Abstract

The purpose of the studies of red cell and granulocyte membranes, outlined in this proposal, is to define changes in cell membrane protein and lipid metabolism which may influence cell flexibility and permeability. The flexibility and permeability of erythrocytes is crucial to cell survival in vivo and is also particularly relevant to the problem of prolonged erythrocyte storage. Particular attention is focused upon the role of the Red cell membrane protein Spectrin since defects in Spectrin appear to be a common denominator in several clinical Hemolytic disorders.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK016095-15
Application #
3225513
Study Section
Hematology Subcommittee 2 (HEM)
Project Start
1977-08-01
Project End
1987-07-31
Budget Start
1986-08-01
Budget End
1987-07-31
Support Year
15
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of California San Francisco
Department
Type
Schools of Medicine
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143

  Publications

Dayel, M J; Hom, E F; Verkman, A S (1999) Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys J 76:2843-51
Verkman, A S (1999) Green fluorescent protein as a probe to study intracellular solute diffusion. Methods Enzymol 302:250-64
Thevenin, B J; Crandall, I; Ballas, S K et al. (1997) Band 3 peptides block the adherence of sickle cells to endothelial cells in vitro. Blood 90:4172-9
Swaminathan, R; Hoang, C P; Verkman, A S (1997) Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys J 72:1900-7
Olveczky, B P; Periasamy, N; Verkman, A S (1997) Mapping fluorophore distributions in three dimensions by quantitative multiple angle-total internal reflection fluorescence microscopy. Biophys J 73:2836-47
Thevenin, B J; Bicknese, S E; Park, J et al. (1996) Distance between Cys-201 in erythrocyte band 3 and the bilayer measured by single-photon radioluminescence. Biophys J 71:2645-55
Bicknese, S; Rossi, M; Thevenin, B et al. (1995) Anisotropy decay measurement of segmental dynamics of the anion binding domain in erythrocyte band 3. Biochemistry 34:10645-51
Zimet, D B; Thevenin, B J; Verkman, A S et al. (1995) Calculation of resonance energy transfer in crowded biological membranes. Biophys J 68:1592-603
Thevenin, B J; Periasamy, N; Shohet, S B et al. (1994) Segmental dynamics of the cytoplasmic domain of erythrocyte band 3 determined by time-resolved fluorescence anisotropy: sensitivity to pH and ligand binding. Proc Natl Acad Sci U S A 91:1741-5
Krishnan, G; MacGregor, R D; Shohet, S B et al. (1994) Characterization of apocytochrome C binding to human erythrocytes. Am J Hematol 47:132-4

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