The activity of cytosolic phospholipase A2 (cPLA2) may be altered by calcium or by phosphorylation of serines in the cPLA2 molecule. A dual hybridization system in yeast was used to identify protein-protein interactions which might also be involved in the modulation of cPLA2 activity. Using this system, a member of the S-100 family of protein was identified as interacting with cPLA2. Ongoing studies include production of recombinant protein and modulation of enzyme function by oxidant molecules.

Agency
National Institute of Health (NIH)
Institute
Clinical Center (CLC)
Type
Intramural Research (Z01)
Project #
1Z01CL000182-06
Application #
6500917
Study Section
(CCM)
Project Start
Project End
Budget Start
Budget End
Support Year
6
Fiscal Year
2001
Total Cost
Indirect Cost
Name
Clinical Center
Department
Type
DUNS #
City
State
Country
United States
Zip Code
Qi, Hai-Yan; Daniels, Mathew P; Liu, Yueqin et al. (2011) A cytosolic phospholipase A2-initiated lipid mediator pathway induces autophagy in macrophages. J Immunol 187:5286-92
Qi, Hai-Yan; Shelhamer, James H (2005) Toll-like receptor 4 signaling regulates cytosolic phospholipase A2 activation and lipid generation in lipopolysaccharide-stimulated macrophages. J Biol Chem 280:38969-75
Huang, Xiuli; Pawliczak, Rafal; Yao, Xiang-Lan et al. (2003) Characterization of the human p11 promoter sequence. Gene 310:133-42
Huang, Xiu-li; Pawliczak, Rafal; Yao, Xiang-lan et al. (2003) Interferon-gamma induces p11 gene and protein expression in human epithelial cells through interferon-gamma-activated sequences in the p11 promoter. J Biol Chem 278:9298-308