibition of the transfection efficiency by 20%, 55%, or none, respectively. The results suggest a moderate involvement of clathrin, a significant involvement of actinassociated macropinocytosis, and no involvement of caveolae in the uptake of the transfection complexes prepared with human serum albumin, DMRIE-C and pCMV?.

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