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3 edition of The structure of erythrocyte spectrin in negatively stained membrane skeletons found in the catalog.

The structure of erythrocyte spectrin in negatively stained membrane skeletons

Amy Marie McGough

The structure of erythrocyte spectrin in negatively stained membrane skeletons

by Amy Marie McGough

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  • 38 Currently reading

Published .
Written in English


Edition Notes

Statementby Amy Marie McGough.
Classifications
LC ClassificationsMicrofilm 93/552 (Q)
The Physical Object
FormatMicroform
Paginationviii, 191 leaves
Number of Pages191
ID Numbers
Open LibraryOL1050683M
LC Control Number93629776

  Spectrin is tethered to the cell membrane by vertical interactions with band 3 proteins via ankyrin and to protein Spectrin also has horizontal interactions with protein , actin, tropomodulin, tropomyosin and adducin. Protein interacts with glycophorin C, a trans-membrane protein. Erythrocyte Membrane Proteins Spectrin. Because the red cell membrane skeleton is the paradigm for studies of spectrin-based membrane skeletons in all cells, and because we now know that spectrin and other membrane skeletal proteins invest internal organelles, some transport vesicles, and plasma membranes, and even play a role in nuclear organization, it is more important than ever to understand the structure and function of the red Cited by:

intact erythrocyte membrane skeleton were obtained by negative staining (1, 2), in only one micrograph published by Pinder et al. (12) can one see individual spectrin tetramers and fragmentary hints of the band actin oligomer junc-tions. We have now obtained clear images of the spectrin meshwork from negatively stained preparations that origi-. The erythrocyte, commonly known as a red blood cell (or RBC), is by far the most common formed element: A single drop of blood contains millions of erythrocytes and just thousands of ically, males have about million erythrocytes per microliter (µL) of blood, and females have approximately million per fact, erythrocytes are estimated to make up about 25 .

Organization of the Erythrocyte Membrane. Reference: Luna, EJ and AL Hitt, Cytoskeleton-plasma membrane interactions, Science , The basic structure of the erythrocyte membrane cytoskeleton has been worked out, although some details remain obscure.   RBC Membrane Defects 1. RBC Membrane Defects 2. Meet The Red Cell Shaped like a flattened, bilaterally indented sphere, a biconcave disc In fixed, stained blood smears, erythrocyte appears circular, with a diameter of about 7 to 8 μm and an area of central pallor. Average values for the mean cellular volume in normal subjects range from 80 to fl. Highly elastic and deformable. The .


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The structure of erythrocyte spectrin in negatively stained membrane skeletons by Amy Marie McGough Download PDF EPUB FB2

We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell membrane. Fourier analysis of electron micrographs of spectrin reveals that the alpha and beta subunits are twisted about a common axis, forming a two-start helix with twofold rotational by:   Spectrin is generally believed to play an important role in the erythrocyte membrane's ability to deform elastically.

We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell by: the skeleton, spectrin is a straight molecule that does not display a well-defined structure.

However, by using condi-tions closer to the physiological range, it is possible to obtain micrographs of skeletons that are partially expanded. In the work described below we have examined electron micro-graphs of negatively stained spectrin molecules that are. The structure of the membrane skeleton on the cytoplasmic surface of the erythrocyte plasma membrane was observed in dried human erythrocyte ghosts by atomic force microscopy (AFM), taking advantage of its high sensitivity to small height variations in by: We have studied the structure of negatively stained spectrin in partially expanded membrane skeletons to determine how its molecular structure confers elastic properties on the cell membrane.

intact erythrocyte membrane skeleton were obtained by negative staining(1, 2), in onlyonemicrographpublishedby Pinder et al.

(12) can one see individual spectrin tetramers and fragmentary hints ofthe band actin oligomerjunc-tions. Wehave now obtained clear images of the spectrin meshwork from negatively stained preparations that origi-Cited by: loss of membrane lipid, and increased tendency for affected erythrocytes to fuse The surface area of the erythrocyte skeleton appears to be larger than necessary to cover the inner surface of the erythrocyte.

Theoretical calculations indicate that spectrin molecules may be 3 times longer than. a modeP 6 of the erythrocyte membrane as a visco. elastic protein-lipid gel, and with a threefold increase in the linear dimensions of the membrane skeleton during spreadinglZ.

Compact spectrin molecules are also apparent in samples of mem- brane skeletons examined by negative staining at. Figure ew of the membrane-associated periodic skeleton (MPS) of neurons and its associated proteins. (A) The MPS abundance and organization in different domains of a neuron, from being robust and well organized in the axon initial segment to being completely absent in the cell soma.(B) Axon shafts from sensory neurons in culture, stained against βII-spectrin and imaged by Cited by: FORUM A model of spectrin as a concertina in.

the erythrocyte membrane skeleton To maintain its distinctive biconcave shape, the erythrocyte has a skeleton composed largely of the protein spectrin, which associates closely and exclusively with the cell by: Localization and Structure of the Ankyrin-binding Site on 2-Spectrin erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in.

Cohen, CM, Langley, RC, Foley, SF, Korsgren, C: Functional associations of band in the erythrocyte membrane skeleton and their role in inherited membrane skeletal abnormalities. Prog Clin Biol Res 13 – 29, Cited by:   Filamentous skeletons were liberated from isolated human erythrocyte membranes in Triton X, spread on fenestrated carbon films, negatively stained, and viewed intact and unfixed in the transmission electron microscope.

Two forms of the skeleton were. We have obtained clear images of the erythrocyte membrane skeleton from negatively stained preparations that originate directly from the intact cell but in which the spectrin meshwork is artificially spread to allow close inspection.

Our procedure requires Cited by:   Figure 1 Negative-stain electron microscopy of the isolated, expanded erythrocyte membrane skeletons. (A and B) Low- (A) and medium-magnification (B) electron micrographs of membrane skeletons prepared by Triton X extraction of mouse erythrocyte ghosts, which were adsorbed to carbon-coated grids and negatively stained.

As a result of this Cited by: The erythrocyte membrane skeleton can be thought of as a two-dimensional, pseudo-hexagonal network of spectrin tetramers that meet at vertices consisting of short actin filaments.

In vivo, the distance between actin filaments is about å, but the spectrin tetramer is Cited by: 7. Filamentous skeletons were liberated from isolated human erythrocyte membranes in Triton X, spread on fenestrated carbon films, negatively stained, and viewed intact and unfixed in the.

Erythrocyte shape and membrane integrity is imparted by the membrane skeleton, which can be isolated as a Triton X insoluble structure that retains the biconcave shape of intact erythrocytes. spectrin andactin injunctional complexes is variable, with as few as three or as many as eight spectrin molecules joined to a single actin filament.

The average number of spectrin molecules per junctional complex (Sp/JC) is be-tween five and six in spread, negatively stained skeletons (Byers and Branton, ; Liu et al., ; Ursitti and.

Structure of the Spectrin-Actin Binding Site of Erythrocyte Protein The complete primary structure of the functional site of erythrocyte protein involved in spectrin-actin associations has been determined. The sequence of this domain, which contains 67 amino acids and has a mo- The membrane skeleton is composed of a two.

Proc. Natl. Acad. Sci. USA87() FIG. 1. Electron micrographs of erythrocyte skeletons. Partial expansion of skeletons was achieved by dilution in 2 mM sodium phosphate/ mMMgCI2/ mMdithiothreitol, pH8 (a), orin mMsodium phosphate/ mMMgCl2, pH8 (b), onice.

Thespectrin molecules are linear structures whoselengths vary from Ato A. (Bar = A.)Cited by: -Glycophorin =main RBC glycoprotein,20% of total RBC membrane protein,contains approximately 60% carbohydrate,has most of the membrane sialic acid giving the RBC its negative charge causing RBCs to repel each other.

Consistent with previous work, membrane skeletons that were adsorbed to the carbon support film and negatively stained adopted a circular shape with a diameter of 10–12 μm. Because this diameter is more than twice that of the mature mouse red cell (5–6 μ m), this preparation is thought to represent a stretched, or expanded, state of the skeleton (Fig.

1 A).Cited by: