This is a study of passive intermembrane transfer of intrinsic proteins.
Three specific aims are addressed: identification of the molecular properties that distinguish proteins that transfer from those that do not, development of protein transfer from model membranes to cells as a noninvasive means of modifying the transport and antigenic properties of biological membranes, and examination of mixtures of natural membranes under conditions where protein exchange might be expected to occur. The proteins under study are the anion transport protein of the human erythrocyte membrane, a histocompatibility antigen derived from mouse spleen, and surface marker antigens found in lymphocyte cell lines in tissue culture. Each of these species can be detected with extremely high sensitivity by complement fixation or assay of membrane anion permeability, measures which reflect on the proteins' native orientation and function in the membrane. Transfer of these species between model membranes and cells will be studied, and physical parameters controlling the rate and extent of functional protein transfer examined. The possibility of cell-to-cell transfer will be explored for normal and transformed cells in culture, and mechanisms whereby normal cells might control such events in vivo will be examined. The overall objective is to evaluate passive protein transfer as a mechanism for modification of membrane properties, either in natural processes or as a research instrument.

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL023787-08
Application #
3337415
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1979-04-01
Project End
1988-09-29
Budget Start
1986-04-01
Budget End
1987-09-29
Support Year
8
Fiscal Year
1986
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
Schools of Arts and Sciences
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
Chen, James Y; Brunauer, Linda S; Chu, Felicia C et al. (2003) Selective amphipathic nature of chlorpromazine binding to plasma membrane bilayers. Biochim Biophys Acta 1616:95-105
Gedde, M M; Yang, E; Huestis, W H (1999) Resolution of the paradox of red cell shape changes in low and high pH. Biochim Biophys Acta 1417:246-53
Chen, J Y; Huestis, W H (1997) Role of membrane lipid distribution in chlorpromazine-induced shape change of human erythrocytes. Biochim Biophys Acta 1323:299-309
Moxness, M S; Brunauer, L S; Huestis, W H (1996) Hemoglobin oxidation products extract phospholipids from the membrane of human erythrocytes. Biochemistry 35:7181-7
Waters, S I; Sen, R; Brunauer, L S et al. (1996) Physical determinants of intermembrane protein transfer. Biochemistry 35:4002-8
Gedde, M M; Yang, E; Huestis, W H (1995) Shape response of human erythrocytes to altered cell pH. Blood 86:1595-9
Lin, S; Huestis, W H (1995) Wheat germ agglutinin stabilization of erythrocyte shape: role of bilayer balance and the membrane skeleton. Biochim Biophys Acta 1233:47-56
Hall, M P; Huestis, W H (1994) Phosphatidylserine headgroup diastereomers translocate equivalently across human erythrocyte membranes. Biochim Biophys Acta 1190:243-7
Yang, E; Huestis, W H (1994) Oxidative interactions between the erythrocyte membrane and phosphatidylcholine vesicles. J Biol Chem 269:14518-24
Brown, J W; Huestis, W H (1994) Quantification of two-dimensional NOE spectra via a combined linear and nonlinear least-squares fit. J Biomol NMR 4:645-52

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