Extensive Pyoderma gangrenosum following breast reduction and abdominoplasty: a challenging case.

Post-surgical pyoderma gangrenosum (P SP G) is a subtype of pyoderma gangrenosum in which non-infectious, painful, inflammatory ulcerative nodules develop in incision sites. Delayed diagnosis and surgical interventions of P SP G often contribute to worsened morbidity. We present a case of a 55-year-old female diagnosed with severe P SP G after breast augmentation and abdominoplasty.

Diversity, Equity, and Inclusion: Sex and Gender and Intersectionality With Race and Ethnicity in Psoriatic Disease.

Sex (biological attributes associated with being male or female) and gender (sociocultural-driven traits and behaviors related to being a man or a woman) are emerging as important determinants of disease course and response to therapy in patients with psoriasis and psoriatic arthritis (PsA). Although psoriatic disease (PsD) is equally prevalent in men and women, the condition affects them in different and unique ways, giving rise to sex- and gender-related differences in clinical presentation, including baseline disease activity, disease course, and response to treatment. Better understanding of the roles sex and gender play in the development and evolution of PsD has the potential to improve patient care. The Group for Research and Assessment of Psoriasis and Psoriatic Arthritis (GRAPPA) continues its effort to highlight issues related to diversity, equity, and inclusion in people with PsD by dedicating a session during the annual meeting to sex and gender and their intersectionality with race and ethnicity in individuals with PsA.

A novel androgen receptor mutant, A748T, exhibits hormone concentration-dependent defects in nuclear accumulation and activity despite normal hormone-binding affinity.

Functional analysis of androgen receptor (AR) gene mutations isolated from prostate cancer has led to the identification of residues that play important roles in the structure and function of the receptor. Here we report the characteristics of a novel AR mutation A748T located in helix 5 of the ligand-binding domain, which was identified in metastatic prostate cancer. Despite a normal hormone-binding affinity, A748T causes hormone concentration-dependent defects in nuclear accumulation and transcriptional activation. Moreover, when equivalent amounts of DNA are transfected, the mutant is expressed at much lower levels than the wild-type AR (ARWT). Treatment with geldanamycin to disrupt receptor-heat shock protein complexes rapidly decreases the levels of ARWT but not A748T, suggesting that the lower expression and rapid degradation rate of A748T is due to weaker interactions with heat shock proteins. Further analysis revealed that hormone dissociates from A748T five times faster than from ARWT. Loss of the ability to form stable amino/carboxyl-terminal interactions causes accelerated dissociation rates in some AR mutants. However, A748T exhibits normal amino/carboxyl-terminal interactions at high hormone concentrations, suggesting that the mutation alters interactions with ligand. Consistent with this conclusion, our structural model predicts that A748T disrupts crucial contact points with ligand, thereby altering the conformation of the ligand-binding domain.