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Comparisons of IgE, IgG, and IgG4 responsiveness to Dermatophagoides farinae in children by immunobulotting (1996)

Noguchi, E. ; Shibasaki, M. ; Isoyama, S. ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Allergy 51 (1996), S. 0

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ISSN: 1398-9995

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Although asthmatic children are often sensitized to the house-dust mite (HDM) during early childhood, it is not clear what antigenic components are associated with the early immune response of these children. To investigate this problem, we evaluated IgE, IgG, and IgG4 antibody responses to Dermatophagoides farinae (Df) by immunoblotting among three groups of children: group I aged 0–4 years, group II aged 5–9 years, and group III aged 10–14 years. In the group I subjects, positive IgE-binding reactions to 15– and 25-kDa components were found in 76% and 44% of sera, respectively. Those to other components were generally low in frequency. In contrast, positive IgG-binding reactions to 15– and 25-kDa components were found in 44% and 24% of sera, and those to 30– and 110-kDa components in 48% and 88% of sera, respectively. Positive IgG4 reactions to 15– and 25-kDa components were found in 48% and 24%, respectively, and those to other components were very low. Positive IgE-binding reactions to these components gradually became more frequent with increasing age in groups II and III, while IgG and IgG4 reactivities were not markedly different in these age groups. These results suggest that the 15-and 25-kDa proteins of Df are important antigens associated with the initial IgE response to HDM in early childhood, while the 30– and 110-kDa proteins are associated with IgG and 15-kDa components with IgG4.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1398-9995.1996.tb04491.x

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Nuclear protein import, but not mRNA export, is defective in all Saccharomyces cerevisiae mutants that produce temperature-sensitive forms of the Ran GTPase homologue Gsp1p (1998)

Oki, M. ; Noguchi, E. ; Hayashi, N. ; [et al.]

Springer

Molecular genetics and genomics 257 (1998), S. 624-634

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ISSN: 1617-4623

Keywords: Key words Ran ; Gsp1 ; Nuclear protein import ; RNA export

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract A series of ts mutations in the GSP1 gene of Saccharomyces cerevisiae was isolated by error-prone PCR. A total of 25 ts gsp1 strains was obtained. Each of these mutants showed between one and seven different amino acid alterations. In several of these ts gsp1 strains, the same amino acid residues in Gsp1p were repeatedly mutated, indicating that our screen for ts gsp1 mutations was saturating. All of the ts gsp1 strains isolated had a defect in nuclear protein import, but only 16 of the 25 ts gsp1 strains had a defect in mRNA export. Thus, Gsp1p is suggested to be directly involved in nuclear protein import, but not in mRNA export. Following release from α-factor arrest, 11 of the ts gsp1 mutants arrested in G1; the remainder did not show any specific cell-cycle arrest, at 37° C, the nonpermissive temperature. While the mutants that are defective in both mRNA export and protein import have a tendency to arrest in G1, there was no clear correlation between the cell cycle phenotype and the defects in mRNA export and nuclear protein import. Based on this, we assume that Ran/Gsp1p GTPase regulates the cell cycle and the nucleus/cytosol exchange of macromolecules through interactions with effectors that were independent of each other, and are differentially affected by mutation.