Research

Atkinson, Mark A.L., D.Phil.

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Contact: mark.atkinson@uthct.edu

Director of Research

Education:
B.A. (Hons) Biochemistry, 1975, Oxford University
M.A. Microbiology, 1978, Oxford University
D.Phil. Physiological Sciences, 1982, Oxford University

Research Interest:
The Cytoskeleton.

Current Projects:

  1. Role of FtsZ in Cell division.
  2. Activation of the Alternative Pathway of Complement (with Dr. Mike Pangburn).

Lay Summary:
The cytoskeleton is composed of a group of proteins which form a complex network or skeleton that gives a cell its shape. These proteins are present in virtually all cells from animals to bacteria. In addition to their structural role they also serve a wide variety of other purposes. They are the tracks along which motor molecules move cargoes of other molecules within the cell, they allow our immune defense cells to move out of the blood and through the tissue to fight infectious organisms, they provide the force that allows muscles to contract, they are the basis of the muco-cillary escalator that clears our lungs of respired particles, they separate the chromosomes and divide a cell into two during cell division and they even form the structures that allow us to hear. We are working to understand how these molecules are assembled to form the skeleton and how they interact with other molecules in such processes as cell movement and cell division.

Research Overview:
My lab has a long term interest in the role of cytoskeletal proteins in cellular function. As a fellow at Yale we were the first to visualize short actin oligomers in the red cell membrane and did some of the first structural studies on the actin binding protein of the human platelet cytoskeleton. As a Visiting Associate in the Fogarty International Program at the National Institutes of Health I worked in the Laboratory of Cell Biology of the Heart, Lung and Blood Institute. My research focused on myosin II isolated from Acanthamoeba castellanii. These studies utilized protein chemical, biochemical and biophysical approaches to understanding the role of phosphorylation in controlling enzymatic activity, filament assembly and the regulation of this molecule.

At the University of Texas Health Science Center at Tyler my initial research focused on the regulation of myosin II in alveolar macrophages as well as the role of myosin I in both alveolar macrophages and lung epithelial cells. More recently my interest has shifted to the molecular mechanics of FtsZ, an analog of eukaryotic tubulins, in the cell division of Mycobacterium tuberculosis. This project is in collaboration with Drs. Murty Madiraju and Malini Rajagopalan and is funded by NIH (AI 48417). We are using biochemical, biophysical, molecular genetic, electron microscopy, confocal microscopy and proteomic techniques to clarify the cell division process in M.tb with the long term goal that this information could be important in the development of novel therapeutic agents to combat Tuberculosis.

Another area of emphasis is in the mechanics of exercise induced muscle injury. This is part of an on-going collaboration with Dr. Jim Schwane at U.T. Tyler, where I hold an adjunct appointment. This project has been carried out by a number of graduate students enrolled in the exercise physiology program at U.T.T. We are developing an RIA for serum troponin I to detect and quantitate the extent and type (fast skeletal, slow skeletal and cardiac) of muscle damage. Changes in serum TnI are correlated with serum enzyme levels, a subjective assessment of muscle soreness, MRI scans of muscle (with Dr. Bob Shepherd at UTHSCT) and histological analyses as appropriate. This will have applications in sports medicine, as a diagnostic tool as well as a possible means to assess muscle atrophy in zero gravity.

Selected Papers and Abstracts: