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Background: U.S. national emergency was declared in mid-March 2020 due to the coronavirus disease 2019 (COVID-19) pandemic. Subsequently, a period of stay-at-home orders, regulatory changes, evolving medical recommendations, and food supply chain disruptions occurred. There is little published research on how such changes affected food allergy management for children with this diagnosis. Objective: The study goal was to identify parent perspectives with regard to if and/or how pandemic-related regulatory changes and evolving medical recommendations have affected food allergy management. Methods: A survey was distributed to parents of children with food allergy. An electronic Internet forms survey link was available for completion during July 2020. Data were presented as descriptive statistics, cleaned, and coded into a spreadsheet before analysis . Frequencies and percentage were calculated to describe participants’ characteristics and responses. Results: Of 377 responses, 359 met inclusion criteria. Concerns about COVID-19 exposure were expressed in 65.7% about accessing an emergency department and 73.6% had school reentry concerns; 66% had not discussed recommended anaphylaxis management algorithm changes with a provider; 85.8% had not discussed the temporary U.S. Food and Drug Administration food labeling policy with a provider. Most (62%) reported shortages of preferred safe food brands. 62% spent more time cooking safe foods from scratch. With regard to the recommendation by the U.S. Centers for Disease Control and Prevention (CDC) for classroom dining, 57.7% planned to request modifications. With regard to the CDC’s recommendation to use inhalers versus nebulizers, 37.7% had not discussed the topic with a provider. Ninety-two written comments were analyzed and grouped into seven themes. Conclusion: New pandemic-related regulations, food supply chain disruptions, and evolving medical recommendations resulted in intensified burdens for respondents, including the increased time needed to complete food allergy management and school reentry concerns. Study results can inform clinical team members (e.g., physicians, nurses, dieticians) of effects that pandemic-related changes may have on this patient population, with subsequent consideration of patient-specific screening, education, and shared decision-making with regard to risk mitigation needs.

Management of food allergy on a daily basis is multifaceted, time consuming, costly, and becomes compounded when multiple food allergies are involved. Allergen avoidance methodologies, monitoring of signs/symptoms of allergic reactions, handling serious medication needs, and planning ahead for a potential emergency due to an accidental exposure can be demanding concerns to the patient/family. Due to the complexity of this diagnosis, its implications to health-related quality of life, and extensive patient/family informational needs, it was necessary to divide this article into a 2-part series. This is the second article of the series. The content of Part 1 of the series focused on patient education associated with common food allergens, food allergy avoidance (eg, allergen identification, ingredient label reading, hidden allergens, cross-contact, precautionary labeling, potential routes of accidental exposures) and the food allergy action plan. Part 2 of the series reviews food-induced anaphylaxis and associated patient educational interventions (eg, use of self-injectable epinephrine, medical identification). Both parts of the series consider developmental concerns of the food allergic young child and adolescent. Parts 1 and 2 should be read collectively to acquire a complete view of suggested patient education for the newly diagnosed food hypersensitive pediatric patient and the role of a food allergy educator in an ambulatory care setting.

Management of food allergy on a daily basis is multifaceted, time consuming, costly, and becomes compounded when multiple food allergies are involved. Families must devise risk reduction techniques as they run repeated surveillance to minimize potential food allergen triggers. Monitoring of signs/symptoms of allergic reactions, handling serious medication needs, and planning ahead for a potential emergency due to an accidental exposure can be arduous responsibilities. This diagnosis has psychological, social, practical, and logistical implications to a family and subsequently the community surrounding the patient. Often, patients with multiple food allergies and/or coexisting atopic conditions must interact with several medical specialists to obtain comprehensive diagnosis and management plans. Patient education, case management, and mentoring are essential in promoting compliance and supporting family efforts. It is also critical that the dignity and autonomy of the family be respected during the diagnostic phase and subsequent educational guidance process. Given the complex nature of this diagnosis and its ramifications on patients/families, it was necessary to divide this article into a 2-part series. This is the first article of the series. Part 1 of the series focuses on patient education associated with common food allergens, potential pitfalls of food allergy avoidance, the food allergy action plan and the role of a food allergy educator. Part 2 covers food-induced anaphylaxis and suggested educational interventions. Both parts consider developmental concerns of the young child and adolescent as they relate to this diagnosis. Parts 1 and 2 should be read collectively to acquire a complete view of suggested patient education for the newly diagnosed patient and family.

Mastocytosis is often associated with organ involvement and hematological disorders. Patients may also exhibit elevated levels of plasma IL-6. To gain insight into the relevance of this observation, we correlated plasma levels of IL-6 and soluble IL-6 receptor (sIL-6R) with multiple disease parameters in 29 patients with mastocytosis. Mean plasma IL-6 levels were elevated in patients compared to healthy controls (P < 0.0001). Disease category significantly correlated with plasma IL-6 levels, as did severity of bone marrow pathology, organomegaly, and extent of skin involvement. In plasma, there was a positive correlation of IL-6 to total tryptase, alkaline phosphatase, IgM, white blood cell count, prothrombin time, partial thromboplastin time, and neutrophil numbers. There was an inverse correlation to hemoglobin. sIL-6R levels were not elevated. These observations demonstrate that IL-6 is a useful surrogate marker of severity of hematologic disease and suggest that IL-6 contributes to pathology.

Objective To determine clinical correlates of urticaria pigmentosa (UP) regression in adult patients with systemic mastocytosis (SM). Design Cohort study of the natural history of mastocytosis. Setting National Institutes of Health Clinical Center. Patients In a study of adult patients referred to the National Institutes of Health after 1980 and observed for a minimum of 10 years, 12 of 106 adult patients experienced clearance or fading of UP. Main Outcome Measures Data from each patient's history and results of physical examination, laboratory evaluation, and organ biopsy at presentation to the National Institutes of Health were compared with findings at the patient's most recent visit. Results In the patients in whom clearance of (n = 5) or a decrease in skin lesions (n = 7) was noted, UP had persisted from 4 to 34 years (median, 17 years). Older age was a prognostic feature for regression of UP. Despite improvement of UP, the 2 patients with SM with an associated hematologic disorder experienced a deterioration in clinical condition. In the 10 patients with indolent SM, severity and frequency of symptoms decreased as the UP regressed. However, bone marrow changes consistent with SM remained. Conclusions Urticaria pigmentosa regresses in approximately 10% of the older patients who have SM. In patients with an associated hematologic disorder such as myelodysplasia, this regression may be accompanied by disease progression. In contrast, regression of UP in patients with indolent SM parallels a decrease in disease intensity, although bone marrow findings of indolent SM remain.

Mast-cell accumulation has been observed in the skin and other organs of patients with systemic indolent mastocytosis (SM). The basis for this pathologic increase is not fully understood.We sought to determine levels of mast-cell growth factors in the skin and plasma of patients with SM, patients with atopic dermatitis (AD), and healthy individuals and to correlate these levels to dermal mast-cell numbers and levels of mast-cell tryptase.Skin suction blister fluid and plasma levels of stem-cell factor, IL-3, IL-4, IL-6, vascular endothelial growth factor, and total mast-cell tryptase were analyzed by means of ELISA. The number of mast cells was determined in a biopsy section taken from adjacent skin.Mast-cell numbers in the dermis were higher in patients with SM compared with numbers in patients with AD (P.001) or in healthy control subjects (P.0001) and correlated with tryptase levels in both skin blister fluid (P.0001) and plasma (P.0001). Stem-cell factor and vascular endothelial growth factor levels in the skin blister fluid and plasma of patients with SM were not significantly different from those in patients with AD or healthy control subjects. IL-3 and IL-4 levels were below the limit of detection. IL-6 levels were significantly increased in the plasma of patients with SM compared with in plasma of patients with AD (P.002) and healthy control subjects (P.0001) and correlated with plasma tryptase levels (P.05) and dermal mast-cell numbers (P.02).Because elevated levels of IL-6 could contribute to the fever, fatigue, and osteoporosis observed in patients with SM and because IL-6 is antiapoptotic for mast cells, IL-6 could potentiate the biologic consequences of this disease.

Type II B arylsulfatases are known to inactivate slow reacting substance (SRS), but the mechanism is unclear. In the present study, ordinary commercial preparations of Sigma limpet arylsulfatase largely inactivated the glutathionyl and cysteinyl-glycyl forms of SRS, but the cysteinyl form of SRS was largely resistant to the enzyme. Evidence is presented which established that a major mechanism for the inactivation of the glutathionyl and cysteinyl-glycyl SRS types, at least by the particular enzyme preparations we have studied, involves cleavage of the glycine moiety from the sulfur containing side chain. This was confirmed by digestion studies with glutathione itself. In addition, there is ome evidence to indicate that the enzyme may destabilize the double bond structure of the SRS molecule, contributing to the overall inactivation.

The most prominent slow reacting substance from rat basophilic leukemia cells (type I) was characterized by radiochemical, chemical and physical methods and shown to contain a C20 unsaturated fatty acid oxygenated at the 5 position and a sulfur containing side chain in thioether linkage at the 6 position. Its spasmogenic action on guinea pig ileal muscle was largely inactivated under reducing conditions which suggested that a peroxy group was present and important for contractile activity. This was supported by ferrous thiocyanate analysis. The peroxy group is almost certainly at the 5 position, probably in the form of a peroxy ester or hydroperoxide. Based on amino acid hydrolysis (0.85 moles of glycine and 0.30 moles of glutamic acid per mole SRS), the sulfur containing side chain is apparently a mixture of glutathione and cysteinyl-glycine, but by chromatography the side chain is predominantly glutathione and the low yield of glutamic acid may be due to complexing of its α COOH group in a peroxy ester linkage. The fatty acid moiety has 3 conjugated double bonds, probably at the 7,8, 9,10 and 11,12 positions. Type II SRS, the second major species, differs in that the sulfur containing side chain is linked at the 12 or 13 position and is almost certainly glutathione and in the failure of alkaline borohydride to produce inactivation. These observations strongly implicate the lipoxygenase pathway in slow reacting substance biosynthesis.

Publisher Summary This chapter discusses the production and purification of slow-reacting substance (SRS). The most useful source of cells for SRS biosynthesis in these initial studies of SRS structure was the RBL-1 cell. RBL-1 cells can be grown in ordinary tissue culture medium in quantities of up to 24 liters. In sequential conversion of arachidonic acid to various SRS species by RBL-1 cells include: 5-hydroperoxide, glutathionyl SRS, cysteinyl-glycyl SRS, and cysteinyl SRS. In purification of SRS, SRS (2000 ml) containing cell supernatant is applied directly as an aqueous solution at ambient temperature to a 890-ml Amberlite XAD-7 column. The SRS is further purified on two high-pressure liquid chromatogram phy columns. The final purified SRS preparations are usually stored in the HPLC solvents in which they cluted from the columns and appear to be stable more or less indefinitely provided they are maintained at –70 °.

The two major species of slow reacting substance (SRS) contain either a glutathionyl or cysteinyl-glycyl side chain. Incubation of these SRS's with undiluted or diluted (usually 1:10 or 1:50) human plasma at 37°C resulted in marked losses of smooth muscle contracting activity due primarily to conversion of their oligopeptide side chains to cysteine.

When synthetic [1- 14 C]5-hydroperoxy-eicosatetraenoic acid was incubated with rat basophilic cells, incorporation of the radiolabel into slow reacting substance (SRS) could be demonstrated as evidenced by comigration of spasmogenic activity and radioactivity after purification by high pressure liquid chromatography. This provides direct evidence that SRS is a product of the lipoxygenase pathway.

In rat basophilic leukemia (RBL-1) cells stimulated with A-23187, the major slow reacting substance (SRS) species contain glutathione, cysteinyl-glycine, or cysteine in their side chains, corresponding or closely related to leukotrienes LTC 4 , LTD 4 , and LTE 4 , respectively. 3 Evidence is presented that most of the SRS produced during the first few minutes of stimulation by the ionophore has a glutathionyl side chain which is sequentially converted to cysteinyl-glycine and cysteine.

Publisher Summary This chapter describes how slow-reacting substances (SRS) smooth muscle contracting activity is measured, including some of the pitfalls and problems in interpretation. SRS activity is frequently measured in crude tissue extracts by bioassay. Because substantial SRS degrading activity may be present, systemic experimentation may be needed to determine the optimal time for generation of maximal SRS activity. The possibility of losses of SRS activity during storage also must be considered. Another way of determining whether or not a spasmogenic response is due to SRS is to see whether the activity is stable to selected enzymes or extremes of pH or temperature. Enzymes that may inactivate SRS include arylsulfatase and lipoxygenase. Most of the SRSs that have been studied to date are inactivated by type B arylsulfatases, at least as these enzymes are presently obtained commercially. The inactivation is seen with both crude and purified SRS preparations. While a description is given only for the guinea pig ileal smooth muscle bioassay system, the general approach with regard to verification of specificity is readily applicable to other SRS activities.