BD31 mAb, raised against a line of gastric carcinoma cells, reacts with intercellular boundaries of human transformed cells originating from carcinomas or sarcomas growing in epithelial-like clusters as well as in primary cultures of epithelial and endothelial cells. BD31 also reacts with intercellular rims of normal and transformed epithelial tissues and is particularly abundant in glands and fast-growing epithelia but absent in nervous and muscle tissues as well as in blood and in mesenchyme-derived cells. Confocal analysis indicates that BD31 is located in dots at cell-cell contacts but not in basal and apical domains of cultured and in situ epithelial cells. mAb BD31 precipitates a 100 kDa protein from cells labeled with [S-35]methionine or [H-3]glucosamine as well as from I-125-surface-labeled cells. This glycoprotein resists to trypsin in the presence of Ca2+, releases an 80 kDa fragment in the medium and does not
A MONOCLONAL-ANTIBODY IDENTIFIES A NOVEL GPI-ANCHORED GLYCOPROTEIN INVOLVED IN EPITHELIAL INTERCELLULAR-ADHESION
CREMONA , OTTAVIO;
1994-01-01
Abstract
BD31 mAb, raised against a line of gastric carcinoma cells, reacts with intercellular boundaries of human transformed cells originating from carcinomas or sarcomas growing in epithelial-like clusters as well as in primary cultures of epithelial and endothelial cells. BD31 also reacts with intercellular rims of normal and transformed epithelial tissues and is particularly abundant in glands and fast-growing epithelia but absent in nervous and muscle tissues as well as in blood and in mesenchyme-derived cells. Confocal analysis indicates that BD31 is located in dots at cell-cell contacts but not in basal and apical domains of cultured and in situ epithelial cells. mAb BD31 precipitates a 100 kDa protein from cells labeled with [S-35]methionine or [H-3]glucosamine as well as from I-125-surface-labeled cells. This glycoprotein resists to trypsin in the presence of Ca2+, releases an 80 kDa fragment in the medium and does notI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
