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.

Regulated expression of MUC1 epithelial antigen in erythropoiesis / Rughetti, Aurelia; Biffoni, Marco; Pierelli, Luca; RAHIMI KOSHKAKI, Hassan; Giuseppina, Bonanno; Serena, Barachini; Ilenia, Pellicciotta; Napoletano, Chiara; Pescarmona, Edoardo; DEL NERO, Angelo; Patrizia, Pignoloni; Frati, Luigi; Nuti, Marianna. - In: BRITISH JOURNAL OF HAEMATOLOGY. - ISSN 0007-1048. - STAMPA. - 120:2(2003), pp. 344-352. [10.1046/j.1365-2141.2003.04038.x]

Regulated expression of MUC1 epithelial antigen in erythropoiesis

RUGHETTI, Aurelia;BIFFONI, Marco;PIERELLI, LUCA;RAHIMI KOSHKAKI, HASSAN;NAPOLETANO, Chiara;PESCARMONA, Edoardo;DEL NERO, Angelo;FRATI, Luigi;NUTI, Marianna
2003

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.
2003
cell-cell interaction; erythropoiesis; haematopoiesis; muc1; sialoadhesin
01 Pubblicazione su rivista::01a Articolo in rivista
Regulated expression of MUC1 epithelial antigen in erythropoiesis / Rughetti, Aurelia; Biffoni, Marco; Pierelli, Luca; RAHIMI KOSHKAKI, Hassan; Giuseppina, Bonanno; Serena, Barachini; Ilenia, Pellicciotta; Napoletano, Chiara; Pescarmona, Edoardo; DEL NERO, Angelo; Patrizia, Pignoloni; Frati, Luigi; Nuti, Marianna. - In: BRITISH JOURNAL OF HAEMATOLOGY. - ISSN 0007-1048. - STAMPA. - 120:2(2003), pp. 344-352. [10.1046/j.1365-2141.2003.04038.x]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/383520
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