The brain consists of billions of cells that communicate with each other to produce fundamental processes such as thought and perception and to orchestrate all body functions. At the molecular level, many of these processes are Ca2+-dependent. The long-term objective is to understand the molecular mechanisms underlying Ca2+-dependent processes in the brain with emphasis on 4 aims. (1) To characterize the regulatory properties of cytosolic calmodulin(CaM)-dependent phosphatase and particulate CaM-dependent phosphatase and to compare their molecular and functional properties, (2) to identify the interacting domains of CaM for phosphodiesterase. (3) to elucidate the interacting sites of subunit B with subunit A of CaM-dependent phosphatase, and (4) characterize a novel Ca2+-binding protein (CaBP-20) from bovine brain and a novel Ca2+-binding protein (CaBP-15) from chick brain. These experiments involve purification of several proteins from the brain tissue using standard biochemical techniques, and their characterization. Other techniques include protein chemistry, monoclonal and polyclonal antibodies, and immunocytochemical localization at both the light and the electronmicroscopic levels.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM036734-21
Application #
3291209
Study Section
Biochemistry Study Section (BIO)
Project Start
1985-09-18
Project End
1993-08-31
Budget Start
1990-09-01
Budget End
1991-08-31
Support Year
21
Fiscal Year
1990
Total Cost
Indirect Cost
Name
St. Jude Children's Research Hospital
Department
Type
DUNS #
067717892
City
Memphis
State
TN
Country
United States
Zip Code
38105
Huang, S; Cheung, W Y (1994) H+ is involved in the activation of calcineurin by calmodulin. J Biol Chem 269:22067-74
Huang, S; Carlson, G M; Cheung, W Y (1994) Calmodulin-dependent enzymes undergo a protein-induced conformational change that is associated with their interactions with calmodulin. J Biol Chem 269:7631-8
Chao, S H; Bu, C H; Cheung, W Y (1990) Activation of troponin C by Cd2+ and Pb2+. Arch Toxicol 64:490-6
Huang, S L; Merat, D; Cheung, W Y (1989) Phosphatidylinositol modulates the response of calmodulin-dependent phosphatase to calmodulin. Arch Biochem Biophys 270:42-9
Pezzi, L; Merat, D L; Winkler, M A et al. (1989) Calmodulin-dependent phosphatase preferentially dephosphorylates a 28 kDa protein in human platelets. Int J Biochem 21:791-8
Cheung, W Y (1988) Calmodulin and its activation by cadmium ion. Ann N Y Acad Sci 522:74-87
Winkler, M A; Zysk, J R; Cheung, W Y (1987) Production and characterization of a monoclonal antibody cross-reactive with calmodulin, calmodulin-dependent phosphodiesterase, and protein phosphatase. Methods Enzymol 139:505-18
Winkler, M A; Fried, V A; Merat, D L et al. (1987) Differential reactivities of lysines in calmodulin complexed to phosphatase. J Biol Chem 262:15466-71
Merat, D L; Cheung, W Y (1987) Calmodulin-dependent protein phosphatase: isolation of subunits and reconstitution to holoenzyme. Methods Enzymol 139:79-87
Winkler, M A; DeWitt, L M; Cheung, W Y (1987) Calmodulin and calcium channel blockers. Hypertension 9:217-23

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