start-ver=1.4
cd-journal=joma
no-vol=36
cd-vols=
no-issue=2
article-no=
start-page=51
end-page=60
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2002
dt-pub=200203
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Regulatory Role for Complement Receptors (CD21/CD35) in the Recombination Activating Gene Expression in Mouse Peripheral B Cells
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=A population of peripheral B cells have been shown to express recombination activating gene products, RAG-1 and RAG-2, which are considered to be involved in revising the B cell antigen receptor (BCR) in the periphery. BCR engagement has been reported to turn off RAG expression in peripheral B cells, whereas the same treatment has an opposite effect in immature B cells in the bone marrow. In contrast to receptor editing that is involved in the removal of autoreactivity in immature B cells, it has been shown that secondary V(D)J rearrangement in peripheral B cells, termed receptor revision, contributes to affinity maturation of antibodies. Here, we show that RAG-2 expression in murine splenic B cells was abrogated by the coligation of BCR with complement receptors (CD21/CD35) much more efficiently than by the engagement of BCR alone. On the other hand, the same coligation augmented proliferation of anti-CD40-stimulated B cells. Consistent with these observations, RAG-2 expression was lower in the draining lymph nodes of the quasi-monoclonal mice when they were immunized with a high-affinity antigen than with a low-affinity one. These findings suggest a crucial role for CD21/CD35 in directing the conservation or the revision of
BCRs in peripheral B cells.
en-copyright=
kn-copyright=

en-aut-name=HikidaMasaki
en-aut-sei=Hikida
en-aut-mei=Masaki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=MagariMasaki
en-aut-sei=Magari
en-aut-mei=Masaki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=NakayamaYasunori
en-aut-sei=Nakayama
en-aut-mei=Yasunori
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=KanayamaNaoki
en-aut-sei=Kanayama
en-aut-mei=Naoki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=OhmoriHitoshi
en-aut-sei=Ohmori
en-aut-mei=Hitoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=3
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=4
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=5
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
END

start-ver=1.4
cd-journal=joma
no-vol=38
cd-vols=
no-issue=1-2
article-no=
start-page=91
end-page=96
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2004
dt-pub=200403
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Generation of IgM and IgG1 monoclonal antibodies with identical variable regions: comparison of avidity
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Generally, IgM antibodies (Abs) produced in a primary immune response show lower affinity for an inducing antigen (Ag) compared with the corresponding IgG Abs that are major switched isotypes formed in the secondary response. An IgM molecule is a pentamer with 10 Ag-binding sites that will contribute to an increase of avidity for an Ag. To estimate the contribution of the pentameric structure to the avidity of an IgM Ab, we generated IgM and IgG1 monoclonal Abs (mAbs) with identical V regions that are specific for 4-hydroxy-3-nitrophenylacetyl (NP) by in vitro class switching of B cells followed by the cell fusion with a mouse myeloma cell line. Compared with an anti-NP IgG1 mAb, the corresponding IgM mAb showed much higher avidity for NP-conjugated
bovine serum albumin, which was drastically reduced after being dissociated into monomers.
en-copyright=
kn-copyright=

en-aut-name=KanayamaNaoki
en-aut-sei=Kanayama
en-aut-mei=Naoki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=YamakoshiKimi
en-aut-sei=Yamakoshi
en-aut-mei=Kimi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=KiyomiMasaaki
en-aut-sei=Kiyomi
en-aut-mei=Masaaki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=MagariMasaki
en-aut-sei=Magari
en-aut-mei=Masaki
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=OhmoriHitoshi
en-aut-sei=Ohmori
en-aut-mei=Hitoshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

affil-num=1
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=2
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=3
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=4
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University

affil-num=5
en-affil=
kn-affil=Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University
END

start-ver=1.4
cd-journal=joma
no-vol=10
cd-vols=
no-issue=
article-no=
start-page=19
end-page=
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=1988
dt-pub=19881201
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=生物系の教育に伴って発生する廃液・排永
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=
en-copyright=
kn-copyright=

en-aut-name=OhmoriHitoshi
en-aut-sei=Ohmori
en-aut-mei=Hitoshi
kn-aut-name=大森齊
kn-aut-sei=大森
kn-aut-mei=齊
aut-affil-num=1
ORCID=

affil-num=1
en-affil=
kn-affil=岡山大学工学部生物応用工学科
END