Redox proteomic evaluation of bleaching and alkali damage in human hair.

OBJECTIVE: Protein modification and damage in human hair, resulting from environmental, cosmetic and grooming stresses, create changes to visual and tactile characteristics and correlates with consumer perception of quality. This study outlines molecular-level evaluation of modification resulting from peroxide (bleaching) and alkaline straightening (relaxing) treatments. METHODS: Redox proteomic profiling of virgin, bleached and relaxed hair tresses was performed, with comprehensive qualitative characterization of modification and semi-quantitative evaluation of damage through adaptation of a new damage scoring system. Modifications were mapped to specific locations in the hair proteome and a range of potential damage marker peptides identified. RESULTS: Virgin hair contained a baseline level of modification, consistent with environmental oxidative insult during hair growth. Hydrogen peroxide bleaching resulted in significantly increased levels of oxidative damage observable at the molecular level. This treatment also resulted in enhanced levels of dehydroalanine and dehydration products; modifications typically associated with alkali or thermal treatment and not previously been reported as a product of hair bleaching. Relaxation treatment with sodium hydroxide increased the formation of dehydroalanine and dehydration products and moderately enhanced the levels of oxidation. Cysteine was the predominant modification site for both bleaching and alkali damage. CONCLUSION: This study validates the utility and power of redox proteomic-based approaches to characterizing hair modification. This offers potential application to a wide range of damage types, as well as evaluation of new damage mitigation and repair technologies.

WT1-specific serum antibodies in patients with leukemia.

WT1 is an oncogenic protein expressed by the Wilms' tumor gene and overexpressed in the majority of acute myelogenous leukemias (AMLs) and chronic myelogenous leukemias (CMLs). The current study analyzed the sera of patients with AML and CML for the presence of antibodies to full-length and truncated WT1 proteins. Sixteen of 63 patients (25%) with AML had serum antibodies reactive with WT1/full-length protein. Serum antibodies from all 16 were also reactive with WT1/NH2-terminal protein. By marked contrast, only 2 had reactivity to WT1/COOH-terminal protein. Thus, the level of immunological tolerance to the COOH terminus may be higher than to the NH2 terminus. The WT1/COOH-terminal protein contains four zinc finger domains with homology to other self-proteins. By implication, these homologies may be related to the increased immunological tolerance. Results in patients with CML were similar with antibodies reactive to WT1/full-length protein detectable in serum of 15 of 81 patients (19%). Antibodies reactive with WT1/NH2-terminal protein were present in the serum of all 15, whereas antibodies reactive with WT1/COOH-terminal protein were present in only 3. By contrast to results in leukemia patients, antibodies reactive with WT1/full-length protein were detected in only 2 of 96 normal individuals. The greater incidence of antibody in leukemia patients provides strong evidence that immunization to the WT1 protein occurred as a result of patients bearing malignancy that expresses WT1. These data provide further stimulus to test therapeutic vaccines directed against WT1 with increased expectation that the vaccines will be able to elicit and/or boost an immune response to WT1.