TFF1 is membrane-associated in breast carcinoma cell line MCF-7.
Trefoil factor family (TFF) domain peptides, products of mucin-secreting epithelial cells, are thought to influence mucosal integrity. Molecular studies revealed that mammalian TFFs lack transmembrane domains. Using immunocytochemistry and FACS analysis we demonstrated the association of TFF1 with the cell membrane in MCF-7 (a breast adenocarcinoma cell line), and tested the hypothesis that glycosylphosphatidylinositol (GPI) linkage is the mechanism for this association. Cleavage of GPI anchorage using phospholipase C did not affect TFF1 binding to the cell membrane. Our results demonstrate for the first time that TFF1 is associated with the cell membrane of MCF-7 cells and is not linked via a GPI anchor.
Siu
Lai-San
LS
Department of Histopathology, Imperial College, Hammersmith Campus, London W12 0NN, UK.
Romanska
Hanna
H
Abel
Paul D
PD
Kayademir
Tuncay
T
Blin
Nikolaus
N
Stamp
Gordon W H
GW
Lalani
El-Nasir
el-N
D001943:Breast Neoplasms / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D005260:Female; D005434:Flow Cytometry; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D006801:Humans; D011506:Proteins / Q000378:metabolism*; D000071163:Trefoil Factor-1; D014407:Tumor Cells, Cultured; D025521:Tumor Suppressor Proteins; D010738:Type C Phospholipases / Q000378:metabolism*
D017261:Glycosylphosphatidylinositols; D011506:Proteins; C051838:TFF1 protein, human; D000071163:Trefoil Factor-1; D025521:Tumor Suppressor Proteins; D010738:Type C Phospholipases