Isolation and Characterization of a Tumor-Associated NADH Oxidase (tNOX) from the HeLa Cell Surface

2001 ◽  
Vol 391 (2) ◽  
pp. 149-159 ◽  
Author(s):  
Ferda Yantiri ◽  
D.James Morré
Keyword(s):  
Cell Surface ◽  
Hela Cell ◽  
Nadh Oxidase ◽  
Isolation And Characterization

Molecular Cloning and Characterization of a Tumor-Associated, Growth-Related, and Time-Keeping Hydroquinone (NADH) Oxidase (tNOX) of the HeLa Cell Surface†

Biochemistry ◽  
2002 ◽  
Vol 41 (11) ◽  
pp. 3732-3741 ◽  
Author(s):  
Pin-Ju Chueh ◽  
Chinpal Kim ◽  
NaMi Cho ◽  
Dorothy M. Morré ◽  
D. James Morré
Keyword(s):  
Cell Surface ◽  
Hela Cell ◽  
Molecular Cloning ◽  
Nadh Oxidase

scholarly journals Isolation of an adhesion-mediating protein from chick neural retina adherons.

1985 ◽  
Vol 101 (3) ◽  
pp. 1071-1077 ◽  
Author(s):  
D Schubert ◽  
M LaCorbiere
Keyword(s):  
Cell Surface ◽  
Heparan Sulfate ◽  
Cultured Cells ◽  
Cell Types ◽  
Neural Retina ◽  
Cell Surface Receptor ◽  
Isolation And Characterization ◽  
Surface Receptor ◽  
Adhesive Interactions

Adherons are high molecular weight glycoprotein complexes which are released into the growth medium of cultured cells. They mediate the adhesive interactions of many cell types, including those of embryonic chick neural retina. The cell surface receptor for chick neural retina adherons has been purified, and shown to be a heparan sulfate proteoglycan (Schubert, D., and M. LaCorbiere, 1985, J. Cell Biol., 100:56-63). This paper describes the isolation and characterization of a protein in neural retina adherons which interacts specifically with the cell surface receptor. The 20,000-mol-wt protein, called retinal purpurin (RP), stimulates neural retina cell-substratum adhesion and prolongs the survival of neural retina cells in culture. The RP protein interacts with heparin and heparan sulfate, but not with other glycosaminoglycans. Monovalent antibodies against RP inhibit RP-cell adhesion as well as adheron-cell interactions. The RP protein is found in neural retina, but not in other tissues such as brain and muscle. These data suggest that RP plays a role in both the survival and adhesive interactions of neural retina cells.

scholarly journals Isolation and partial characterization of antibody- and globin-enriched complexes from membranes of dense human erythrocytes

1991 ◽  
Vol 278 (1) ◽  
pp. 57-62 ◽  
Author(s):  
R Kannan ◽  
J Yuan ◽  
P S Low
Keyword(s):  
Membrane Protein ◽  
Cell Surface ◽  
Integral Membrane Protein ◽  
Protein Band ◽  
Reticuloendothelial System ◽  
Band 3 ◽  
Isolation And Characterization ◽  
Protein Clusters ◽  
Associated Proteins

In previous studies we have described a process whereby an erythrocyte in biochemical distress can initiate its own removal by macrophages of the reticuloendothelial system. This process involves the clustering of the integral membrane protein band 3 by denatured haemoglobin and the subsequent recognition of the exofacial poles of clustered band 3 and associated proteins by autologous antibodies. To determine whether this clearance pathway might mediate normal cell turnover, the fraction of normal erythrocytes containing the 0.5% densest cells, which are known to be destined for immediate removal, was isolated and characterized biochemically. This densest fraction was found to contain 6 times more membrane-bound globin (haemichromes) and 10 times more surface-bound autologous IgG than the other fractions containing cells of lower density. To determine whether the autologous IgG was physically associated with the haemichrome-stabilized membrane protein clusters, a procedure was developed for isolation and characterization of the microscopic aggregates. The isolated aggregates were found to contain a disulphide-cross-linked mixture of several membrane proteins, predominantly haemichromes, spectrin and band 3. Although the aggregates constituted only 0.09% of the total membrane protein, they still contained approximately 55% of the total cell-surface IgG. Since in control studies anti-(blood group A) antibodies, which are distributed randomly over the surface of type A cells, could not be recovered in the aggregate, we conclude that the autologous cell-surface IgGs were physically associated with the membrane protein clusters when they were co-isolated with them in our procedure. Thus the 640-fold enrichment of autologous IgG in the aggregates compared with regions of the membrane devoid of tightly clustered protein suggests that sites of integral protein clustering either are non-specifically sticky to IgG or are viewed as foreign or ‘non-self’ by the immune system and aggressively opsonized with IgG.

Molecular Cloning and Characterization of a Candidate Human Growth-Related and Time-Keeping Constitutive Cell Surface Hydroquinone (NADH) Oxidase

Biochemistry ◽  
2008 ◽  
Vol 47 (52) ◽  
pp. 14028-14038 ◽  
Author(s):  
Ziying Jiang ◽  
Nina M. Gorenstein ◽  
Dorothy M. Morré ◽  
D. James Morré
Keyword(s):  
Cell Surface ◽  
Molecular Cloning ◽  
Nadh Oxidase ◽  
Human Growth
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