publication . Article . 2011

Keratinocyte Secretion of Cyclophilin B via the Constitutive Pathway Is Regulated through Its Cyclosporin-Binding Site

Paula Fearon; Ann A Lonsdale-Eccles; O Kehinde Ross; Carole Todd; Aparna Sinha; Fabrice Allain; Nick J Reynolds;
Open Access
  • Published: 01 May 2011 Journal: Journal of Investigative Dermatology, volume 131, issue 5, pages 1,085-1,094 (issn: 0022-202X, Copyright policy)
  • Publisher: Elsevier BV
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 1pM 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 CypB W128A -green fluorescent protein (GFP) from the ER. Photobleaching studies revealed a sig...
free text keywords: Cell Biology, Biochemistry, Molecular Biology, Dermatology, Original Article, Secretion, Brefeldin A, chemistry.chemical_compound, chemistry, Golgi apparatus, symbols.namesake, symbols, Endoplasmic reticulum, Green fluorescent protein, Immunology, Cyclophilin, Biology, Constitutive secretory pathway, Secretory pathway
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