Spontaneous release of Fc receptor‐like material from human lymphoblastoid cell lines

Molenaar, J Jaap; Galen, M.A. van; Hannema, A.J.; Zeijlemaker, W. P.; Pondman, K. W.

doi:10.1002/eji.1830070409

Cited by 53 publications

(26 citation statements)

References 34 publications

(8 reference statements)

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“…With this procedure, the FcT-binding protein changed its mol wt to 115,000, probably by forming tetramers. The 115,000-dalton protein was reminiscent of the 125,000-dalton peak of Cooper et al (14), the 120,000-dalton peak of Bourgeois et al (17), the 110,000-dalton peak of Frade and Kourilsky (16), and the 100,000-dalton peak of Molenaar et al (15). The Fcy-binding proteins described by those authors might correspond to the tetrameric FcT,-affined proteins that we isolated.…”

Section: Segment Nosupporting

confidence: 55%

“…The Fcy-binding proteins described by those authors might correspond to the tetrameric FcT,-affined proteins that we isolated. This assumption would explain why the 100,000-dalton protein described by Molenaar et al (15) was able to agglutinate EA and our 28,000-dalton peak was not. In its tetrameric form, the IgG-binding protein should be muhivalent and thus capable of agglutinating EA.…”

Section: Segment Nomentioning

confidence: 56%

“…It is notable, however, that in two of those studies the Fcy-binding proteins revealed apparent mol wt of 110,000 and 120,000, respectively, under nonreducing conditions. Two research groups (13,15) looked for Fcy-binding material either spontaneously released from cells or released by shedding with IgG aggregates and anti-IgG antibodies. One group (13) reported on the isolation of a 45,000-dalton protein from a murine leukemia cell line (L1210) and the other (15) on a 100,000-dalton protein from human lymphoid cell lines.…”

Section: Segment Nomentioning

confidence: 99%

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Properties of an Fc gamma-binding protein isolated from human leukemic B cells.

Thoenes¹,

Stein²

1979

The Journal of Experimental Medicine

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A selectively Fc gamma-binding protein was isolated from purified and radioiodinated cell membranes from two cases of B-type chronic lymphocytic leukemia and one case of B-type prolymphocytic leukemia by binding to IgG aggregates, horseradish peroxidase-anti-peroxidase IgG complexes, and sheep erythrocyte membrane sheets densely coated with IgG. This protein could not be isolated from the cell membranes of an Fc gamma-receptor-negative chronic lymphocytic leukemia of the T type or from membranes of human erythrocytes. The Fc gamma-binding protein was efficiently solubilized by a mixture of Na-EDTA and 2-mercaptoethanol, but not with one of these agents alone, indicating that both divalent cations and disulfide bridges are involved in the linkage of the Fc gamma-binding protein to the cell membrane. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the Fc gamma-binding protein revealed an apparent mol wt of 28,000 and in isoelectric focusing it showed an isoelectric point of 5.5. The electrophoretic mobility of the 28,000-dalton protein did not change after reduction and alkylation. It was determined that the NH2-terminal amino acid of the protein was glycine. The isolated protein was unable to agglutinate antibody-coated erythrocytes. These findings suggest that the 28,000-dalton IgG-affined protein was composed to O2-enriched buffer lacking reducing agents, the 28,000-dalton protein aggregated to a 115,000-dalton molecule. The isolated Fc gamma-binding protein proved to be different from C1q or its subunits.

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Section: Segment Nosupporting

confidence: 55%

Section: Segment Nomentioning

confidence: 56%

Section: Segment Nomentioning

confidence: 99%

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Properties of an Fc gamma-binding protein isolated from human leukemic B cells.

Thoenes¹,

Stein²

1979

The Journal of Experimental Medicine

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“…In mice as well as in man it has been shown that T-cells release FcyR which exert nonspecific suppression of the primary PFC response to SE in vitro (19,20). The cells were found to be less suppressive after having lost their FcR (19).…”

Section: Discussionmentioning

confidence: 99%

Localization of human antigen-specific helper and suppressor function in distinct T-cell subpopulations

Heijnen

Uytdehaag

Gmelig-Meyling

et al. 1979

Cellular Immunology

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Distinct human T-cell subpopulations were isolated and cultured in the presence of B-cells and antigens. After an incubation period of 6 days cells were tested for their capacity to secrete antigen-specific antibodies in the PFC-assay. The results indicate that the T-helper activity for the antigen-induced T-dependent B-cell differentiation is located in the Tp-subpopulation, whereas the suppressor-cell activity is confined to the Ty-subpopulation.

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“…The mouse and human T cell lines that express FcgR upon activation release soluble FcRs which, in vitro, suppress the production of immunoglobulin [59]. The enrichment of FcRs during MR aggregation could result in enhanced receptor shedding [34].…”

Section: Cd4mentioning

confidence: 99%