New cell-surface antigens expressed on proliferating T cells and their possible relation to the polyclonal expansion of the cells.
| Project/Area Number |
61570247
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
Immunology
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| Research Institution | Juntendo University, School of Medicine. |
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Principal Investigator |
SATO Hidetoshi Department of Pathology, Juntendo University, School of Medicine., 医学部, 助教授 (30091573)
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| Co-Investigator(Kenkyū-buntansha) |
TNNO Masataka Department of Pathology, Juntendo University, School of Medicine., 医学部, 助手 (50171913)
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| Project Period (FY) |
1986 – 1987
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| Project Status |
Completed (Fiscal Year 1987)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1987: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1986: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | a mutant gene / lpr / Lp-1 antigen / 免疫異常 |
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| Research Abstract |
To understand a mechanism of lpr gene-induced polyclonal proliferation of T cells and possible relationship between unusual cell-surface phenotype and proliferating capacity, we have characterized Lp-1 and Lp-2 antigens which can define lpr cells as unusual.
1. Lp-1 antigen. The Lp-1 antigen is expressed exclusively on approximately 50% of proliferating lpr cells. On SDS-PAGE Lp-1 antigen was identified in 100Kd region by Western blotting and immunostaining. The reactivity of lpr cells with anti-Lp-1 Ab was completely lost when pretreated with 200mM NaI04, suggesting that an Lp-1 epitope consists largely of NaI04-sensitive carbohydrate(s). This finding, taken together with absence of Lp-1(+) cells in normal mice, may indicate that carbohyrate(s) constituting the Lp-1 epitope must be unique to 1pr cells, and we now wonder how this finding is related ot the reported one that some carbohydrates are unusual in lpr mice.
2. Lp-2 antigen. The lp-2 antigen considered unique in its expression no
… More
t only on lpr cells but also on normal B cells. Further studies indicated that a certain proportion of Ly-2 positive cells also express Lp-2. Immunochemically, Lp-2 antigen proved to be a glycoprotein of 220-240Kd in contrast with revious estimatio as 140Kd. Several experiments indicated after all that previous estimation of molecular size is wrong. These characteristics suggested that Lp-2 antigen is similar to and possibly identical with a subtype of Ly-5(B220) antigens. To clarify this problem, Dr.H.Nishimura, one of our collaborators, has sequenced Lp-2 cDNA cloned from lpr cells and found that critical sequences of Lp-2 cDNA are the same as the reported ones of the ly-5 cDNA cloned from a certain B cell line. Functional analysis of Lp-2 antigen indicated Lp-2 may work in a such way so as to enhance IgG1 production by B cells which are cultured in presence of LPS and IL-4. This was indicated by results that anti-Lp-2 Ab inhibited in a specific manner IgG1 production in th etest system. Less
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Report
(2 results)
Research Products
(16 results)
