Prolactin is an autocrine growth factor for the Jurkat human T-leukemic cell line

Matera, Lina; Cutufia, Miguel Angel; Geuna, Massimo; Contarini, M.; Buttiglieri, Stefano; Galin, Shawn; Fazzari, Annamaria; Cavaliere, Cristina

doi:10.1016/s0165-5728(97)00096-9

Cited by 57 publications

(42 citation statements)

References 38 publications

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“…50 The present study demonstrates that treatment with PRL for 30 min triggers the tyrosine phosphorylation of JAK-2, STAT-3, STAT-5, and paxillin in the Jurkat-T human leukemic cell line, a PRL target cell. 54 This finding is consistent with extensive evidence showing that PRL stimulates tyrosine phosphorylation of JAK-2, STAT-3, and STAT5 in other cell types. 5,6,55 Although PRL-induced tyrosine phosphorylation of JAK-2, STAT-5, paxillin, and FAK has been reported in breast cancer cells, 31 this is the first study showing the activation of the JAK/STAT/paxillin pathway in immune cells.…”

Section: Discussionsupporting

confidence: 90%

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Macotela

Nava

et al. 2005

Laboratory Investigation

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Attachment of leukocytes to endothelial cells is an essential step for the extravasation and recruitment of cells at sites of inflammation. The pituitary hormone prolactin (PRL) is involved in the inflammatory process. Here, we show that treatment with PRL of human peripheral blood mononuclear cells (PBMC) stimulates their adhesion to human umbilical vein endothelial cells (HUVEC) activated by interleukin-1b. Stimulation of adhesion by PRL is mediated via integrins leukocyte functional antigen-1 (LFA-1) and very late antigen-4 (VLA-4), because immunoneutralization of both integrins prevents PRL action. Also, PRL promotes the adhesion of PBMC to immobilized intercellular adhesion molecule-1 and fibronectin, ligands for LFA-1 and VLA-4, respectively. Stimulation of integrin-mediated cell adhesion by PRL may involve the activation of chemokine receptors, because PRL upregulates the expression of the G-protein-coupled chemokine receptor CXCR3 in PBMC, and pertussis toxin, a specific G-protein inhibitor, blocks PRL stimulation of PBMC adhesion to HUVEC. In addition, PRL stimulates tyrosine phosphorylation pathways leading to leukocyte adhesion. PRL triggered the tyrosine phosphorylation of Janus kinase-2, of signal transducer and activator of transcription-3 and 5, and of the focal adhesion protein paxillin. Furthermore, genistein, a tyrosine kinase inhibitor, blocked PRLstimulated adhesion of PBMC and Jurkat T-cells to HUVEC. These results suggest that PRL promotes integrinmediated leukocyte adhesion to endothelial cells via chemokine receptors and tyrosine phosphorylation signaling pathways.

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Section: Discussionsupporting

confidence: 90%

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Macotela

Nava

et al. 2005

Laboratory Investigation

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“…The rationale for selecting Jurkat cells, instead of PRL-dependent Nb-2 rat lymphoma cell line, was to have a human model system previously shown to be PRL sensitive (Matera et al, 1997). Apoptosis was induced in Jurkat cells either by starvation in RPMI 1640 medium supplemented with 0.5% charcoal-striped FCS or by treatment of the cells with the Fas crosslinking CH-11 mAb, dexamethasone, or VP-16 for various time periods (Figure 1).…”

Section: Prolactin and Apoptosis Induction In Jurkat Cellsmentioning

confidence: 99%

Role of prolactin receptor and CD25 in protection of circulating T lymphocytes from apoptosis in patients with breast cancer

et al. 2003

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Prolactin (PRL) has been reported to inhibit apoptosis in various cell types and to serve as a cofactor in the upregulation of CD25 on T cells during activation. We investigated a possible relation between prolactin receptor (PRL-R) or IL-2 receptor alpha (IL-2Ra, CD25) expression on circulating T lymphocytes and their apoptosis in patients with breast cancer. Peripheral blood mononuclear cells obtained from 25 patients, 25 normal controls (NC) and three cord blood samples were evaluated for Annexin V binding and expression of CD95, CD25, and PRL-R on CD3 + T cells by multicolour flow cytometry. Plasma levels of PRL, sCD95L, and sIL-2R were determined in patients and controls and related to T-cell apoptosis. The ability of PRL to protect T cells from apoptosis induced by various agents was also studied. Expression of PRL-R on the surface of T cells was comparable in patients with breast cancer and NC, but PRL plasma levels in patients were significantly lower (Po0.05). In patients, 18711% (mean7s.d.) of CD3 + cells bound Annexin V, compared to 976% in NC (Po0.0004). Percentages of CD3 + Fas + and CD3 + CD25 + cells were higher in the peripheral circulation of patients than NC (Po0.0001 and o0.04, respectively). Levels of sFasL were lowest in plasma of the patients with the highest proportions of CD3 + Fas + T cells. Most T cells undergoing apoptosis were CD3 + CD25 À in patients, and the proportion of CD3 + CD25 À Annexin V + cells was significantly increased in patients compared to NC (Po0.006). Ex vivo PRL protected T cells from starvation-induced or anti-CD3Ab-induced but not from Fas/FasL-dependent apoptosis. These results indicate that expression of CD25 but not of PRL-R on the surface of activated T lymphocytes appears to be involved in modulating Fas/Fas -ligand interactions, which are, in part, responsible for apoptosis of T lymphocytes and excessive turnover of immune cells in the circulation of patients with breast cancer.

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“…The mouse MAb B6.2 also immunoprecipitates the 40 kDa form of the receptor, although the 90 kDa form is dominant (Banerjee et al,1993). The optimal dilution for the 2 MAbs was 1:10, as established in pilot experiments using the positive cell line Jurkat (Matera et al,1997) and the negative cell lines M07 (Bellone et al,1995). Anti-human PRL rabbit antisera employed in this study are: 1.…”

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confidence: 99%

“…In addition, IM9-P3, a human plasmocytoma cell line (DiMattia et al,1988), kindly provided by G. DiMattia (University of Western Ontario, London, Canada), was used as a positive control for production of the 23.5 (non-glycosylated) and 25 (glycosylated) kDa forms of PRL. The hepG-2 liver cell line, kindly provided by Dr. L. Silengo (University of Turin, Italy) has already been used by us in previous studies as a negative control for PRL (Matera et al,1997). …”

mentioning

confidence: 99%

Expression of prolactin and prolactin receptors by non-Hodgkin's lymphoma cells

et al. 2000

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Prolactin is an autocrine growth factor for the Jurkat human T-leukemic cell line

Cited by 57 publications

References 38 publications

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Prolactin stimulates integrin-mediated adhesion of circulating mononuclear cells to endothelial cells

Role of prolactin receptor and CD25 in protection of circulating T lymphocytes from apoptosis in patients with breast cancer

Expression of prolactin and prolactin receptors by non-Hodgkin's lymphoma cells

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