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Breast involvement is a rare event in SLE patients. The most frequent presentation is lupus panniculitis with skin erithema, tenderness, and parenchymal nodules. However, when breast masses are detected in SLE patients without significant superficial inflammation, it is mandatory to rule out breast carcinoma. Here, we report the case of a 47-year-old woman with an 18-year-long history of SLE, who presented with a suspicious breast mass. Since surgical trauma has been reported to be able to exacerbate breast inflammation in lupus mastitis, an ultrasound-guided minimally invasive Mammotome biopsy was performed to obtain tissue samples for histological and immunohistochemical examinations. Histology was consistent with lupus mastitis. The patient was already on mycophenolate mofetil and hydroxychloroquine. At the latest follow-up visit 6 years later, no progression of the breast lesion was observed.

Background: IL-4 is central to the development of TH2 responses and atopic conditions. We have reported cyclo-oxygenase (COX)-independent inhibition of IL-4 transcription by therapeutic concentrations of acetylsalicylic acid (ASA) and salicylic acid (SA) (Blood 2001;97:1742). We hypothesized that salicylates target the Ca2+-dependent IL-4 transactivator, NFAT. Methods: To elucidate this point, we transfected Jurkat T cells (JKT) with luciferase plasmids driven by the proximal IL-4 promoter (pIL4.96), or by artificial promoters consisting of either a multimeric consensus NFAT/AP-1 composite site (pNFAT) or the AP-1-independent IL-4 P1 NFAT consensus (pIL-4.P1). Cells were stimulated with the Ca2+ ionophore A23187 and treated with ASA (1 mM) or the benchmark COX inhibitor, flurbiprofen (FBP, 0.01 mM). Results: Luciferase expression in pIL4.96 transfectants was significantly reduced by ASA (58.8±3.8% of control) but not FBP (96.8±8.8%; n=8). In stark contrast, NFAT-dependent transcription was upregulated by ASA in both pNFAT (614.5±120.6%; n=12) and pIL4.P1 transfectants (937.5±371%; n=8). NFAT function was only weakly enhanced by FBP in these experiments (133.2±14.72% of pIL4.P1; n=3). In parallel experiments the effects of salicylates on NFAT activation in JKT and peripheral blood T cells (PBT) was analyzed by immunofluorescent staining and Western blot using NFAT-1 and NFAT-2 specific antibodies. As previously shown, Ca2+-mediated stimulation induced the rapid (<30 min) and transient nuclear translocation of NFAT family members. Treatment with ASA caused prolonged NFAT nuclear expression presumably due to delayed cytosolic re-export. NFAT nuclear overexpression was apparent at 2 and 3 hours post-stimulation in both JKT and PBT. Conclusions: We conclude that the effects of salicylates on IL-4 expression cannot be ascribed to inhibition of NFAT activity, and point to the involvement of a novel, unique molecular pathway of IL-4 transcriptional activation in T cells. Uncovering this pathway might lead to the development of selective immune regulatory regimens in the control of atopic disease.