Cytochemistry of colloidal iron binding to the surface of hela cells and human erythrocytes

1976 ◽  
Vol 48 (1) ◽  
pp. 71-80 ◽  
Author(s):  
M. Mareel ◽  
C. Dragonetti ◽  
M. C. Van Peteghem
1977 ◽  
Vol 53 (4) ◽  
pp. 285-290 ◽  
Author(s):  
M. C. Van Peteghem ◽  
M. Mareel ◽  
C. Dragonetti

1975 ◽  
Vol 64 (3) ◽  
pp. 538-550 ◽  
Author(s):  
P P Silva ◽  
A Martínez-Palomo ◽  
A Gonzalez-Robles

Treatment of living entamoeba histolytica cells with low concentrations of concanavalin A (con A) and peroxidase results in redistribution of the plasma membrane con A receptors to one pole of the cell where a morphologically distinct region--the uroid--is formed. Capping of con A receptors is not accompanied by parallel accumulation of ruthenium red-stainable components. In capped cells, the pattern of distribution of acidic sites ionized at pH 1.8 (labeled by colloidal iron) at the outer surface and of membrane particles (integral membrane components revealed by freeze-fracture) is not altered over the uroid region. Cytochemistry of substrate-attached microexudate located in regions adjacent to E. histolytica cells demonstrates the presence of con A binding sites and ruthenium red- and alcian blue-stainable components and the absent of colloidal iron binding sites. In a previous report we demonstrated that glycerol-induced aggregation of the plasma membrane particles is accompanied by a discontinuous distribution of colloidal iron binding sites, while con A receptors and acidic sites ionized at pH 4.0 remain uniformly distributed over the cell surface. Taken together, our experiments show that, in E. histolytica cells, peripheral membrane components may move independently of integral components and, also, that certain surface determinants may redistribute independently of others. These results point to the complexity of the membrane structure-cell surface relationship in E. histolytica plasma membranes relative to the membrane of the erythrocyte ghost where integral components (the membrane-intercalated particles) contain all antigens, receptors, and anionic sites labeled so far. We conclude that fluidity of integral membrane components (integral membrane fluidity) cannot be inferred from the demonstration of the mobility of surface components nor, conversely, can the fluidity of peripheral membrane components (peripheral membrane fluidity) be assumed from demonstration of the mobility of integral membrane components.


2004 ◽  
Vol 14 (1-2) ◽  
pp. 41-46 ◽  
Author(s):  
Jan Kovár ◽  
Hana Stýbrová ◽  
Petr Novák ◽  
Marie Ehrlichová ◽  
Jaroslav Truksa ◽  
...  

1990 ◽  
Vol 25 (3) ◽  
pp. 129-134 ◽  
Author(s):  
Masaharu Ozaki ◽  
Yoichiro Miyake ◽  
Masaharu Shirakawa ◽  
Toshinobu Takemoto ◽  
Hiroshi Okamoto ◽  
...  

1984 ◽  
Vol 30 (1) ◽  
pp. 52-56
Author(s):  
G. M. Wiseman ◽  
C. F. Martin ◽  
P. J. McNicol

Pilated gonococci added to human erythrocytes apparently bind to polypeptide band 3 and inhibit chloride–bicarbonate exchange across the membrane in contrast with nonpilated organisms. Known covalent inhibitors of anion transport (4,4′-diisothiocyano-2,2′-disulphonic acid stilbene and α-cyano-4-hydroxycinnamic acid) inhibit chloride efflux from erythrocytes and also reduce hemagglutination titres, strongly suggesting that band 3 is the major host-cell receptor involved in all interaction between gonococci and erythrocytes. In studies of other cell species, however, band 3 prepared from human erythrocytes inhibited adherence of pilated gonococci to human foreskin and HeLa cells, but was without effect in human buccal, Vero, and mouse L cells.


1972 ◽  
Vol 69 (12) ◽  
pp. 3708-3712 ◽  
Author(s):  
E. Robbins ◽  
J. Fant ◽  
W. Norton

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