Abstract

The proposed research represents an integrated chemical and physicochemical approach to elucidate the molecular parameters involved in the association of calmodulin with Beta-endorphin, phenothiazines, phosphodiesterase, calcium and vanadyl. Direct binding studies of endorphin and phenothiazines will be conducted to pursue the nature of the cooperativity that has been observed. Chemical studies will focus on differential trace labeling to assess individual lysine reactivities in calmodulin as influenced by the various ligands. A feasibility study will be undertaken using a novel technique for identification of the endorphin binding sites on calmodulin and the regions. Considerable effort will be devoted to ESR spectroscopy of spin labeled calmodulin and vanadyl-calmodulin complexes, several probes will be used to modify calmodulin, and spin labeled chlorpromazine-calmodulin complexes will be investigated. These studies should provide useful information on the mechanisms by which calmodulin can associate with a variety of simple ligands and complex enzymes.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM035415-02
Application #
3288115
Study Section
Biochemistry Study Section (BIO)
Project Start
1985-08-30
Project End
1988-07-31
Budget Start
1986-08-01
Budget End
1987-07-31
Support Year
2
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of Miami School of Medicine
Department
Type
Schools of Medicine
DUNS #
City
Miami
State
FL
Country
United States
Zip Code
33101

  Publications

Bowman, Paula B; Puett, David (2014) Electron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin. Protein J 33:267-77
Parra-Diaz, D; Wei, Q; Lee, E Y et al. (1995) Binding of vanadium (IV) to the phosphatase calcineurin. FEBS Lett 376:58-60
Parra-Diaz, D; Echegoyen, L; Zot, H G et al. (1995) Vanadium (IV) inhibits calmodulin-stimulated skeletal muscle myosin light chain kinase activity. Biofactors 5:25-8
Zot, H G; Aden, R; Samy, S et al. (1990) Fluorescent adducts of wheat calmodulin implicate the amino-terminal region in the activation of skeletal muscle myosin light chain kinase. J Biol Chem 265:14796-801
Chin, D; Brew, K (1989) Effects of modifying individual amino or carboxyl groups on the affinity of calmodulin for calcineurin. J Biol Chem 264:15367-75
Zot, H G; Puett, D (1989) An enzymatically active cross-linked complex of calmodulin and rabbit skeletal muscle myosin light chain kinase. J Biol Chem 264:15552-5
Sanyal, G; Richard, L M; Carraway 3rd, K L et al. (1988) Binding of amphiphilic peptides to a carboxy-terminal tryptic fragment of calmodulin. Biochemistry 27:6229-36
Lovegren, E S; Ling, N; Puett, D (1988) Interaction of alpha-N-Acetyl-beta-endorphin and calmodulin. J Protein Chem 7:35-47
Wei, Q; Jackson, A E; Pervaiz, S et al. (1988) Effects of interaction with calcineurin on the reactivities of calmodulin lysines. J Biol Chem 263:19541-4
Giedroc, D P; Puett, D; Sinha, S K et al. (1987) Calcium effects on calmodulin lysine reactivities. Arch Biochem Biophys 252:136-44

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