TFF1 is membrane-associated in breast carcinoma cell line MCF-7

Lai San Siu, Hanna Romanska, Paul D. Abel, Tuncay Kayademir, Nikolaus Blin, Gordon W.H. Stamp, El Nasir Lalani

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)745-753
Number of pages9
Issue number5
Publication statusPublished - May 2004
Externally publishedYes


  • Breast carcinoma
  • Glycosylphosphatidylinositol
  • TFF1


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