PubMed · 14458884
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M KOUT, H BAITSCH. 1962-02-15. [Serum haptoglobin groups].. https://pubmed.ncbi.nlm.nih.gov/14458884/
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A high-throughput affinity capture and reduction approach was developed for phenotype and post-translational modification analysis of a complexed globular protein, haptoglobin (Hp), directly from human plasma. Hp was selectively retrieved utilizing anti-Hp antibodies immobilized onto affinity pipette tips, eluted onto a formatted mass spectrometer target for reduction of Hp alpha-chains (Hpalpha1 and Hpalpha2) and subjected to subsequent MALDI-MS analysis. The affinity capture and reduction approach was originally developed from a pre-extraction reduction methodology that was optimized to an affinity capture post-reduction technique for intact Hp alpha-chain variant analysis, phenotype classification and ensuing post-translational variant detection. Three common Hp phenotypes (1-1, 2-1 and 2-2) were assigned according to detection of Hpalpha1 and/or Hpalpha2 reduced intact chain(s) average mass(es). The affinity capture post-reduction approach was scaled for high-throughput Hp alpha-chain phenotype analysis from a normal plasma cohort. The entire sample cohort was successfully analyzed and phenotyped using the developed approach. Additionally, Hp post-translational variants were detected and assigned via accurate MS analyses. The results of this study suggest use of the methodology in future analyses of other similarly complexed proteins and in normal versus disease cohort population proteomics studies.
BACKGROUND: Haptoglobin (Hp) is an acute-phase reactant, known to be produced mainly in the liver. Haptoglobin can also be detected in the cytoplasm of normal epidermal Langerhans cells (LCs), and can prevent their functional maturation. The synthesis of Hp in skin cells has not been well studied. METHODS: We examined Hp expression at mRNA and protein levels by in situ hybridization and immunohistochemistry, respectively, in normal human skin and in the skin of patients with psoriasis, lichen planus, erythroderma, seborrheic keratosis, verruca vulgaris, basal cell carcinoma, systemic lupus erythematosus, pemphigus and bullous pemphigoid. RESULTS: (1) Haptoglobin mRNA was expressed in the epidermal keratinocytes (KCs), the epithelial cells of hair follicles, sebaceous glands and eccrine glands in normal skin and all dermatoses investigated. (2) Whereas compared with normal skin, the Hp mRNA in KCs of patients with psoriasis, lichen planus, erythroderma, seborrhoea keratosis and verruca vulgaris was significantly intensified, it was weaker in patients with systemic lupus erythematosus, pemphigus and bullous pemphigoid. (3) Haptoglobin protein only stained positively in some KCs of patients with psoriasis, lichen planus and erythroderma. (4) Although some but not all epidermal LCs were positively stained with anti-Hp antibody in normal skin and in skin samples from all patients, the ratios of Hp-positive LCs/total LCs were significantly higher in those diseases with intensified Hp mRNA in KCs. CONCLUSIONS: Skin is another extrahepatic organ where Hp can be synthesized by KCs. The expression of Hp mRNA in KCs and the Hp protein in both LCs and KCs appears to be correlated with the amount of inflammation, which might indicate that skin itself is involved in down-regulating the local inflammatory reaction by KC-synthesized Hp.