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Stable isotope labeling method for the investigation of protein haptenation by electrophilic skin sensitizers.
Parkinson, Erika; Boyd, Pete; Aleksic, Maja; Cubberley, Richard; O'Connor, David; Skipp, Paul.
Afiliación
  • Parkinson E; Centre for Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK Centre for Proteomic Research, Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, UK epp@soton.ac.uk.
  • Boyd P; Centre for Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK Centre for Proteomic Research, Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, UK.
  • Aleksic M; Safety and Environmental Assurance Centre, Unilever, Colworth Science Park, Sharnbrook, MK44 1LQ, UK.
  • Cubberley R; Safety and Environmental Assurance Centre, Unilever, Colworth Science Park, Sharnbrook, MK44 1LQ, UK.
  • O'Connor D; Department of Biological Sciences, Xi'an Jiaotong-Liverpool University, SIP Suzhou, Jiangsu Province 215123, China.
  • Skipp P; Centre for Biological Sciences, University of Southampton, Southampton, SO17 1BJ, UK Centre for Proteomic Research, Institute for Life Sciences, University of Southampton, Southampton, SO17 1BJ, UK.
Toxicol Sci ; 142(1): 239-49, 2014 Nov.
Article en En | MEDLINE | ID: mdl-25145658
The risk of contact sensitization is a major consideration in the development of new formulations for personal care products. However, developing a mechanistic approach for non-animal risk assessment requires further understanding of haptenation of skin proteins by sensitizing chemicals, which is the molecular initiating event causative of skin sensitization. The non-stoichiometric nature of protein haptenation results in relatively low levels of modification, often of low abundant proteins, presenting a major challenge for their assignment in complex biological matrices such as skin. Instrumental advances over the last few years have led to a considerable increase in sensitivity of mass spectrometry (MS) techniques. We have combined these advancements with a novel dual-labeling/LC-MS(E) approach to provide an in-depth direct comparison of human serum albumin (HSA), 2,4-dinitro-1-chlorobenzene (DNCB), 5-chloro-2-methyl-4-isothiazolin-3-one (MCI), trans-cinnamaldehyde, and 6-methyl coumarin. These data have revealed novel insights into the differences in protein haptenation between sensitizers with different reaction mechanisms and sensitizing potency; the extreme sensitizers DNCB and MCI were shown to modify a greater number of nucleophilic sites than the moderate sensitizer cinnamaldehyde; and the weak/non-sensitizer 6-methyl coumarin was restricted to only a single nucleophilic residue within HSA. The evaluation of this dual labeling/LC-MS(E) approach using HSA as a model protein has also demonstrated that this strategy could be applied to studying global haptenation in complex mixtures of skin-related proteins by different chemicals.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tiazoles / Acroleína / Albúmina Sérica / Cumarinas / Dermatitis por Contacto / Dinitroclorobenceno / Haptenos Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Toxicol Sci Asunto de la revista: TOXICOLOGIA Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Tiazoles / Acroleína / Albúmina Sérica / Cumarinas / Dermatitis por Contacto / Dinitroclorobenceno / Haptenos Tipo de estudio: Risk_factors_studies Límite: Humans Idioma: En Revista: Toxicol Sci Asunto de la revista: TOXICOLOGIA Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos