Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 2812-2820 |
| Number of pages | 9 |
| Journal | Blood |
| Volume | 105 |
| Issue number | 7 |
| DOIs | |
| Publication status | Published - Apr 1 2005 |
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ASJC Scopus subject areas
- Hematology
Cite this
Tumor protein D52 (TPD52) : A novel B-cell/plasma-cell molecule with unique expression pattern and Ca2+-dependent association with annexin VI. / Tiacci, Enrico; Orvietani, Pier Luigi; Bigerna, Barbara; Pucciarini, Alessandra; Corthals, Garry L.; Pettirossi, Valentina; Martelli, Maria P.; Liso, Arcangelo; Benedetti, Roberta; Pacini, Roberta; Bolli, Niccolò; Pileri, Stefano; Pulford, Karen; Gambacorta, Marcello; Carbone, Antonino; Pasquarello, Carla; Scherl, Alexander; Robertson, Helen; Sciurpi, Maria Teresa; Alunni-Bistocchi, Giovanni; Binaglia, Luciano; Byrne, Jennifer A.; Falini, Brunangelo.
In: Blood, Vol. 105, No. 7, 01.04.2005, p. 2812-2820.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Tumor protein D52 (TPD52)
T2 - A novel B-cell/plasma-cell molecule with unique expression pattern and Ca2+-dependent association with annexin VI
AU - Tiacci, Enrico
AU - Orvietani, Pier Luigi
AU - Bigerna, Barbara
AU - Pucciarini, Alessandra
AU - Corthals, Garry L.
AU - Pettirossi, Valentina
AU - Martelli, Maria P.
AU - Liso, Arcangelo
AU - Benedetti, Roberta
AU - Pacini, Roberta
AU - Bolli, Niccolò
AU - Pileri, Stefano
AU - Pulford, Karen
AU - Gambacorta, Marcello
AU - Carbone, Antonino
AU - Pasquarello, Carla
AU - Scherl, Alexander
AU - Robertson, Helen
AU - Sciurpi, Maria Teresa
AU - Alunni-Bistocchi, Giovanni
AU - Binaglia, Luciano
AU - Byrne, Jennifer A.
AU - Falini, Brunangelo
PY - 2005/4/1
Y1 - 2005/4/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=20144388563&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=20144388563&partnerID=8YFLogxK
U2 - 10.1182/blood-2004-07-2630
DO - 10.1182/blood-2004-07-2630
M3 - Article
C2 - 15576473
AN - SCOPUS:20144388563
VL - 105
SP - 2812
EP - 2820
JO - Blood
JF - Blood
SN - 0006-4971
IS - 7
ER -