Paraneoplastic pemphigus without antibodies to desmoglein 1 and 3.

Paraneoplastic pemphigus is a severe autoimmune blistering disease presenting in the setting of underlying malignancy. Paraneoplastic pemphigus is associated with diffuse painful stomatitis throughout the oral cavity with extension to the lips. The cutaneous findings are varied and have been described as lichenoid, pemphigoid, and targetoid lesions. Herein, we report a patient with paraneoplastic pemphigus whose routine testing led to a diagnosis of pemphigus vulgaris. However, further testing was pursued revealing an antibody profile consistent with paraneoplastic pemphigus. Subsequent neoplastic workup revealed an intra-abdominal mass. Our case represents a subtle, non-classic presentation of paraneoplastic pemphigus and suggests the importance of a comprehensive investigative work-up in atypical cases of pemphigus.

Psoriasis mimicking mycosis fungoides clinically.

Psoriasis is a complex, chronic immune-mediated inflammatory disease that most commonly presents as well-demarcated erythematous plaques with micaceous scale, affecting roughly 3-4% of the US population [1-4]. Clinically, lesions are often well demarcated thick, scaly, erythematous plaques, characteristically located on the extensor surfaces, such as elbows and knees [1]. In most cases, clinical impression is sufficient to diagnose psoriasis. However, sometimes psoriasis can mimic other cutaneous disorders and biopsy may be warranted to discover the diagnosis. We report an unusual presentation of psoriasis clinically mimicking mycosis fungoides.

Petrified Ear - A Case Report and Review of the Literature.

Petrified ear is the transformation of normal, flexibleauricular cartilage into rigid, immobile auricularcartilage due to abnormal calcification or ossification.Etiologies of petrified ear include tissue injury,systemic endocrine diseases, congenital disorders,or petrified ear of unknown origin. We present a caseof a 69-year-old male with a one-month history ofnon-painful rigidity of the right ear that was found tohave petrified ear of unknown etiology confirmed byradiography.

Integrin α2ß1 mediates tyrosine phosphorylation of vascular endothelial cadherin induced by invasive breast cancer cells.

The molecular mechanisms that regulate the endothelial response during transendothelial migration (TEM) of invasive cancer cells remain elusive. Tyrosine phosphorylation of vascular endothelial cadherin (VE-cad) has been implicated in the disruption of endothelial cell adherens junctions and in the diapedesis of metastatic cancer cells. We sought to determine the signaling mechanisms underlying the disruption of endothelial adherens junctions after the attachment of invasive breast cancer cells. Attachment of invasive breast cancer cells (MDA-MB-231) to human umbilical vein endothelial cells induced tyrosine phosphorylation of VE-cad, dissociation of ß-catenin from VE-cad, and retraction of endothelial cells. Breast cancer cell-induced tyrosine phosphorylation of VE-cad was mediated by activation of the H-Ras/Raf/MEK/ERK signaling cascade and depended on the phosphorylation of endothelial myosin light chain (MLC). The inhibition of H-Ras or MLC in endothelial cells inhibited TEM of MDA-MB-231 cells. VE-cad tyrosine phosphorylation in endothelial cells induced by the attachment of MDA-MB-231 cells was mediated by MDA-MB-231 α(2)ß(1) integrin. Compared with highly invasive MDA-MB-231 breast cancer cells, weakly invasive MCF-7 breast cancer cells expressed lower levels of α(2)ß(1) integrin. TEM of MCF-7 as well as induction of VE-cad tyrosine phosphorylation and dissociation of ß-catenin from the VE-cad complex by MCF-7 cells were lower than in MDA-MB-231 cells. These processes were restored when MCF-7 cells were treated with ß(1)-activating antibody. Moreover, the response of endothelial cells to the attachment of prostatic (PC-3) and ovarian (SKOV3) invasive cancer cells resembled the response to MDA-MB-231 cells. Our study showed that the MDA-MB-231 cell-induced disruption of endothelial adherens junction integrity is triggered by MDA-MB-231 cell α(2)ß(1) integrin and is mediated by H-Ras/MLC-induced tyrosine phosphorylation of VE-cad.