Leung AS, Estrada-Reyes E, Goto K, Huang CH, Li JM, et al.
Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology β’
This review examines the evolving global landscape of food-induced anaphylaxis (FIA), revealing critical epidemiological shifts that challenge traditional allergen management paradigms. As the leading cause of anaphylaxis worldwide, FIA demonstrates striking geographic, age-specific, and temporal patterns that reflect broader changes in dietary practices, environmental exposures, and food production systems. Emerging trends reveal novel allergen sources that evade current regulatory frameworks, including non-priority legumes, edible insects and galacto-oligosaccharides with distinct cross-reactivity patterns and the expanding prevalence of buckwheat, tree nut and seeds anaphylaxis. Complex syndromes such as lipid transfer protein syndrome, tick-borne Ξ±-Gal syndrome and food-dependent exercise-induced anaphylaxis represent diagnostic challenges requiring heightened clinical suspicion. Critical knowledge gaps remain in certain regions where limited surveillance, inadequate adrenaline access, and uncharacterized regional allergens create substantial management disparities. The review emphasizes urgent needs for comprehensive global surveillance networks, precision diagnostic tools for atypical presentations, expanded allergen labeling policies encompassing novel proteins, and equity-centered interventions addressing geographic disparities in emergency treatment access.
The present study sought to characterize the expression and distribution of complex glycoconjugates in the rat retina by lectin histochemistry, using a panel of 21 different lectins with different carbohydrate specificities. Paraffin sections of Carnoy-fixed Sprague-Dawley rat eyes were stained with various biotinylated lectins, followed by the streptavidin-peroxidase and glucose oxidase-diaminobenzidine-nickel staining procedures. The results showed that the retinal pigment epithelium was stained intensely with LCA, Jacalin, WFA, S-WGA, PWA, DSA, UEA-I, LTA and PHA-E, suggesting that this epithelium contained glycoconjugates with alpha-Man, alpha-Glc, alpha-Gal/GalNAc, beta-GalNAc, alpha-Fuc, NeuAc and other oligosaccharide residues. The outer and inner segments of the photoreceptor layer showed different lectin binding affinities. The outer segments reacted with S-WGA and GS-II, whereas the inner segments reacted with UEA-II, UEA-I, LTA and MAA, suggesting that the inner segments contained glycoconjugates rich in alpha-Fuc and NeuAc(alpha2,3)Gal residues. PNA labelled specifically the cones and could be used as a specific marker for these photoreceptors. RCA-I, WFA, S-WGA, DSA, MAA and PHA-E reacted with both the outer and inner plexiform layers. On the other hand, UEA-I and LTA specifically labelled the outer plexiform layer, while PNA labelled the inner plexiform layer. The retinal microglial cells were labelled specifically by GS-I-B4 and SNA. Interestingly, we also observed that WFA bound specifically to MΓΌller cells and could be used as a novel marker for this retinal glial cell. The capillaries and larger vessels in the retina and choriocapillaris reacted intensely with GS-I-B4, RCA-I, S-WGA, PWA, DSA and PHA-E. No significant differences in lectin binding were observed in the microvessels at these two sites. In summary, the present study demonstrated the expression patterns of glycoconjugates in the rat retina and that certain lectins could be used as histochemical markers for specific structural and cellular components of the rat retina.
The rat prostate gland is composed of several distinct lobes: the ventral, lateral, dorsal, and anterior (also called the coagulating gland). Each prostatic lobe is different in its morphology, secretions, and response to hormones. The present study characterized and compared the expression of glycoconjugates in three different lobes (ventral, lateral, and dorsal) of the Noble rat prostate gland by lectin histochemistry, using a battery of 30 different lectins. The results indicate that different prostatic lobes elaborate and secrete different glycoconjugates. The dorsal prostatic epithelium secretes mainly in an apocrine mode, as characterized by the presence of apical cytoplasmic blebs which are absent in the other two lobes, though merocrine secretion is also suggested. These cytoplasmic blebs were rich in Man, GlcNAc, Gal/GalNac, Fuc, NeuAc(alpha2,6)Gal, and oligosaccharides. Two types of cytoplasmic belbs were also identified according to their lectin bindings: blebs stained by S-Con A, LCA, PWA, UEA-II, RCA-I, DBA, ECA, WFA, Jacalin, MPA, SJA, LTA, UEA-I, PHA-E, and PHA-L, and some blebs stained by S-WGA, SBA, HAA, HPA, VAA, BPA, MAA, and SNA. The lectins, which reacted with the second type of blebs, also revealed some cytoplasmic granules in the dorsal prostatic epithelial cells. The epithelium of the lateral prostate showed weak or negative reactions to lectins, suggesting that it may express fewer glycoconjugates as compared to the other two lobes. The epithelial Golgi region of the ventral prostate is the most developed among the three lobes, and contained abundant GlcNAc, alpha/beta-GalNAc, and NeuAc(alpha2,6)Gal residues, as shown by its intense reactions to S-WGA, DBA, SBA, HAA, HPA, WFA, and SNA. GS-I-B4 reacted specifically with the basal epithelial cells in all three lobes, indicating that glycoconjugates with terminal alpha-Gal/GalNAc were commonly expressed in these basal cells. The basal cells in ventral prostate might express more complex glycoconjugates, as they were also stained by PWA, RCA-I, ECA, and PHA-L, in addition to GS-I-B4, suggesting that these basal cells contained more Gal(beta1,4)GlcNAc and Gal(beta1,4)GlcNAc(alpha1,2)Man residues. GS-I-B4 and PHA-L also demonstrated a differential staining of the stromal smooth muscles and their associated extracellular matrix in the three prostatic lobes, suggesting that these structural components in different prostatic lobes were different in their complex oligosaccharide contents, which probably has an influence on the epithelial-stromal interaction in the prostate. In summary, the present study has established for the first time the expression patterns of glycoconjugates in the three lobes of the Noble rat prostate gland and suggests that certain lectins are useful as histochemical markers for the three individual prostatic lobes.
The present study sought to identify and partially characterize the glycoconjugates specific to the double-layered ciliary body epithelium of the rat eye by lectin histochemistry and lectin blottings. Hydrated paraffin sections of Carnoy-fixed Sprague-Dawley rat eyes were stained with a panel of 21 different biotinylated lectins, followed by streptavidin-peroxidase and the glucose oxidase-diaminobenzidine-nickel staining procedure. The results of lectin histochemistry revealed that the inner epithelial layer was rich in GlcNAc(beta1,4)GlcNAc, alpha-Gal, Gal(beta1,3)GalNAc, GalNAc(alpha1,3)GalNAc/Gal, GalNAc(alpha1,6)Gal, Fuc(alpha1,2)Gal(beta1,4)GlcNAc and Gal(beta1,4)GlcNAc(beta1,2)Man(alpha1,6) sugar residues as shown by its positive reactivities with S-WGA, PWA, DSA, GS-I-B4, PNA, DBA, SBA, WFA, UEA-I, LTA and PHA-E. The reactivities of GS-I-B4, PNA, DBA and SBA were restricted to the inner layer at the tips of the ciliary processes. On the other hand, the outer epithelial layer was stained evenly by DSA and Jacalin, and partly by MAA, showing that this epithelial layer was rich in GlcNAc(beta1,4)GlcNAc, Gal(beta1,3)GalNAc and NeuAc(alpha2,3)Gal disaccharides. These lectin binding patterns of the ciliary body epithelium suggest a topographical and functional difference in this double cell-layered epithelium. Their possible roles in the secretion of aqueous humour and production of ciliary zonule are discussed. Some identified lectin markers specific to these two cell layers may be useful for further experimental studies. Glycoproteins extracted from the dissected ciliary body were separated by SDS-PAGE electrophoresis and analyzed by protein blottings with 8 different lectins. The results showed that at least 10 major membrane-bound glycoproteins, with molecular weights ranging from 30 to 150 kD, rich in beta-GlcNAc, beta-Gal, alpha/beta-GalNAc and NeuAc(alpha2,6)Gal residues, were present in the microsomal fraction.
