Abstract
Six-membered peptide fragment TGENHR (HLDF-6) was identified in the HL-60 cell culture of human promyelocyte leukemia treated with retinoic acid when studying the differentiation factor HLDF of this cell line. HLDF-6 retains the ability of the full-size factor to induce the differentiation and arrest the proliferation of the starting HL-60 cells. It was shown that the synthetic peptide HLDF-6 has no specific receptors on the surface of the HL-60 cells but can affect the binding of interleukin IL-1 beta, a cytokine involved in proliferation, to the cell surface. It was found on a model of transplantable NSO myeloma that HLDF-6 has an antitumor activity.
MeSH terms
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Animals
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Antineoplastic Agents / chemistry*
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Antineoplastic Agents / metabolism
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Antineoplastic Agents / pharmacology
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Cell Differentiation
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Cell Division / drug effects
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HL-60 Cells
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Humans
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Interferon-alpha / metabolism
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Interleukin-1 / metabolism
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Male
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Membrane Fluidity / drug effects
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Mice
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Mice, Inbred BALB C
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Neoplasm Proteins / chemistry*
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Peptide Fragments / pharmacology
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Protein Binding
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Recombinant Proteins / metabolism
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Xenograft Model Antitumor Assays
Substances
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Antineoplastic Agents
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Interferon-alpha
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Interleukin-1
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Neoplasm Proteins
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Peptide Fragments
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Recombinant Proteins
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cell differentiation factor 8.2-kDa