PubMed HealthSearch

PubMed · 7952259

How is anaphylaxis recognized?

Abstract

Prompt recognition of anaphylaxis may be lifesaving. Although its presentation has been described, there are no criteria for making a rapid diagnosis. A systematic review of the literature was performed to develop objective clinical criteria aimed at improving the recognition of anaphylaxis. A MEDLINE search of the word anaphylaxis over a 1-year period identified all of the reports describing the initial manifestations. Of 160 reviewed articles, 116 contained a clinical description of anaphylaxis. Eighty-nine (77%) of these 116 articles were case reports. Hypotension (84 reports [72%]) and urticaria and/or angioedema (70 reports [60%]) were the most frequently described signs. Of the identified allergens, 73% were diagnostic or therapeutic agents. In 72 of the 80 articles in which a reaction time could be identified, the reaction occurred within 60 minutes. As a result of this analysis, we conclude that anaphylaxis recognition may be improved by the identification of one of the following criteria, which describe the presentation in 82% of the analyzed reports: (1) exposure to an allergen within 1 hour produces one or more systemic signs (hypotension, upper or lower respiratory tract compromise, or increased gastrointestinal tract motility), or (2) urticaria or angioedema accompanies at least one of these systemic signs.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A J Apter, H A LaVallee. 1994. How is anaphylaxis recognized?. https://doi.org/10.1001/archfami.3.8.717

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Purification and characterization of a novel peptidase (IImes) from mesquite (Prosopis velutina) pollen.

Although the mesquite plant (Prosopis velutina) is not as widely distributed as some other allergenic species, its pollen can induce serious pollinosis in areas where it is localized. We previously isolated and characterized a peptidase from mesquite pollen with trypsin-like specificity (peptidase Imes) (Matheson, N., Schmidt, J., and Travis, J. (1995) Am. J. Respir. Cell Mol. Biol. 12, 441-448). Now we have characterized a second enzyme with specificity for hydrophobic residues (mesquite pollen peptidase IImes). This enzyme has a molecular mass near 92 kDa and activity that was not affected by reducing or chelating agents but was inhibited by specific synthetic serine proteinase inhibitors and the aminopeptidase inhibitor bestatin. However, it was not inhibited by human plasma proteinase inhibitors, nor did it inactivate any of those tested. The enzyme possessed amidolytic activity against p-nitroanilide substrates most effectively after alanine residues and also displayed aminopeptidase activity against non-p-nitroanilide peptides with a preference for phenylalanine. This specificity for hydrophobic amino acid residues was corroborated by inhibition studies with chloromethyl ketone and organophosphonate inhibitors. More interesting from a physiological point of view is that the bioactive peptides, angiotensins I and II and vasoactive intestinal peptide, were also hydrolyzed rapidly, indicating an ability of peptidase IImes to act also as an oligopeptidase. Because these bioactive peptides play a role in the inflammatory responses in allergic asthma, our data suggest that the purified mesquite pollen peptidase IImes may be involved in the degradation of neuro- and vasoactive peptides during pollen-initiated allergic reactions.

Allergens

Molecular and crystal properties of Bos d 2, an allergenic protein of the lipocalin family.

The relationship between the molecular structure of allergenic proteins and the allergenic determinants is one of the central issues in allergology. We report here that the natural preparation of Bos d 2, a mammalian lipocalin allergen, comprises three molecular variant proteins of 17,829, 17,781, and 17,800 Da. When cDNA of Bos d 2 (Genome Sequence Data Base No. L42867) was recloned and expressed in Pichia pastoris, two proteins were produced. One of the proteins (17,831 Da) and the proteins in the natural preparation had pyroglutamate as the N-terminal residue; in the other (17,849 Da) the N-terminal residue was glutamine. Recombinant Bos d 2 protein was crystallized and the native data set was collected at 1.8 A resolution.

Allergens

Immunization with purified natural and recombinant allergens induces mouse IgG1 antibodies that recognize similar epitopes as human IgE and inhibit the human IgE-allergen interaction and allergen-induced basophil degranulation.

Molecular characterization of allergens by recombinant DNA technology has made rapid progress in the recent few years. In the present study we immunized mice with aluminum hydroxide-adsorbed purified recombinant major timothy grass pollen allergens (rPhl p 1, rPhl p 2, rPhl p 5), dog albumin, a major animal dander allergen, and proteins with low (beta-lactoglobulin) or no (ribulose diphosphate carboxylase) allergenic potential in humans. Allergens that bind high levels of IgE in humans (Phl p 1, Phl p 5, dog albumin) induced high IgE and IgG1 levels in mice, whereas proteins with little or no allergenic activity in humans failed to induce significant IgE and IgG1 levels in mice. Continuous immunization for a period of 27 wk resulted in the production of mouse IgG1 Abs that recognized recombinant allergen fragments/epitopes defined by IgE Abs of allergic patients. As a consequence, allergen-specific mouse Abs strongly inhibited human IgE binding to the allergens and suppressed the allergen-induced histamine release from human basophils. In summary, our data indicate that 1) the allergenic potency of a protein may be related to its overall immunogenicity and 2) prolonged immunization with single purified recombinant allergens induces protective IgG Abs. The presented experimental in vivo/in vitro system allows the evaluation of Ag preparations (e.g., recombinant allergens) to be used for immunotherapy in humans.

Allergens