title: Expression of epidermal CAMP changes in parallel with permeability barrier status.
abstract: Two critical defensive functions of the outer epidermis, the permeability barrier and antimicrobial defense, share certain structural and biochemical features. Moreover, three antimicrobial peptides (AMPs), i.e., mouse β-defensin 3 (mBD3), mouse cathelicidin antimicrobial peptide (mCAMP), and the neuroendocrine peptide, catestatin (Cst), all localize to the outer epidermis, and both mBD3 and mCAMP are secreted from the epidermal lamellar bodies with other organelle contents that subserve the permeability barrier. These three AMPs are upregulated in response to acute permeability barrier disruption, whereas conversely, mCAMP-/- mice (unable to combat Gram-positive pathogens) also display abnormal barrier homeostasis. To determine further whether these two functions are co-regulated, we investigated changes in immunostaining for these three AMPs in skin samples in which the permeability barrier function in mice had been either compromised or enhanced. Compromised or enhanced barrier function correlated with reduced or enhanced immunohistochemical expression of mCAMP, respectively, but conversely with Cst expression, likely due to the role of this AMP as an endogenous inhibitor of cathelicidin expression. mBD3 expression correlated with experimental barrier perturbations, but poorly with developmental changes in barrier function. These studies show that changes in cathelicidin and Cst expression parallel changes in permeability barrier status, with a less clear relationship with mBD3 expression.
authors.affiliation: Dermatology Service, Hospital Universitario de Canarias, University of La Laguna, Tenerife, Spain.
authors.forename: Marina
authors.initials: M
authors.lastname: Rodriguez-Martin
authors.forename: Gemma
authors.initials: G
authors.lastname: Martin-Ezquerra
authors.forename: Mao-Qiang
authors.initials: MQ
authors.lastname: Man
authors.forename: Melanie
authors.initials: M
authors.lastname: Hupe
authors.forename: Jong-Kyung
authors.initials: JK
authors.lastname: Youm
authors.forename: Donald S
authors.initials: DS
authors.lastname: Mackenzie
authors.forename: Soyun
authors.initials: S
authors.lastname: Cho
authors.forename: Carles
authors.initials: C
authors.lastname: Trullas
authors.forename: Walter M
authors.initials: WM
authors.lastname: Holleran
authors.forename: Katherine A
authors.initials: KA
authors.lastname: Radek
authors.forename: Peter M
authors.initials: PM
authors.lastname: Elias
mesh_terms: D000375:Aging / Q000378:metabolism; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D054804:Cathelicidins / Q000235:genetics / Q000378:metabolism*; D002463:Cell Membrane Permeability / Q000187:drug effects / Q000502:physiology*; D053379:Chromogranin A / Q000378:metabolism; D004817:Epidermis / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D005260:Female; D008297:Male; D051379:Mice; D008812:Mice, Hairless; D018345:Mice, Knockout; D023421:Models, Animal; D010446:Peptide Fragments / Q000378:metabolism; D013315:Stress, Psychological / Q000378:metabolism; D014466:Ultraviolet Rays / Q000009:adverse effects; D023083:beta-Defensins / Q000378:metabolism
chemical_list: D023181:Antimicrobial Cationic Peptides; D054804:Cathelicidins; D053379:Chromogranin A; D010446:Peptide Fragments; D023083:beta-Defensins; C540070:beta-defensin 3, mouse; C109084:chromogranin A (344-364)