Exchange-enhanced Ultrastrong Magnon-Magnon Coupling in a Compensated Ferrimagnet

The ultrastrong coupling of (quasi-)particles has gained considerable attention due to its application potential and richness of the underlying physics. Coupling phenomena arising due to electromagnetic interactions are well explored. In magnetically ordered systems, the quantum-mechanical exchange-interaction should furthermore enable a fundamentally different coupling mechanism. Here, we report the observation of ultrastrong intralayer exchange-enhanced magnon-magnon coupling in a compensated ferrimagnet. We experimentally study the spin dynamics in a gadolinium iron garnet single crystal using broadband ferromagnetic resonance. Close to the ferrimagnetic compensation temperature, we observe ultrastrong coupling of clockwise and anticlockwise magnon modes. The magnon-magnon coupling strength reaches more than 30% of the mode frequency and can be tuned by varying the direction of the external magnetic field. We theoretically explain the observed phenomenon in terms of an exchange-enhanced mode-coupling mediated by a weak cubic anisotropy

Protease inhibitors prevent plasminogen-mediated, but not pemphigus vulgaris-induced, acantholysis in human epidermis

Pemphigus is an autoimmune blistering disease of the skin and mucous membranes. It is caused by autoantibodies directed against desmosomes, which are the principal adhesion structures between epidermal keratinocytes. Binding of autoantibodies leads to the destruction of desmosomes resulting in the loss of cell-cell adhesion (acantholysis) and epidermal blisters. The plasminogen activator system has been implicated as a proteolytic effector in pemphigus. We have tested inhibitors of the plasminogen activator system with regard to their potential to prevent pemphigus-induced cutaneous pathology. In a human split skin culture system, IgG preparations of sera from pemphigus vulgaris patients caused histopathologic changes (acantholysis) similar to those observed in the original pemphigus disease. All inhibitors that were tested (active site inhibitors directed against uPA, tPA, and/or plasmin; antibodies neutralizing the enzymatic activity of uPA or tPA; substances interfering with the binding of uPA to its specific cell surface receptor uPAR) failed to prevent pemphigus vulgaris IgG-mediated acantholysis. Plasminogen-mediated acantholysis, however, was effectively antagonized by the synthetic active site serine protease inhibitor WX-UK1 or by p-aminomethylbenzoic acid. Our data argue against applying anti-plasminogen activator/anti-plasmin strategies in the management of pemphigus