title: Regulated expression of MUC1 epithelial antigen in erythropoiesis.
abstract: MUC1 is a large surface glycoprotein expressed by epithelial cells, which is overexpressed and aberrantly glycosylated in carcinomas. MUC1 is involved in epithelial cell interactions and appears to function as a signal-transducing molecule. The finding that MUC1 can also be expressed in the haematopoietic lineages prompted us to further investigate the possible function(s) of this molecule in haematopoietic cells. In bone marrow differentiating cells, MUC1 was strongly and selectively expressed during erythropoiesis; it was also weakly expressed during megakaryocytopoiesis and granulomonocytopoiesis; however, no correlation between MUC1 and differentiation marker expression was observed in these lineages. In vitro CD34+ cells, induced towards erythroid differentiation, acquired MUC1 transiently, while expressing increasing levels of the lineage marker glycophorin A. MUC1 was absent in the circulating erythrocytes. During erythropoiesis, MUC1 expression was transcriptionally regulated and the molecule underwent phosphorylation. To investigate the possible role of MUC1 during erythropoiesis, we studied the ability of MUC1 to act as ligand for cell-cell interaction. The sialylated MUC1 glycoforms selectively expressed on erythroid cells were able to bind the macrophage-restricted molecule sialoadhesin. These results suggest that MUC1 can function as a cross-talk molecule between the erythroblasts and the surrounding cells during erythropoiesis.
authors.affiliation: Department of Experimental Medicine and Pathology, University La Sapienza, Italy.
authors.forename: Aurelia
authors.initials: A
authors.lastname: Rughetti
authors.forename: Mauro
authors.initials: M
authors.lastname: Biffoni
authors.forename: Luca
authors.initials: L
authors.lastname: Pierelli
authors.forename: Hassan
authors.initials: H
authors.lastname: Rahimi
authors.forename: Giuseppina
authors.initials: G
authors.lastname: Bonanno
authors.forename: Serena
authors.initials: S
authors.lastname: Barachini
authors.forename: Ilenia
authors.initials: I
authors.lastname: Pellicciotta
authors.forename: Chiara
authors.initials: C
authors.lastname: Napoletano
authors.forename: Edoardo
authors.initials: E
authors.lastname: Pescarmona
authors.forename: Angelo
authors.initials: A
authors.lastname: Del Nero
authors.forename: Patrizia
authors.initials: P
authors.lastname: Pignoloni
authors.forename: Luigi
authors.initials: L
authors.lastname: Frati
authors.forename: Marianna
authors.initials: M
authors.lastname: Nuti
mesh_terms: D018952:Antigens, CD34; D015415:Biomarkers / Q000032:analysis; D015153:Blotting, Western / Q000379:methods; D001854:Bone Marrow Cells / Q000166:cytology*; D002448:Cell Adhesion / Q000502:physiology; D002450:Cell Communication / Q000502:physiology; D002454:Cell Differentiation; D002461:Cell Line, Transformed; D002478:Cells, Cultured; D004920:Erythropoiesis / Q000502:physiology*; D005434:Flow Cytometry; D006021:Glycophorins / Q000032:analysis; D006098:Granulocytes / Q000166:cytology; D006801:Humans; D007124:Immunoenzyme Techniques; D008533:Megakaryocytes / Q000166:cytology; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism / Q000502:physiology*; D010766:Phosphorylation; D011971:Receptors, Immunologic / Q000378:metabolism; D063267:Sialic Acid Binding Ig-like Lectin 1
chemical_list: D018952:Antigens, CD34; D015415:Biomarkers; D006021:Glycophorins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D011971:Receptors, Immunologic; C571166:SIGLEC1 protein, human; D063267:Sialic Acid Binding Ig-like Lectin 1