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Cutaneous Biology: In vivo blockade of pemphigus vulgaris acantholysis by inhibition of intracellular signal transduction cascades
Authors: Sanchez-Carpintero-Abad, I. (Ignacio)
España, A. (Agustín)
Pelacho, B. (Beatriz)
Lopez-Moratalla, N. (Natalia)
Rubenstein, D.S. (D. S.)
Diaz, L.A. (L. A.)
Lopez-Zabalza, M.J. (María Jesús)
Keywords: Calmodulin/antagonists & inhibitors/physiology
Immunoglobulin G/immunology
Protein Kinases/physiology
Issue Date: 2004
Publisher: Wiley-Blackwell
Publisher version: http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2133.2004.06147.x/pdf
ISSN: 0007-0963
Citation: Sanchez-Carpintero I, Espana A, Pelacho B, Lopez Moratalla N, Rubenstein DS, Diaz LA, et al. In vivo blockade of pemphigus vulgaris acantholysis by inhibition of intracellular signal transduction cascades. Br J Dermatol 2004 Sep;151(3):565-570.
Abstract
Pemphigus vulgaris (PV) is an autoimmune disease characterized by mucocutaneous intraepithelial blisters and pathogenic autoantibodies against desmoglein 3. The mechanism of blister formation in pemphigus has not been defined; however, in vitro data suggest a role for activation of intracellular signalling cascades. OBJECTIVES: To investigate the contribution of these signalling pathways to the mechanism of PV IgG-induced acantholysis in vivo. METHODS: We used the passive transfer mouse model. Mice were injected with IgG fractions of sera from a patient with PV, with or without pretreatment with inhibitors of proteins that mediate intracellular signalling cascades. RESULTS: Inhibitors of tyrosine kinases, phospholipase C, calmodulin and the serine/threonine kinase protein kinase C prevented PV IgG-induced acantholysis in vivo. CONCLUSIONS: These observations strongly support the role of intracellular signalling cascades in the molecular mechanism of PV IgG-induced acantholysis
Permanent link: http://hdl.handle.net/10171/27343
Appears in Collections:DA - CUN - Bioquímica clínica - Artículos de revista
DA - CUN - Dermatología médico-quirúrgica y venereológica - Artículos de revista

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