The Biochemistry of Antigen-Specific T-Cell Factors

Webb, David R.; Kapp, Judith A.; Pierce, Carl W.

doi:10.1146/annurev.iy.01.040183.002231

Cited by 59 publications

(16 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Suppression may be mediated by many diverse cell types (8)(9)(10)(11)25) and by a variety of soluble products (10,25,26 (27,28). In other cases heterodimeric polypeptides have not been identified (29,30 It is interesting to speculate that the receptor polypeptides have similar molecular masses to murine 'y-8 heterodimeric proteins (21)(22)(23)(24).…”

Section: Discussionmentioning

confidence: 99%

CD3-associated heterodimeric polypeptides on suppressor hybridomas define biologically active inhibitory cells.

Weiner

Hanna²,

Bluestone³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We have investigated the relationship between CD3 expression and the suppressor T-cell function. We have isolated stable clonal cell lines of the F12.23 suppressor T-cell hybridoma that are either CD3+ or CD3-. These lines were subjected to functional assays including inhibition of in vivo hapten-specific delayed-type hypersensitivity responses, in vitro hapten-specific interleukin 2 responses, as well as haptenspecific cytotoxic T-lymphocyte assays. In all assays, the functional suppressor phenotype absolutely correlated with CD3 surface expression. Furthermore, we have immunoprecipitated heterodimeric proteins that share molecular features with some receptor polypeptides previously described. CD3 polypeptides found on the surface of suppressor T cells are phosphorylated after phorbol ester stimulation. Collectively these studies unambiguously define the suppressive supernatant function as a product of CD3+ receptor-bearing T cells.

show abstract

Section: Discussionmentioning

confidence: 99%

CD3-associated heterodimeric polypeptides on suppressor hybridomas define biologically active inhibitory cells.

Weiner

Hanna²,

Bluestone³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…This type of TsF comes to be secreted from inducible anti-Id Ts hybridoma (C57BL/6 KLH-Ts x BW5147) after activation by TsF| from Id-positive KLH-Ts or by monoclonal anti-KLH antibody with suppressive activity [6,8]. In that sense the TsF examined here is the TsF2 type, as has been shown in the case of the GAT-and NP-specific suppressor systems [3,4,17].…”

Section: Discussionmentioning

confidence: 99%

Biochemical Characterization of an Antigen-Specific Suppressor T Cell Factor

Matsushita

Sumida

Tagawa

et al. 1989

Int Arch Allergy Immunol

View full text Add to dashboard Cite

We describe here the biochemical properties of suppressor T cell factor (TsF₂) released from an inducible anti-idiotypic T cell hybridoma (C57BL/6 T cell × BW5147) which mediates antigen (keyhole limpet hemocyanin) specific and genetically (H-2^b) restricted suppression of IgG plaque-forming cell responses. We examined the suppressive activity by in vitro functional assay in fractions of chromatography and in the materials eluted from gels of sodium dodecyl sulfate polyacrylamide and isoelectric focusing and determined the molecular weight(s) (22–37 kD) and the isoelectric point(s) (pH 6.0–6.1) of this secreted factor. Messenger RNA products of the hybridoma translated in the rabbit reticulocyte lysate system were similarly examined, and the functionally active molecule was seen to migrate to almost the similar molecular weight(s) (23–40 kD), and isoelectric point(s) (pH 5.5–6.2) range as those of secreted TsF. Moreover, the TsF activity was recovered from gel slice corresponding to the similar molecular weight range analyzed in sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing and nonreducing conditions. Thus, we speculate that this molecule is composed of a single chain, biologically active. Comparison of autoradiograms on in vitro translation products between activated and resting hybridomas by two-dimensional gel electrophoresis showed that the molecular weights and isoelectric points of two spots (28 kD, 5.7; 25 kD, 5.5) newly appearing or markedly enhanced after activation in the area with suppressor activity were concordant with the data on secreted TsF, suggesting that one of these two spots represents the functional molecule which causes antigen-specific and genetically restricted suppression of IgG responses.

show abstract

“…Polyclonality of TABM analogous to immunoglobulins is suggested by charge hetero geneity [8]; but the non-MHC-restricted TABM demonstrate similar characteristics [5,8,21]. TABM can be isolated from serum of sensitized mice [29] and are found on the surface of T cells, as well as in supernatants of lymphoid cell cultures [7,21,31] and display common serologic determinants [6,7], sug gesting a common isotype among antigen-specific T cell factors.…”

Section: Introductionmentioning

confidence: 99%

Identification and Partial Characterization of a T-Cell-Derived Antigen-Binding Factor from Mice Infected with the Intestinal Helminth <i>Trichinella spiralis</i>

Parmentier

Dijkstra

Wissink

et al. 1989

Int Arch Allergy Immunol

View full text Add to dashboard Cite

Immunochemical and biological characterization was performed of an antigen-binding factor derived from culture supernatants of T cells from mice infected 4 days previously with the intestinal helminth Trichinella spiralis. Affinity chromatography with T. spiralis antigen resulted in the purification of a protein, provisionally designated Trichinella factor (Tric-F), that shared antigenic and other properties with a known T-cell-derived antigen-binding factor of different antigenic specificity, picryl chloride factor, which mediates an early 2-hour component of contact sensitivity. Tric-F lacked determinants of immunoglobulins and possessed determinants shared by other antigen-specific T cell factors, as determined by ELISA and antibody affinity chromatography. Biological activity of Tric-F was assayed in vivo and in vitro. Mice injected intravenously with Tric-F developed an antigen-specific early 2-hour ear swelling response following local challenge with T. spiralis antigen. These results corresponded to delayed-type hypersensitivity responses in the ears of T. spiralis-infected mice that comprised early 2-hour and late classical 24-hour responses. In vitro, Tric-F induced serotonin release by mast cells in the presence of T. spiralis antigen. Mast cells sensitized with Tric-F formed rosettes with antigen-coated sheep erythrocytes. It is suggested that Tric-F, an antigen-binding molecule that is T-cell-derived, mediates the early 2-hour component of delayed-type hypersensitivity and is involved in the initiation and regulation of T-cell-mediated intestinal inflammation during a T. spiralis infection in mice.

show abstract

The Biochemistry of Antigen-Specific T-Cell Factors

Cited by 59 publications

References 27 publications

CD3-associated heterodimeric polypeptides on suppressor hybridomas define biologically active inhibitory cells.

CD3-associated heterodimeric polypeptides on suppressor hybridomas define biologically active inhibitory cells.

Biochemical Characterization of an Antigen-Specific Suppressor T Cell Factor

Identification and Partial Characterization of a T-Cell-Derived Antigen-Binding Factor from Mice Infected with the Intestinal Helminth <i>Trichinella spiralis</i>

Contact Info

Product

Resources

About