University at Buffalo
H610 Hochstetter Hall
Buffalo, NY 14260
PH: (716) 645-2363, ext. 194
Web: http://www.biology.buffalo.edu/dept/facu...
E: thennes@acsu.buffalo.edu
H611, H612, H670 Hochstetter Hall
Buffalo, NY 14260
PH: (716) 645-2363, ext. 195
Research
Lipid biochemistry; electrophysiology; paramecium membrane biology; sensory transduction; Tetrahymena molecular biology.
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.
- Voltage clamp
- Video analysis of cell motility
Video analysis of cell motility
- Paramecium
- Tetrahymena
- ATP receptors
- Ecto-ATPase
- 7-transmembrane G-coupled protein receptors
- Dynein
- Pain
- Polycystic kidney
- Immmotile ciliary syndrome
- Emphysema
- Reproductive sterility
- Electrophysiology
- Biolistic transformation
- Lipid analysis
- Membrane purifications
- Ciliary beat frequency analysis
- Paramecium
- Tetrahymena