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Human B-cell TNF-beta microheterogeneity.

D Benjamin1, G Kofler, E Tschachler

  • 1Lymphokine Research Laboratory, Arthur G. James Cancer Hospital, Ohio State University, Columbus 43210.

Lymphokine and Cytokine Research
|February 1, 1992
PubMed
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Human B-cell lines produce tumor necrosis factor-alpha (TNF-alpha) and tumor necrosis factor-beta (TNF-beta). Differences in TNF-beta glycosylation affect its neutralization and biological activity, particularly in AIDS-associated B-cell lines.

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Tumor necrosis factor-alpha (TNF-alpha) and TNF-beta are key cytokines involved in immune responses.
  • B-cell lines, including Epstein-Barr virus-positive (EBV+), EBV-negative (EBV-), and AIDS-associated B-cell lines (AABCL), are studied for their cytokine production.
  • Understanding TNF production and modification in B cells is crucial for immune system research.

Purpose of the Study:

  • To investigate the molecular and biological production of TNF-alpha and TNF-beta by various human B-cell lines.
  • To analyze the microheterogeneity of TNF-beta and its potential link to glycosylation.
  • To assess the functional significance of TNF glycosylation on secretion, neutralization, and cytotoxic activity.

Main Methods:

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  • Radioimmunoprecipitation was used to detect TNF-alpha and TNF-beta.
  • Deglycosylation studies with specific enzymes (N-glycanase, neuraminidase, O-glycanase) were performed on TNF-beta.
  • TNF secretion, neutralization by antibodies, and biological activity were assessed across 24 B-cell lines.

    • Main Results:

    • TNF-alpha was detected at 17 kDa, while TNF-beta showed microheterogeneity (26, 24, 22 kDa in AABCL; 26, 22 kDa in non-AABCL).
    • Deglycosylation reduced all TNF-beta forms to an 18.6 kDa backbone, indicating glycosylation as the cause of heterogeneity.
    • Constitutive TNF-alpha and TNF-beta secretion was observed only in AABCL; secretion was induced by teleocidin in other cell lines. Neutralization by antibodies was limited.

    Conclusions:

    • Differential glycosylation of B-cell-derived TNF-beta contributes to its molecular heterogeneity.
    • Glycosylation differences may explain incomplete antibody-mediated neutralization of TNF.
    • Altered glycosylation patterns of TNF could influence its cytotoxic biological activity, especially in AABCL.