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This Article Accepted manuscript (PDF) All Versions of this Article: JOE-08-0479v1 JOE-08-0479v2 201/1/115    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Panina, S. Articles by Rasmussen, L. Search for Related Content PubMed PubMed Citation Articles by Panina, S. Articles by Rasmussen, L.

S Panina, Cytokine Biology, Novo Nordisk A/S, Maaloev, 2760, Denmark
E Galsgaard, Histology, Novo Nordisk A/S, Maaloev, Denmark
B Rasmussen, Nordsjaellands Hospital, Hilleroed, Denmark
C Folkesson, Cytokine Biology, Novo Nordisk A/S, Maaloev, Denmark
L Christensen, Biopharm Chemistry, Novo Nordisk A/S, Maaloev, Denmark
M Berchtold, Biology, University of Copenhagen, Copenhagen, Denmark
L Rasmussen, Cytokine Biology, Novo Nordisk A/S, Maaloev, Denmark

Correspondence: Svetlana Panina, Email: svt{at}novonordisk.com

Abstract

The pituitary hormone prolactin (PRL) is involved in tumorigenesis in rodents and human. PRL promotes proliferation, survival and migration of cancer cells acting via the prolactin receptor (PRLR). Aiming to perform a large-scale immunohistochemical screening of human mammary carcinomas for PRLR expression we evaluated the specificity of commercially available anti-human PRLR antibodies (B6.2, U5, PRLRi pAb, 1A2B1, 250448 and H-300). The latter three antibodies were found to specifically recognize PRLR. The relative PRLR expression level detected with these antibodies closely reflected the level of 125I-PRL binding to the cell surface. The monoclonal antibody 250448 was specific for the N-glycosylated form of PRLR and blocked PRL binding and signalling. The PRLRi polyclonal antibody recognized cytokeratin-18. The monoclonal antibody B6.2, previously used in a number of studies, was found to lack specificity for PRLR and to rather recognize a PRLR-associated protein. The monoclonal antibody U5 raised against the rat PRLR did not cross-react with the human receptor. Only one monoclonal antibody, 1A2B1, was found useful for detection of PRLR in immunohistochemical applications. This antibody recognized PRLR expressed in human breast cancer cell lines and decidual cells in tissue sections of human placenta. Screening of 160 mammary adenocarcinomas demonstrated significant immunoreactivity in only 4 tumours, indicating that PRLR is generally not strongly up-regulated in human breast cancer. However, even very low level of PRLR expression was found to be sufficient to mediate PRL responsiveness in breast cancer cell lines.

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