Localization of Thymosin β‐4 in Tumors
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Overexpression of thymosin beta-4 has been linked to malignant progression but the localization of this polypeptide within tumors is incompletely known. We therefore examined breast cancers for thymosin beta-4 using immunofluorescence. Reactive cells were identified with monoclonal cell marker antibodies. A very heterogeneous staining pattern for thymosin beta-4 was observed. Thus, while leukocytes and macrophages showed intense reactivity for this polypeptide, cancer cells, and endothelial cells showed a much more variable reactivity. A similar heterogeneous staining was observed also in colorectal carcinomas. The degree of staining of breast cancer cells for thymosin beta-4 correlated neither to histological grade nor to endothelial cell staining. However, there was a tendency toward correlation (P = 0.07) between staining of endothelial cells and histological grade. Treatment of cultured breast cancer cells (SK-BR-3) with 1-4 microg thymosin beta-4/mL significantly increased cell numbers, as determined by MTT-assays. These data reveal an unexpected cellular heterogeneity of thymosin beta-4 expression in breast and colonic carcinomas and suggest that local release of this polypeptide in the tumor microenvironment may modulate tumor behavior.Keywords:
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A partially purified extract from thymus tissue termed thymosin Fraction 5 has been shown to reconstitute immunological deficiencies resulting from the lack of thymic function in several animal models, as well as humans with primary and secondary immunodeficiency diseases. Thymosin Fraction 5 consists of a family of polypeptides with molecular weights ranging from 1,000 to 15,000. Several of these polypeptides contribute individually to the biological activity of the parent compound. Two polypeptide components of thymosin Fraction 5, termed thymosin alpha1 and polypeptide beta1, have been characterized chemically and biologically. Thymosin alpha1 is a highly acidic molecule composed of 28 amino acid residues. This polypeptide has potent biological activity and has been found to be 10 to 1,000 times as active as thymosin Fraction 5 in one in vivo and several in vitro bioassay systems designed to measure differentiation and function of thymus-dependent lymphocytes (T cells). Polypeptide beta1, in contrast, is inactive in our bioassay systems, suggesting that it is not involved in thymic hormone action. Sequence analysis and homology studies have indicated that polypeptide beta1, although present in Fraction 5, does not contribute to the biological activity of thymosin Fraction 5.
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Guanidinium chloride
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The indirect ELISA method for measuring thymosinα1content in the transgenic Synochococcus sp.PCC7942with thymosinα1gene has been established by using the anti_thymosinα1-BSA fusion protein serum prepared in rabbits.The experiment reveals that the method is sensitive,specific and reliable.It can be used to measure content of thymosinα1expressed in transgenic Synochococcus sp.PCC7942with thymosinα1gene.It also shows that thymosinα1gene can be expressed steadily in Synochococcus sp.PCC7942.
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Thymosin
Peptide fragment
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【Objective】To investigate the effect of thymosin-α1 on immune function and cytokines in the CNS infective and discuss the therapeutic function of thymosin-α1 in sepsis. 【Methods】Fifty-two sepsis patients admitted between February 2006 and June 2008 were randomly divided into the treatment group (27 cases) and control group (25 cases). Thymosin-α1 was used in the treatment group on the basis of infection control treatment. The concentration of cytokines (TNF-α, IL-6) and the percentage of CD3+, CD4+, CD8+, NK cell were observed. 【Results】 The concentrations of TNF-α and IL-6 were increased significantly in both group. But it was more prominently in the control group. The percent of CD3+, CD4+ cell increased more significantly in thymosin-α1 treatment group than in the control group. 【Conclusion】Thymosin-α1 can modulate the release of TNF-α, IL-6, mitigate the inflammatory reaction and improve the immune function.
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Objective:To isolate and purify thymosin β4 from calf thymus.Methods: Thymosin fraction 5 was extracted by ammonium sulfate precipitation.Thymosin β4 was purified by ion exchange chromatography,and elucidated by SDS-PAGE and HPLC.Results:The purity of thymosin β4 was 90.1%.Conclusion:Thymosin β4 was purified by ion exchange chromatography and warranted for the pilot manufacture.
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Ammonium sulfate precipitation
Ion chromatography
Ammonium sulfate
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