ABSTRACT
Neutrophilic dermatoses (NDs) are inflammatory skin conditions that are not associated with infection. The classification and clinical approach to these conditions in children is poorly described. This review classifies these conditions into five nosological subtypes: Sweet's syndrome, pyoderma gangrenosum, aseptic pustules, neutrophilic urticarial dermatoses, and Marshall's syndrome. In addition, we review the various secondary diseases that need to be excluded in the clinical management of the NDs of childhood, with a focus on the autoinflammatory conditions that the reader may not be familiar with. We propose a practical clinical approach to these disorders.
Subject(s)
Neutrophil Infiltration , Skin Diseases/classification , Abscess/classification , Abscess/diagnosis , Abscess/drug therapy , Cataract/classification , Cataract/diagnosis , Cataract/drug therapy , Child , Collagen Type XI/classification , Collagen Type XI/deficiency , Craniofacial Abnormalities/classification , Craniofacial Abnormalities/diagnosis , Craniofacial Abnormalities/drug therapy , Diagnosis, Differential , Hearing Loss, Sensorineural/classification , Hearing Loss, Sensorineural/diagnosis , Hearing Loss, Sensorineural/drug therapy , Humans , Osteochondrodysplasias/classification , Osteochondrodysplasias/diagnosis , Osteochondrodysplasias/drug therapy , Pyoderma Gangrenosum/classification , Pyoderma Gangrenosum/diagnosis , Pyoderma Gangrenosum/drug therapy , Skin Diseases/diagnosis , Skin Diseases/drug therapy , Sweet Syndrome/classification , Sweet Syndrome/diagnosis , Sweet Syndrome/drug therapy , Urticaria/classification , Urticaria/diagnosis , Urticaria/drug therapyABSTRACT
In a subset of human lipomas, a specific t(3;12) chromosome translocation gives rise to HMGA2-LPP fusion protein, containing the amino (N)-terminal DNA binding domains of HMGA2 fused to the carboxyl (C)-terminal LIM domains of LPP. In addition to its role in adipogenesis, several observations suggest that HMGA2-LPP is linked to chondrogenesis. Here, we analyzed whether HMGA2-LPP promotes chondrogenic differentiation, a marker of which is transactivation of the alpha 2 type XI collagen gene (Col11a2). Real-time PCR analysis showed that HMGA2-LPP and COL11A2 were co-expressed. Luciferase assay demonstrated that either of HMGA2-LPP, wild-type HMGA2 or the N-terminal HMGA2 transactivated the Col11a2 promoter in HeLa cells, while the C-terminal LPP did not. RT-PCR analysis revealed that HMGA2-LPP transcripts in lipomas with the fusion were 591-fold of full-length HMGA2 transcripts in lipomas without the fusion. These results indicate that in vivo overexpression of HMGA2-LPP promotes chondrogenesis by upregulating cartilage-specific collagen gene expression through the N-terminal DNA binding domains.
