TY - JOUR
T1 - Expression of S100P and its novel binding partner S100PBPR in early pancreatic cancer
AU - Dowen, Sally E.
AU - Crnogorac-Jurcevic, Tatjana
AU - Gangeswaran, Rathi
AU - Hansen, Mikkel
AU - Eloranta, Jyrki J.
AU - Bhakta, Vipul
AU - Brentnall, Teresa A.
AU - Lüttges, Jutta
AU - Klöppel, Gunther
AU - Lemoine, Nick R.
PY - 2005/1
Y1 - 2005/1
N2 - S100P is a member of the S100 family of calcium-binding proteins and there have been several recent reports of its overexpression in pancreatic ductal adenocarcinoma (PDAC). We have used Far Western screening and in vitro interaction assays to identify and confirm a novel target protein for SlOOP. We have named this protein S100PBPR, and shown that its interaction with S100P is dependent on Ca2+ or Mg2+. S100PBPR was found to localize to cell nuclei where S100P is also present, and the two proteins co-immunoprecipitate. By in situ hybridization, S100PBPR transcript was found in islet cells but not duct cells of the healthy pancreas. Both S100P and S100PBPR were detected by quantitative real-time polymerase chain reaction in pancreatic intraepithelial neoplasia (PanIN) and PDAC samples, and in situ hybridization revealed the presence of S100PBPR transcript in malignant PDAC cells. These data suggest that an interaction between S100P and S100PBPR may be involved in early pancreatic cancer. S100P was further investigated in PanIN lesions and immunohistochemical analysis showed its expression to correlate significantly with increasing grade of PanINs, being found as early as PanIN-1 with more prevalent expression in PanIN-2 and -3. These data suggest that S100P can be added to the genetic progression model for PDAC.
AB - S100P is a member of the S100 family of calcium-binding proteins and there have been several recent reports of its overexpression in pancreatic ductal adenocarcinoma (PDAC). We have used Far Western screening and in vitro interaction assays to identify and confirm a novel target protein for SlOOP. We have named this protein S100PBPR, and shown that its interaction with S100P is dependent on Ca2+ or Mg2+. S100PBPR was found to localize to cell nuclei where S100P is also present, and the two proteins co-immunoprecipitate. By in situ hybridization, S100PBPR transcript was found in islet cells but not duct cells of the healthy pancreas. Both S100P and S100PBPR were detected by quantitative real-time polymerase chain reaction in pancreatic intraepithelial neoplasia (PanIN) and PDAC samples, and in situ hybridization revealed the presence of S100PBPR transcript in malignant PDAC cells. These data suggest that an interaction between S100P and S100PBPR may be involved in early pancreatic cancer. S100P was further investigated in PanIN lesions and immunohistochemical analysis showed its expression to correlate significantly with increasing grade of PanINs, being found as early as PanIN-1 with more prevalent expression in PanIN-2 and -3. These data suggest that S100P can be added to the genetic progression model for PDAC.
UR - http://www.scopus.com/inward/record.url?scp=19944385563&partnerID=8YFLogxK
U2 - 10.1016/S0002-9440(10)62234-1
DO - 10.1016/S0002-9440(10)62234-1
M3 - Article
C2 - 15632002
AN - SCOPUS:19944385563
SN - 0002-9440
VL - 166
SP - 81
EP - 92
JO - American Journal of Pathology
JF - American Journal of Pathology
IS - 1
ER -
