Todd M. Hennessey

Membrane Biochemistry and Cell Physiology

Professor

PhD 1981 University of Wisconsin-Madison
Postdoctoral work 1981 University of Wisconsin-Madison
Assistant Professor 1985;
Associate Professor 1991 University at Buffalo


Address Information

Todd M. Hennessey
Department of Biological Sciences
610 Hochstetter Hall
State University of New York at Buffalo
Buffalo, NY 14260

(716) 645-4973

To send e-mail: thennes@buffalo.edu


RESEARCH SUMMARY

We are using the unicellular eukaryotes Paramecium and Tetrahymena as model sensory cells to study the chemosensory pathways involved in cellular responses to depolarizing chemorepellents such as ATP, GTP, and polycations (such as lysozyme) as well as the mechanisms responsible for adaptation to these stimuli. Swimming behaviors are used in convenient bioassays to estimate the responsiveness of these free swimming sensory cells and intracellular electrophysiology is done to confirm the roles of specific ionic conductances. These unicellular eukaryotic cells can be grown to high densities in clonal, axenic cultures so that large amounts of cells can be obtained as starting material for biochemical and molecular analyses. "Genetic dissection" of the sensory transduction and adaptation pathways can be approached by screening for behavioral mutants that have altered responses to chemoeffectors. Molecular Biological approaches such as gene knockouts, RNAi and antisense ribosome mutagenesis are used to study the regulation and functional expression of the gene products involved in chemosensory transduction and adaptation in Tetrahymena. We have also begun a collaboration with Dr David Pennock at Miami University in Ohio to generate and characterize knockout mutants of the various inner arm dynein heavy chain genes of Tetrahymena to help to understand the roles of the different ciliary dyneins in proper ciliary function.


SELECTED PROJECTS

  • Purification, cloning and regulated expression of and ectonucleotidases in Tetrahymena
    T. Smith, T. Santangelo, T. Hennessey
    Tetrahymena hydrolyze external nucleotide triphosphates (like ATP and GTP) by an ecto-nTPase and external nucleotide monophosphates (like AMP and GMP) by a different ecto-nMPase. The ecto-nTPase may be involved in inactivating external GTP as a signaling molecule because GTP is a chemorepellent (Clark et al., 1993). This may be analogous to a system such as acetylcholine/acetylcholinesterase. The ecto-nTPase may also act as either a cell adhesion molecule in the mating response or in extracellular metabolism of nucleotide phosphates to provide for their guanine auxotrophy. The ecto-nMPase may also be involved in this extracellular scavenge pathway for nucleotides. These two enzymes (ecto-nTPase and ecto-nMPase) will be characterized in vivo and in vitro, purified, sequenced, and cloned to provide the molecular tools necessary to study their functions and possible regulation of functional surface expression. Monoclonal antibodies are also being generated to aid in these efforts.

    PUBLICATIONS



  • Surface membrane preparation (pellicle) from Paramecium.