Atopic dermatitis is a common, complex disease that frequently follows a chronic, relapsing course. The disease can impact the quality of life (QOL) of patients and families to a significant degree. Patients and caregivers may focus on unproven triggers at the expense of proper skin care. A multidisciplinary approach is needed to comprehensively evaluate triggers and response to treatment, address confounding factors including sleep disruption, and educate patients and caregivers.
Food allergies may impact the emotions of patients through both direct and indirect mechanisms. Direct mechanisms include the effects on the central nervous system from biologic mediators released during an allergic reaction to food. Indirect mechanisms include the stress of coping with a food allergy--for example, food preparation and avoidance--as well as managing the fear of the potential consequences of ingesting the food. Indirect effects may also be mediated through family members--for example, the impact of a parent's stress on the child. These relationships are difficult to study, in part because many patients who report food allergy symptoms do not have objective symptoms when challenged with the offending food. Symptoms may be misinterpreted as food allergy more often by patients with certain psychological profiles. In this paper, relevant literature is reviewed, and clinical treatment designed to minimize the emotional suffering of patients and their families is presented through the description of a case vignette.
We have previously described a method for producing recombinant methionyl bovine PRL (Met-bPRL), which is as bioactive as the authentic hormone in the Nb2 cell lactogen bioassay; in contrast, a Met-bPRL variant lacking tyrosine 28 was essentially devoid of bioactivity. In the present study we have investigated this loss of bioactivity at the molecular level by determining the bioactivities of a number of Met-bPRL variants engineered to contain specific changes in their primary structures. It was found that the presence of tyrosine per se at the 28 position in Met-bPRL was not essential for high bioactivity, since Met-bPRL variants prepared by replacing tyrosine 28 with other amino acids (arginine, phenylalanine, alanine, and histidine) still had substantial bioactivity (40-74% that of Met-bPRL). Neither was the loss of bioactivity related to a shift in the relative positions of conserved histidines 27 and 30; in fact, histidine 27 was found not to be essential for the bioactivity of the hormone. The loss of bioactivity after deletion of tyrosine 28 from Met-bPRL appears to be related to the removal of an amino acid from the middle of a putative helix (no. 1) rather than to the loss of a residue specific to lactogen function. This suggestion is supported by the finding that Met-bPRL variants obtained by deletion of selected single amino acids from center domains of putative helix 2, 3, or 4 were also essentially devoid of bioactivity. It is speculated that this lack of bioactivity reflects an inability of the proteins to assume a native conformation.
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