We review the literature regarding axillary hyperhidrosis, discuss normal sweat gland function and postulate on the respective roles of the eccrine, apocrine and apo-eccrine glands in the pathophysiology of excessive axillary sweating.
We have found that topical pimecrolimus 1% cream is an effective treatment for GLP. Local irritation can limit its use, but it may be better tolerated than topical tacrolimus: three of our complete responders had previously been intolerant of tacrolimus. Topical pimecrolimus may be a valuable second-line treatment for patients with steroid-related side-effects or steroid-resistant GLP.
We present long-term follow-up data (mean follow-up 4.8 years, range 10 months-10.5 years) of the treatment of DMC with IRC. Treatment was well tolerated, with few side-effects, and cosmetic outcome was excellent. While recurrence rates were similar to many existing therapies, the ease of delivery, tolerability and cosmetic results make IRC a favourable option for the treatment of DMC.
Cyclophilin B (CypB) is an endoplasmic reticulum (ER)-resident member of the cyclophilin family of proteins that bind cyclosporin A (CsA). We report that as in other cell types, CypB trafficked from the ER and was secreted by keratinocytes into the media in response to CsA. Concentrations as low as 1 p of CsA induced secretion of CypB. Using brefeldin A, we showed that CypB is secreted from keratinocytes via the constitutive secretory pathway. We defined that substitution of tryptophan residue 128 in the CsA-binding site of CypB with alanine resulted in dissociation of CypBW128A-green fluorescent protein (GFP) from the ER. Photobleaching studies revealed a significant reduction in the diffusible mobility of CypBW128A-GFP compared with CypBWT-GFP, consistent with redistribution of CypBW128A-GFP into secretory vesicles disconnected from the ER/Golgi network. Furthermore, CsA significantly decreased the mobility of CypBWT-GFP but not CypBW128A-GFP. These studies demonstrate that therapeutically relevant concentrations of CsA regulate secretion of CypB by keratinocytes, and that a key residue within the CsA-binding site of CypB controls retention of CypB within the ER and regulates entry into the secretory pathway. As keratinocytes express CypB receptors (CD147) and CypB exhibits chemotactic properties, these data have implications for the therapeutic effects of CsA in inflammatory skin disease.
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