Biosynthesis of the Cell Surface Sialomucin from Ascites 13762 Rat Mammary Adenocarcinoma Cells: Intracellular Maturation

1989 ◽  
pp. 71-79
Author(s):  
Steven R. Hull ◽  
Julie Spielman ◽  
Kermit L. Carraway
Keyword(s):  
Cell Surface ◽  
Mammary Adenocarcinoma ◽  
Adenocarcinoma Cells

scholarly journals Mechanism of concanavalin A-induced anchorage of the major cell surface glycoproteins to the submembrane cytoskeleton in 13762 ascites mammary adenocarcinoma cells.

1984 ◽  
Vol 98 (1) ◽  
pp. 179-187 ◽  
Author(s):  
G Jung ◽  
R M Helm ◽  
C A Carraway ◽  
K L Carraway
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Binding Protein ◽  
Gradient Centrifugation ◽  
Sucrose Density Gradient ◽  
Mammary Adenocarcinoma ◽  
Con A ◽  
Sucrose Density Gradient Centrifugation ◽  
Adenocarcinoma Cells ◽  
Triton X

Concanavalin A (Con A)-induced anchorage of the major cell surface sialoglycoprotein component complex (ASGP-1/ASGP-2) was studied in 13762 rat mammary adenocarcinoma sublines with mobile (MAT-B1 subline) and immobile (MAT-C1 subline) cell surface Con A receptors. Treatment of cells, isolated microvilli, or microvillar membranes with Con A resulted in marked retention of ASGP-1 and ASGP-2, a Con A-binding protein, in cytoskeletal residues of both sublines obtained by extraction with Triton X-100 in PBS. When Con A-treated microvillar membranes were extracted with a buffer containing Triton X-100, the sialoglycoprotein complex was found associated in the residues with a transmembrane complex composed of actin, a 58,000-dalton polypeptide, and a cytoskeleton-associated glycoprotein (CAG), also a Con A-binding protein, in MAT-C1 membranes, and of actin and CAG in MAT-B1 membranes. Untreated membrane Triton residues retained very little ASGP-1/ASGP-2 complex. Association of the sialoglycomembrane complex and the transmembrane complex was also demonstrated in Con A-treated, but not untreated, microvilli by their comigration on CsCl gradients. Association of both complexes with the cytoskeleton of microvilli was shown by sucrose density gradient centrifugation. A fraction of the polymerized actin comigrated with the transmembrane complex alone in the absence of Con A and with both the transmembrane complex and the sialoglycoprotein complex in the presence of Con A. From these results we propose that anchorage of the sialoglycoprotein complex to the cytoskeleton on Con A treatment occurs by cross-linking ASGP-2, the major cell surface Con A-binding component, to CAG of the transmembrane complex, which is natively linked to the cytoskeleton via its actin component. Since Con A-induced anchorage occurs in sublines with mobile and immobile receptors, the anchorage process cannot be responsible for the differences in receptor mobility between the sublines.

Aminolevulic acid transport in murine mammary adenocarcinoma cells

2002 ◽  
Vol 30 (3) ◽  
pp. A71-A71
Author(s):  
M. Bermudez Moretti ◽  
S. Correa Garcia ◽  
C. Perotti ◽  
A. Casas ◽  
A. Batlle
Keyword(s):  
Mammary Adenocarcinoma ◽  
Acid Transport ◽  
Adenocarcinoma Cells
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