Richard C. Kurten
Associate Professor
Ph.D., Baylor College of Medicine
Office: (501) 686-8269, 364-2823
Lab: (501) 364-1060
Email: KurtenRichardC@uams.edu

Our laboratory is interested in understanding how we can manipulate the intracellular trafficking of cell surface receptors to regulate physiological response in cells and tissues. The Lung Cell Biology Laboratory is a collaborative effort with Stacie M. Jones, M.D. and Bradley Schnackenberg, Ph.D. in the Department of Pediatrics. The laboratory is located in the Arkansas Children’s Hospital Research Institute. At the current time, our major interests include (1) understanding mechanisms for enhancing and inhibiting wound healing in airway epithelium and (2) manipulating b₂ adrenergic receptors to regulate airway contractility. In addition, we are also interested in understanding the structure and function of two members of the sorting nexin family of proteins, SNX1 and SNX2.

We use cultured cells, rat airway organ cultures and intact rats in a variety of experimental approaches to study these problems. Much of the work involves the use of time-lapse imaging techniques to evaluate the behavior of cell and tissues over time. For example, by monitoring scrape wound closure, we have discovered that epidermal growth factor (EGF) induced motility is coordinated by serum factors to significantly enhance wound closure. More recently, Dr. Schnackenberg has discovered that b-agonists (widely used as bronchodilator medications) actually inhibit wound healing human airway epithelial cell lines. Using cyan, green and yellow fluorescent proteins as tags, we monitor the distribution and behavior of proteins in cells with time lapse imaging, fluorescence recovery after photobleaching and fluorescence resonance energy transfer techniques. For example, using an adenovirus encoding the human b₂-adrenergic receptor (b₂AR) to infect rat tracheal explants, we have used a yellow fluorescent protein tag to demonstrate efficient and specific expression of a functional receptor in airway epithelial cells. Moreover, the physiological effect of the virally encode receptor is to suppress airway contractile responses. We are working toward translating this result into one that is clinically useful. Dr. Jones has found that an adeno-associated virus encoding the human b₂AR has significant effects to suppress methocholine induced bronchoconstriction in intact rats. These experiments are performed in collaboration with Dr. Larry Cornett (Physiology & Biophysics) and with Dr. Mark Heulitt (Pediatrics) in the Respiratory Mechanics Laboratory at the Arkansas Children’s Hospital Research Institute. Taken together, these results provide new approaches to enhancing the effectiveness of bronchodilator medications used in the management of asthma.

The Lung Cell Biology Laboratory is well equipped for cell and molecular biology. Two sterile hoods are available for cell and tissue culture work with one of the hoods in a dedicated tissue culture room. Major equipment in the laboratory includes: a Zeiss Axioskop digital deconvolution microscope, several time lapse microscope systems (both dissecting and inverted microscopes), a Perkin Elmer Victor³ fluorescence plate reader, a Beckman Coulter Epics XL flow cytometer, a Ciphergen SELDI mass spectrometer, a Beckman Optima TL tabletop ultracentrifuge and a Beckman Biomek 2000 laboratory robot. Dr. Kurten is also Director of the UAMS/ACRC Digital and Confocal Microscopy Laboratory.

Microscope Lab Homepage

Representative Publications

Kurten RC, Chowdhury P, Sanders Jr RC, Pittman LM, Sessions LW, Chambers TC, Lyle CM, Schnackenberg BJ, Foreman S, Jones SM (2005). Coordinating epidermal growth factor induced motility promotes efficient wound closure. Am J Physiol Cell Physiol. 288(1):C109-21.

Zent, C.S., J.B. Chan, R.C. Kurten, G.P. Kjaushak, H.M. Lacy, S.A. Schickman. (2004) Alemtuzumab (CAMPATH 1H) does not kill chronic lymphocytic leukemia cells in serum free medium Leukemia Research 28(5):495-507.

Jones, S.M., S.K. Foreman, B.B. Shank, and R.C. Kurten. (2002). EGF receptor down-regulation depends on a trafficking motif in the distal tyrosine kinase domain. Am J Physiol Cell Physiol.   282:C420-C433.

Kurten, R.C., A.D. Eddington, P. Chowdhury, R.D. Smith, A.D. Davidson, and B.B. Shank (2001) Self-assembly and sorting endosome binding by a sorting nexin. J. Cell Science 114:1743-1756.

Kurten, R.C., D.L. Cadena, and G.N. Gill (1996) Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272:1008-1010.

Link to Dr. Kurten at PubMed

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