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Blood, 1 April 2005, Vol. 105, No. 7, pp. 2812-2820. Prepublished online as a Blood First Edition Paper on December 2, 2004; DOI 10.1182/blood-2004-07-2630.
IMMUNOBIOLOGY Tumor protein D52 (TPD52): a novel B-cell/plasma-cell molecule with unique expression pattern and Ca2+-dependent association with annexin VIFrom the Section of Physiopathology, Department of Clinical and Experimental Medicine, University of Perugia, Perugia, Italy; Geneva Proteomics Research Center, Genève, Switzerland; Institute of Hematology, University of Foggia, Foggia, Italy; Institute of Pathology, Policlinico S. Orsola, Bologna, Italy; Leukemia Research Fund (LRF) Immunodiagnostic Unit, John Radcliffe Hospital, Oxford, United Kingdom; Institute of Pathology, Niguarda Hospital, Milan, Italy; Division of Pathology, Oncology Reference Center, National Tumor Institute, Aviano, Italy; and Oncology Research Unit and the University of Sydney Department of Pediatrics and Child's Health, The Children's Hospital at Westmead, NSW, Australia.
We generated a murine monoclonal antibody (B28p) detecting an antigenic determinant shared by the immunoglobulin superfamily receptor translocation-associated 1 (IRTA1) receptor (the immunogen used to raise B28p) and an unrelated 28-kDa protein that was subsequently subjected to extensive characterization. The expression of the 28-kDa protein in normal lymphohematopoietic tissues was restricted to B cells and plasma cells and clearly differed from that expected for IRTA1 (selectively expressed by mucosa-associated lymphoid tissue [MALT] marginal zone B cells). Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE)/mass-spectrometry analysis identified the 28-kDa protein as human tumor protein D52 (TPD52), whose expression had been previously described only in normal and neoplastic epithelia. Specific B28p reactivity with TPD52 was confirmed by immunostaining/immunoblotting of TPD52-transfected cells. TPD52 expression pattern in normal and neoplastic B cells was unique. In fact, unlike other B-cell molecules (paired box 5 [PAX5], CD19, CD79a, CD20, CD22), which are down-regulated during differentiation from B cells to plasma cells, TPD52 expression reached its maximum levels at the plasma cell stage. In the Thiel myeloma cell line, TPD52 bound to annexin VI in a Ca2+-dependent manner, suggesting that these molecules may act in concert to regulate secretory processes in plasma cells, similarly to what was observed in pancreatic acinar cells. Finally, the anti-TPD52 monoclonal antibody served as a valuable tool for the diagnosis of B-cell malignancies.
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