Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0220723 (PCA)
 4,687 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Two allergenic components, termed J1 and J2, were isolated from a soluble egg antigen preparation (SEA) of Schistosoma japonicum by anion-exchange chromatography on DE52 and gel chromatography on Sephacryl S-200. The apparent molecular weights of J1 and J2 were 260,000 and 46,000, respectively, by gel chromatography on Sephadex G-150. By SDS-polyacrylamide gel electrophoresis, both J1 and J2 showed apparent homogenicity and their estimated molecular weights were 135,000 and 45,000, respectively. The isoelectric point of J1 (pI 4.9) was similar to that of J2 (pI 4.8). Both J1 and J2 bound to Con A-Sepharose 4B, indicating their glycoprotein nature. The amino acid compositions of J1 and J2 have some similarities. However, phenylalanine and leucine, which contain large hydrophobic groups, were dominant in J1, whereas serine and threonine, which contain a hydroxyl group, were dominant in J2. J1 was sensitive to heating or pronase treatment, whereas J2 was rather stable to these treatments. Both J1 and J2 were sensitive to 0.1 M periodate treatment. When mice were immunized with either J1 or J2 with A1(OH)3 as an adjuvant, anti-J1 or anti-J2 IgE antibody was highly specific to the respective antigens. Since S. japonicum-infected mouse serum has high PCA titer to J1 and J2, these two components are the major allergens of S. japonicum eggs.
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PMID:Isolation of two immunogenically different allergens from Schistosoma japonicum eggs. 303 85

Mice with a primary infection of Schistosoma japonicum develop high levels of both total immunoglobulins and parasitic-specific antibodies, beginning about 1.5 wk after the onset of oviposition in the host. Radial immunodiffusion demonstrated an 18-fold, fivefold, and threefold increase in the levels of IgG1, IgM, and IgA, respectively, during the course of infection. Schistosoma japonicum-specific antibodies, as measured by an enzyme-linked immunoabsorbent assay, appeared and increased at about the same time as total immunoglobulins, and were predominantly of the IgG1 and IgM classes. The specific/ELISA response to a purified antigen from S. japonicum SEA was distinct from the total specific response to crude SEA. Hemagglutinating antibodies increased at 5 wk PI and remained at high levels for the duration of infection. Specific, circulating IgE measured by PCA appeared 6 wk PI, reaching a peak at 9 wk, and persisted at moderate levels throughout the infection period.
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PMID:Serologic responses to Schistosoma japonicum: evaluation of total and parasite-specific immunoglobulins during the course of murine infection. 711 81

The relationship between the cercarial allergen and two previously isolated egg allergens (J1, J2) of Schistosoma japonicum was examined especially in terms of the cross-reactivity between them. Semi-purified cercarial allergen (JAC) was obtained from the crude extract of S. japonicum cercariae by gel chromatography on Sephadex G-200. The apparent molecular weight of JAC was estimated approximately as 60-100 kDa. JAC could bind to Con A-Sepharose, indicating its glycoprotein nature. Three groups of BALB/c mice were immunized with JAC , J1 or J2 using A1(OH)3 as adjuvant, and the cross-reactivity of each anti-serum was examined by PCA. Anti-JAC, anti-J1 or anti-J2 serum was highly specific to the corresponding antigen. When IgE-ELISA of S. japonicum patient sera was performed using JAC, J1 or J2 as an antigen, the correlation between anti-J1 and anti-J2 (r = 0.78) was high, whereas the correlation between anti-JAC and anti-J1 (r = 0.27) or between anti-JAC and anti-J2 (r = 0.12) was low. These results suggest that most IgE epitopes on cercarial allergen are independent from those on egg allergens in S. japonicum.
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PMID:IgE response in schistosomiasis japonica: characterization of a cercarial allergen in comparison with purified egg allergens. 927 69