课题基金 / 基金详情

Analysis of molecular structures of B cell differentiation factors and the corresponding receptors, and their functions.

Analysis of molecular structures of B cell differentiation factors and the corresponding receptors, and their functions.
B细胞分化因子及相应受体的分子结构及其功能分析。
批准号:
59440035
负责人:
HAMAOKA Toshiyuki
金额:
$12.48万
依托单位:
依托单位国家:
日本
项目类别:
Grant-in-Aid for General Scientific Research (A)
财政年份:
1984
资助国家:
日本
项目状态:
已结题
起止时间:
1984 至 1985

项目摘要

项目成果

HAMAOKA Toshiyuki的其他基金

相关文献

中文摘要
翻译
1)从B151 K12 T细胞杂交瘤中产生的两种分离B细胞分化因子的分子性质:B151-TRF 1,是一种抗原激活的B细胞在抗原形成细胞中的差异化的含义,是一种含有硅酸和N-乙酰半乳糖胺(Ga 1 NAc)的羟基糖基蛋白。约50,000人通过凝胶渗透,19,000人通过SDS-PAGE和PI 4.9 - 5.1。B151-TRF 2,一种解释非初级B细胞的多克隆B细胞差异的含义,是一种具有一定M.W.的非糖基化蛋白。约30,000人通过凝胶渗透和PI 4.3 - 4.5。B151-TRF 2比B151-TRF 1更羟基,与热处理(56 ° C30 ')相反,与热稳定B151-TRF 1不激活。在补充中,B151-TRF 2与N-乙酰葡萄糖胺(G1 cNAc)具有亲和力。2)根据突变DBA/2 Ha Mice Lack B细胞表达B151-TRF 1受体在X-连接受体标志中的一个单克隆抗体特异性,B151-TRF 1受体从杂交瘤中获得。 ... More 来自TRF 1低响应者(DBA/2 HaxBALB/c)的B细胞受到高响应者BALB/c B细胞的影响。它被揭示为B151-TRF 1-受体是一种含有m.w.糖蛋白的甘露状替代物。约120,000人,其中含有m.w.糖蛋白质的紊乱-连接同源物的几个因素。约60 000人。在另一只手上,B151-TRF 2-受体是一种含有N-终端G1 cNAc的糖蛋白质,通过分析揭示B151-TRF 2-B细胞在治疗Wih蛋白酶或糖基酶后的吸收能力。有趣的是, CBA/N B细胞承载X-连接免疫缺陷未能对两个B151 TRFs做出反应,对响应接收器的正常表达不满意。在对比下, DBA/2 Ha B细胞响应于B151-TRF 2,但不是B151-TRF 1-受体的缺失)证明了B151-TRF 1分子对B151-TRF 1分子的一个重要作用,在B151-TRF 2上的G1 cNAc residues的B151-TRF 2-受体需要B细胞激活。Less(低)
英文摘要
1) Molecular properties of two distinct B cell differentiation factors produced from B151K12 T cell hybridoma: The B151-TRF1, which induces differentiation of antigen-activated B cells into antibody-forming cells, is a hydrophobic glycoprotein bearing sialic acid and N-acetylgalactosamine (Ga1NAc) with an apparent m.w. of 50,000 by gel-permeation and 19,000 by SDS-PAGE and PI 4.9 - 5.1. The B151-TRF2, which induces polyclonal B cell differentiation of unprimed B cells, is a non-glycosylated protein with an apparent m.w. of 30,000 by gel-permeation and PI 4.3 - 4.5. The B151-TRF2 is more hydrophobic than B151-TRF1, and inactivated by heat-treatment (56゜C 30') in contrast to heat-stable B151-TRF1. In addition, B151-TRF2 has affinity for N-acetylglucosamine (G1cNAc).2) By taking advandtage of the fact that mutant DBA/2Ha mice lack B cells expressing B151-TRF1-receptor in an X-linked recessive manner, a monoclonal antibody specific for B151-TRF1receptor was obtained from a hybridoma establ … More ished from B cells of TRF1-low responder (DBA/2HaxBALB/c)F1 male mice immunized with high-responder BALB/c B cells. It was revealed that B151-TRF1-receptor is a glycoprotein containing mannose residues with m.w. of 120,000, which consists of a disulfide-linked homodimer of a glycoprotein with m.w. of 60,000. On the other hand, B151-TRF2-receptor is a glycoprotein with N-terminal G1cNAc residues as revealed by analysis of B151-TRF2-absorbing ability of B cells after treatment wih proteinase or glycosidase. Interestingly, CBA/N B cells bearing ax X-linked immune defect failed to respond to both B151TRFs, irrespective of normal expression of respective receptors. In contrast, DBA/2Ha B cells responded to B151-TRF2 but not B151-TRF1 by virtue of the absence of B151-TRF1-receptor.3) It was demonstrated that Ga1NAc residues on B151-TRF1 molecule plays an important role in binding of B151-TRF1 molecule to the receptor, whereas recognition by B151-TRF2 of G1cNAc residues on B151-TRF2-receptor is required for B cell activation. Less
期刊论文(10)
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会议论文
J. Immunol.134. (1985)
J.免疫学杂志134。
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Lymphokine Research. 4. (1985)
淋巴因子研究。
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J. Immunol.125. (1985)
J.免疫学杂志125。
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共 7 条
    Mechanisms underlying generation and activation of class II MHC-restricted B lymphocytes and their function
    • 批准号:
      02454189
    • 项目类别:
      Grant-in-Aid for General Scientific Research (B)
    • 资助金额:
      $3.97万
    • 财政年份:
      1990
    • 负责人:
      HAMAOKA Toshiyuki
    • 依托单位:
    A site-specific antibody produced with a novel immunization procedure by induction of tolerance to cross-reacting determinants and its utilization in clinical research.
    Adaptire differentiation of self-Ia-recognition molecules involved in B-B cell interaction