A study of the dynamic properties of the human red blood cell membrane using quasi-elastic light-scattering spectroscopy. 1993

R B Tishler, and F D Carlson
Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218.

A quasi-elastic light-scattering (QELS) microscope spectrometer was used to study the dynamic properties of the membrane/cytoskeleton of individual human red blood cells (RBCs). QELS is a spectroscopic technique that measures intensity fluctuations of laser light scattered from a sample. The intensity fluctuations were analyzed using power spectra and the intensity autocorrelation function, g(2)(tau), which was approximated with a single exponential. The value of the correlation time, Tcorr, was used for comparing results. Motion of the RBC membrane/cytoskeleton was previously identified as the source of the QELS signal from the RBC (R. B. Tishler and F. D. Carlson, 1987. Biophys. J. 51:993-997), and additional data supporting that conclusion are presented. Similar results were obtained from anucleate mammalian RBCs that have structures similar to that of the human RBC, but not for morphologically distinct, nucleated RBCs. The effect of altering the physical properties of the cytoplasm and the membrane/cytoskeleton was also studied. Osmotically increasing the cytoplasmic viscosity led to significant increases in Tcorr. Increasing the membrane cholesterol content and increasing the intracellular calcium content both led to decreased deformability of the human RBC. In both cases, the modified cells with decreased deformability showed an increase in Tcorr, demonstrating that QELS could measure biochemically induced changes of the membrane/cytoskeleton. Physiological changes were measured in studies of age-separated RBC populations which showed that Tcorr was increased in the older, less deformable cells.

UI MeSH Term Description Entries
D008027 Light That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range. Light, Visible,Photoradiation,Radiation, Visible,Visible Radiation,Photoradiations,Radiations, Visible,Visible Light,Visible Radiations
D008297 Male Males
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008853 Microscopy The use of instrumentation and techniques for visualizing material and details that cannot be seen by the unaided eye. It is usually done by enlarging images, transmitted by light or electron beams, with optical or magnetic lenses that magnify the entire image field. With scanning microscopy, images are generated by collecting output from the specimen in a point-by-point fashion, on a magnified scale, as it is scanned by a narrow beam of light or electrons, a laser, a conductive probe, or a topographical probe. Compound Microscopy,Hand-Held Microscopy,Light Microscopy,Optical Microscopy,Simple Microscopy,Hand Held Microscopy,Microscopy, Compound,Microscopy, Hand-Held,Microscopy, Light,Microscopy, Optical,Microscopy, Simple
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002784 Cholesterol The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils. Epicholesterol
D003599 Cytoskeleton The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm. Cytoplasmic Filaments,Cytoskeletal Filaments,Microtrabecular Lattice,Cytoplasmic Filament,Cytoskeletal Filament,Cytoskeletons,Filament, Cytoplasmic,Filament, Cytoskeletal,Filaments, Cytoplasmic,Filaments, Cytoskeletal,Lattice, Microtrabecular,Lattices, Microtrabecular,Microtrabecular Lattices
D004548 Elasticity Resistance and recovery from distortion of shape.
D004905 Erythrocyte Aging The senescence of RED BLOOD CELLS. Lacking the organelles that make protein synthesis possible, the mature erythrocyte is incapable of self-repair, reproduction, and carrying out certain functions performed by other cells. This limits the average life span of an erythrocyte to 120 days. Erythrocyte Survival,Aging, Erythrocyte,Survival, Erythrocyte
D004910 Erythrocyte Membrane The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS. Erythrocyte Ghost,Red Cell Cytoskeleton,Red Cell Ghost,Erythrocyte Cytoskeleton,Cytoskeleton, Erythrocyte,Cytoskeleton, Red Cell,Erythrocyte Cytoskeletons,Erythrocyte Ghosts,Erythrocyte Membranes,Ghost, Erythrocyte,Ghost, Red Cell,Membrane, Erythrocyte,Red Cell Cytoskeletons,Red Cell Ghosts

Related Publications

R B Tishler, and F D Carlson
May 1977, Biochimica et biophysica acta,
R B Tishler, and F D Carlson
December 2000, Bioelectrochemistry (Amsterdam, Netherlands),
R B Tishler, and F D Carlson
January 1996, Ukrainskii biokhimicheskii zhurnal (1978),
R B Tishler, and F D Carlson
January 1978, Methods in enzymology,
R B Tishler, and F D Carlson
April 1991, Biochemical Society transactions,
R B Tishler, and F D Carlson
April 1991, Biochemical Society transactions,
R B Tishler, and F D Carlson
April 1982, Diabetes,
R B Tishler, and F D Carlson
September 1988, Science (New York, N.Y.),
R B Tishler, and F D Carlson
August 1987, Journal of biochemical and biophysical methods,
Copied contents to your clipboard!