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- Moverare, Robert, et al.
(författare)
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Evaluation of IgE Antibodies to Recombinant Peanut Allergens in Patients with Reported Reactions to Peanut
- 2011
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Ingår i: International Archives of Allergy and Immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 156:3, s. 282-290
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Tidskriftsartikel (refereegranskat)abstract
- Background: Peanut may cause severe reactions in allergic individuals. The objective was to evaluate IgE antibodies to various recombinant (r) peanut and birch pollen allergens in relation to IgE levels to whole peanut extract and severe allergic reactions to peanut. Methods: Seventy-four Swedish peanut-allergic patients (age: 14-61 years) reported previous peanut exposure and associated symptoms using a questionnaire. Their IgE reactivity to peanut, birch pollen and individual allergen components was analyzed using ImmunoCAP(R). Results: Of the 48 subjects sensitized to Ara h 1, 2 or 3, 60% had peanut-specific IgE levels >15 kU(A)/l, while 100% of the subjects without detectable IgE to these allergens had low peanut-specific IgE levels (<10 kU(A)/l). The levels of IgE to rAra h 8, rBet v 1 and birch pollen were highly correlated (r(S) = 0.94, p < 0.0001). Fifty-eight patients reported adverse reactions after accidental or deliberate peanut exposure (oral, inhalation or skin) of whom 41 had IgE to rAra h 1, 2 or 3. Symptoms of respiratory distress were associated with sensitization to Ara h 1, 2 or 3 (56 vs. 18%, p < 0.01). Two cases of anaphylaxis were reported among the individuals sensitized to Ara h 1-3. IgE to rAra h 8, rAra h 9, profilin or cross-reactive carbohydrate determinants were not associated with severe symptoms. Conclusions: The results indicate that IgE reactivity to Ara h 1, 2 and 3 is associated with severe reactions after exposure to peanut in Swedish patients.
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- Poorafshar, Maryam
(författare)
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Chymotrypsin/trypsin-related serine proteases : A structural, functional and evolutionary analysis
- 2000
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- Is life possible without proteolytic enzymes? Proteases participate in almost everyaspect of life and they can be found throughout the body and in every cell. Mast cells,together with basophils are, two important effector cells of the immune system. Neutralproteases are the major granule constituents of mast cells and have been also found inbasophils. Besides conferring important biological functions to the mast cells andbasophils, neutral proteases also serve as selective markers for the identification ofdifferent mast cell sub-populations and to distinguish mast cells from basophils. Inaddition, such markers can be used as indicators of allergic inflammation. Studies of apotent IL-4-producing cell population in mice infected with malaria resulted in theidentification of the first basophil specific granule marker in the mouse, MMCP-8.MMCP-8 belongs to a recently identified subfamily of mast cell/basophil serineproteases, clearly distinct from classical chymases and tryptases. To further study thestructure and function of MMCP-8 and its rat homologues, RMCP-8, -9 and 10,recombinant zymogens of these enzymes were expressed in a mammalian expressionsystem. Based on primary amino acid sequences, MMCP-8, RMCP-8, -9 and -10 werefound to have five, three, two and two potential glycosylation sites, respectively. SDS-PAGE analysis of the recombinant proteases strongly indicated that all these potentialsites were used for carbohydrate addition in vivo. In addition, MMCP-8 showed highaffinity for heparin at both pH 5.5, and neutral pH, whereas RMCP-10 bound to heparin only at pH 5.5. Screening for a human homologue to MMCP-8 or another basophil-specific serine protease resulted in the identification of leydin, a novel tyrosine-likeserine protease expressed in the Leydig cells of the testis.Studies of the appearance of the various subfamilies of hematopoietic (and other)serine protease during vertebrate evolution may clarify some of the central questions concerning their biological importance. A screening for novel serine proteases inplatypus, a mammal distantly related to the placentals, led to the isolation of c-DNAclones encoding platypus coagulation factor X, complement factor D and twohematopoietic serine proteases; a neutrophil elastase-like protease and a distantly relatedmember of the T cell granzymes of placental mammals. The isolation of these clonesshows that these four subfamilies of serine protease were already present during earlymammalian evolution. A comparison between aa sequences of these proteases and theircounterparts in placental mammals shows a higher degree of conservation in non-hematopoietic compared to hematopoietic serine proteases.
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- Wernersson, Sara, et al.
(författare)
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Granzyme-like sequences in bony fish shed light on the emergence of hematopoietic serine proteases during vertebrate evolution
- 2006
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Ingår i: Developmental and Comparative Immunology. - : Elsevier BV. - 0145-305X .- 1879-0089. ; 30:10, s. 901-918
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Tidskriftsartikel (refereegranskat)abstract
- Hematopoietic serine proteases (SPs) are stored in the granules of different leukocytes and these enzymes are important effector molecules in the immune system of mammals. However, very little is known about the presence of these proteins in lower vertebrates. Herein, the primary structures of five novel fish SPs, from the Atlantic cod (Gadus morhua) and the channel catfish (Ictalurus punctatus), are presented. One of the cod SPs is a homologue to human GzmA and K. The other fish SPs identified are termed 'Gzm-like' and are distantly related to a large heterogeneous group of hematopoietic SPs, including most of the T-cell Gzms (B-H), the mast cell chymases, the mast cell/basophil proteases of the mouse mast cell protease-8 subfamily (W-family) and the neutrophil cathepsin G. Extensive BLAST-searches in genome and expressed sequence tag (EST) databases identified 40 additional teleost SPs related to the mammalian hematopoietic SP family. Subsequent phylogenetical analyses clearly demonstrate that the diversification into different subgroups within the GzmB/chymase/cathepsin G-related family has occurred independently in bony fishes and in mammals. In contrast, our findings suggest that the three subgroups, including (1) GzmK and the potent apoptosis-inducing GzmA, (2) the neutrophil proteases (proteinase 3, N-elastase and azurocidin), and (3) adipsin, have all evolved as distinct groups before the separation of tetrapods from the ray-finned fish approximately 420 million years ago.
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