Abstract

The objective of this work is to investigate the structural and biochemical state of the cytoskeletal protein actin on the red cell membrane. Further, we propose to lay the foundations for studies of the diseases hereditary sphero and eliptocytosis (which may be the result of cytoskeletal abnormalities) and also for studies of cytoskeletal-membrane associations in complex blood cells, such as monocytes, platelets and macrophages. Our experiments focus on defining the role of the cell membrane as a catalytic structure which may influence or promote associations of actin with itself or with other membrane or cytoplasmic proteins. We hope to identify the membrane components (likely to be proteins) which are responsible for the association of actin with the red cell membrane and will examine the structure of actin complexes with purified membrane proteins in solution to obtain information on the kinds of associations to be expected on the membrane.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL024382-08
Application #
3337667
Study Section
Hematology Subcommittee 2 (HEM)
Project Start
1979-07-01
Project End
1987-06-30
Budget Start
1986-07-01
Budget End
1987-06-30
Support Year
8
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
St. Elizabeth's Medical Center of Boston
Department
Type
DUNS #
City
Boston
State
MA
Country
United States
Zip Code
02135

  Publications

Boukharov, A A; Cohen, C M (1998) Guanine nucleotide-dependent translocation of RhoA from cytosol to high affinity membrane binding sites in human erythrocytes. Biochem J 330 ( Pt 3):1391-8
Ai, Z; Misra, S; Susa, M et al. (1995) Phosphatidylinositol 3-kinase activity in murine erythroleukemia cells during DMSO-induced differentiation. Exp Cell Res 219:454-60
Gascard, P; Cohen, C M (1994) Absence of high-affinity band 4.1 binding sites from membranes of glycophorin C- and D-deficient (Leach phenotype) erythrocytes. Blood 83:1102-8
Gascard, P; Pawelczyk, T; Lowenstein, J M et al. (1993) The role of inositol phospholipids in the association of band 4.1 with the human erythrocyte membrane. Eur J Biochem 211:671-81
Al, Z; Cohen, C M (1993) Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors: possible role of protein kinase M. Biochem J 296 ( Pt 3):675-83
Cohen, C M; Gascard, P (1992) Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins. Semin Hematol 29:244-92
GuptaRoy, B; Cohen, C M (1992) Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C. J Biol Chem 267:15326-33
Korsgren, C; Lawler, J; Lambert, S et al. (1990) Complete amino acid sequence and homologies of human erythrocyte membrane protein band 4.2. Proc Natl Acad Sci U S A 87:613-7
Danilov, Y N; Fennell, R; Ling, E et al. (1990) Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C. J Biol Chem 265:2556-62
Danilov, Y N; Cohen, C M (1989) Wheat germ agglutinin but not concanavalin A modulates protein kinase C-mediated phosphorylation of red cell skeletal proteins. FEBS Lett 257:431-4

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