Abstract

In our previous study we demonstrated rat T cell factors having affinity for IgE. One of the IgE-binding factors has the ability to selectively enhance the IgE response (IgE-potentiating factor) and another factor selectively suppressed the IgE response (IgE-suppressive factor). In the next fiscal year, 1) we shall study the differences between the two factors with respect to their physicochemical properties and the source from which the factors are derived. 2) Mechanisms for the formation of IgE-suppressive factors will be studied using rat lymphocytes, 3) IgE-binding factors of similar biologic activities will be searched in the mouse as well.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI011202-14
Application #
3124917
Study Section
Immunological Sciences Study Section (IMS)
Project Start
1978-02-01
Project End
1988-01-31
Budget Start
1986-02-01
Budget End
1987-01-31
Support Year
14
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Johns Hopkins University
Department
Type
Schools of Medicine
DUNS #
045911138
City
Baltimore
State
MD
Country
United States
Zip Code
21218

  Publications

Ishizaka, K; Ishii, Y; Nakano, T et al. (2000) Biochemical basis of antigen-specific suppressor T cell factors: controversies and possible answers. Adv Immunol 74:Jan-60
Ishizaka, K; Nakano, T; Ishii, Y et al. (1996) Controversial issues and possible answers on the antigen-specific regulation of the IgE antibody response. Adv Exp Med Biol 409:317-25
Nakano, T; Ishii, Y; Ishizaka, K (1996) Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. I. Identification of a 55-kilodalton glycosylation-inhibiting factor peptide with TCR alpha-chain determinant. J Immunol 156:1728-34
Ishii, Y; Nakano, T; Ishizaka, K (1996) Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. II. The 55-kDa glycosylation-inhibiting factor peptide is a derivative of TCR alpha-chain and a subunit of antigen-specific glycosyl J Immunol 156:1735-42
Ishii, Y; Nakano, T; Ishizaka, K (1996) Cellular mechanisms for the formation of a soluble form derivative of T-cell receptor alpha chain by suppressor T cells. Proc Natl Acad Sci U S A 93:7207-12
Nakano, T; Liu, Y C; Mikayama, T et al. (1995) Association of the ""major histocompatibility complex subregion"" I-J determinant with bioactive glycosylation-inhibiting factor. Proc Natl Acad Sci U S A 92:9196-200
Ishii, Y; Nakano, T; Honma, N et al. (1995) Preparation of soluble recombinant T cell receptor alpha chain by using a calmodulin fusion expression system. J Immunol Methods 186:27-36
Gomi, H; Tagaya, Y; Nakano, T et al. (1994) Antigen-binding glycosylation inhibiting factor from a human T-cell hybridoma specific for bee venom phospholipase A2. Proc Natl Acad Sci U S A 91:2824-8
Liu, Y C; Nakano, T; Elly, C et al. (1994) Requirement of posttranslational modifications for the generation of biologic activity of glycosylation-inhibiting factor. Proc Natl Acad Sci U S A 91:11227-31
Mikayama, T; Nakano, T; Gomi, H et al. (1993) Molecular cloning and functional expression of a cDNA encoding glycosylation-inhibiting factor. Proc Natl Acad Sci U S A 90:10056-60

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