The Role of Oxidation in Diseases of the Human Erythrocyte

1990 ◽  
pp. 34-47
Author(s):  
Bertram Lubin ◽  
Frans Kuypers ◽  
Elliott Vichinsky ◽  
Daniel Chiu
Keyword(s):  
Human Erythrocyte

Role of spectrin in membrane fusion and in shape change of human erythrocyte ghost

1978 ◽  
Vol 36 (2) ◽  
pp. 328-329
Author(s):  
Hideo Hayashi ◽  
Yoshikazu Hirai ◽  
John T. Penniston
Keyword(s):  
Conformational Changes ◽  
Human Erythrocyte ◽  
Shape Change ◽  
Membrane Surface ◽  
Slight Modification ◽  
Active Role ◽  
Main Role ◽  
Bank Blood ◽  
Human Erythrocyte Ghost

Spectrin is a membrane associated protein most of which properties have been tentatively elucidated. A main role of the protein has been assumed to give a supporting structure to inside of the membrane. As reported previously, however, the isolated spectrin molecule underwent self assemble to form such as fibrous, meshwork, dispersed or aggregated arrangements depending upon the buffer suspended and was suggested to play an active role in the membrane conformational changes. In this study, the role of spectrin and actin was examined in terms of the molecular arrangements on the erythrocyte membrane surface with correlation to the functional states of the ghosts.Human erythrocyte ghosts were prepared from either freshly drawn or stocked bank blood by the method of Dodge et al with a slight modification as described before. Anti-spectrin antibody was raised against rabbit by injection of purified spectrin and partially purified.

scholarly journals Human erythrocyte sorbitol metabolism and the role of sorbitol dehydrogenase

Diabetologia ◽  
1988 ◽  
Vol 31 (10) ◽  
pp. 766-770 ◽  
Author(s):  
Y. Nagasaka ◽  
S. Fujii ◽  
T. Kaneko
Keyword(s):  
Human Erythrocyte ◽  
Sorbitol Dehydrogenase ◽  
Sorbitol Metabolism

Role of Glycosphingolipids in HIV-1 Entry: Requirement of Globotriosylceramide (Gb3) in CD4/CXCR4-dependent Fusion

1999 ◽  
Vol 19 (4) ◽  
pp. 317-325 ◽  
Author(s):  
Anu Puri ◽  
Peter Hug ◽  
Kristine Jernigan ◽  
Patrick Rose ◽  
Robert Blumenthal
Keyword(s):  
Structural Analysis ◽  
Cell Fusion ◽  
Envelope Glycoprotein ◽  
Human Erythrocyte ◽  
Head Group ◽  
Specific Interactions ◽  
Cd4 Cells ◽  
Fusion Site ◽  
Hiv 1

We have recently shown that addition of human erythrocyte glycosphingolipids (GSL) to non-human CD4+ or GSL-depleted human CD4+ cells rendered those cells susceptible to gp120-gp41-mediated cell fusion (Puri et al., BBRC, 1998). One GSL fraction (Fraction 3) isolated from human erythrocyte GSL mixture exhibited the highest recovery of fusion following incorporation into CD4+ non-human and GSL-depleted HeLa-CD4 cells (HeLa-CD4/GSL-). Structural analysis of Fraction 3 showed that this GSL had identical head group as the known GSL, Gal(α1→4)Gal(β1→4)Glc-Ceramide (Gb3) (Puri et al., PNAS, 1998). Here we report that presence of Gb3 in CD4+/CXCR4+ cells but not CD4+/CXCR4- cells allows fusion with HIV-1Lai-envelope glycoprotein expressing cells (TF228). Therefore, Gb3 functions in conjunction with HIV-1 co-receptor, CXCR4 to promote fusion. We propose that Gb3 functions by recruiting CD4 and/or CXCR4 at the fusion site through structurally specific interactions.

scholarly journals The role of inositol phospholipids in the association of band 4.1 with the human erythrocyte membrane

1993 ◽  
Vol 211 (3) ◽  
pp. 671-681 ◽  
Author(s):  
Philippe GASCARD ◽  
Tadeusz PAWELCZYK ◽  
John M. LOWENSTEIN ◽  
Carl M. COHEN
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Inositol Phospholipids

Role of Spectrin in Human Erythrocyte IMP Aggregation

1980 ◽  
Vol 38 ◽  
pp. 622-623
Author(s):  
CM. Doerschuk ◽  
R.S. Weinstein ◽  
T.L. Steck
Keyword(s):  
Human Erythrocyte ◽  
Low Ph ◽  
Human Erythrocytes ◽  
Partial Removal ◽  
Intramembrane Particles ◽  
Cytoplasmic Surface ◽  
Inner Surface ◽  
Induced Aggregation ◽  
Experimentally Induced

A wide variety of perturbations result in aggregation of intramembrane particles (IMP) in human erythrocytes1–3. Experimentally induced aggregation may involve partial removal of the spectrin-actin reticulum from the inner surface of the membrane followed by incubations under conditions which decrease the solubility of spectrin and promote rebinding of spectrin to the cytoplasmic surface2. In this study, we have re-evaluated the role of spectrin in IMP aggregation induced by low pH and by proteolysis1, 3.

scholarly journals Mechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins.

1985 ◽  
Vol 101 (4) ◽  
pp. 1379-1385 ◽  
Author(s):  
C L Howe ◽  
L M Sacramone ◽  
M S Mooseker ◽  
J S Morrow
Keyword(s):  
Brush Border ◽  
Human Erythrocyte ◽  
Binding Capacity ◽  
Cytoskeletal Regulation ◽  
Associated Proteins ◽  
Chicken Erythrocytes ◽  
Related Proteins ◽  
Inside Out

The spectrins isolated from chicken erythrocytes and chicken intestinal brush border, TW260/240, share a common alpha subunit and a tissue-specific beta subunit. The ability of these related proteins to bind human erythrocyte inside out vesicles (IOVs) and human erythrocyte ankyrin in vitro have been quantitatively compared with human erythrocyte spectrin. Chicken erythrocyte spectrin binds human IOVs and human ankyrin with affinities nearly identical to that for human erythrocyte spectrin. TW260/240 does not significantly bind to either IOVs or ankyrin. These results demonstrate a remarkable tissue preservation of ankyrin-binding capacity, even between diverse species, and confirm the role of the avian beta-spectrins in modulating this functionality. Avian brush border spectrin may represent a unique spectrin which serves primarily as a filament cross-linker and which does not interact strongly with membrane-associated proteins.

Sign in / Sign up

Export Citation Format

Share Document