Modulation of terminal deoxynucleotidyl transferase activity by thymosin

Hu, Shu-Kuang; Low, Teresa L. K.; Goldstein, Allan L.

doi:10.1007/978-94-009-8030-3_6

Cited by 11 publications

(13 citation statements)

References 25 publications

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“…Although its role was initially attributed to T cell differentiation (7), it later was found that thymosin β 4 binds to G-actin in a 1:1 complex that prevents monomeric G-actin from polymerizing to filamentous F-actin but supplies a pool of actin monomers inside the cells (12,13). We and others identified thymosin β 4 as an angiogenic factor with activity during HUVEC differentiation in vitro and in vivo (5,(14)(15)(16).…”

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confidence: 99%

“…Thymosin β 4 , a 43 amino acid peptide, is the most abundant member of the β-thymosins, a family of highly conserved 5 kD peptides (6). Thymosin β 4 was first isolated from calf thymus and was later found in a variety of tissues and cell types as well as in malignant cells (7)(8)(9)(10)(11). By using cDNA subtractive cloning in an in vitro vessel-forming assay for angiogenesis, thymosin β 4 expression A was increased in human umbilical vein endothelial cells (HUVECs) that were plated on Matrigel compared with HUVECs plated on plastic (5).…”

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confidence: 99%

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The actin binding site on thymosin β₄promotes angiogenesis

et al. 2003

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Thymosin beta4 is a ubiquitous 43 amino acid, 5 kDa polypeptide that is an important mediator of cell proliferation, migration, and differentiation. It is the most abundant member of the beta-thymosin family in mammalian tissue and is regarded as the main G-actin sequestering peptide. Thymosin beta4 is angiogenic and can promote endothelial cell migration and adhesion, tubule formation, aortic ring sprouting, and angiogenesis. It also accelerates wound healing and reduces inflammation when applied in dermal wound-healing assays. Using naturally occurring thymosin beta4, proteolytic fragments, and synthetic peptides, we find that a seven amino acid actin binding motif of thymosin beta4 is essential for its angiogenic activity. Migration assays with human umbilical vein endothelial cells and vessel sprouting assays using chick aortic arches show that thymosin beta4 and the actin-binding motif of the peptide display near-identical activity at ~50 nM, whereas peptides lacking any portion of the actin motif were inactive. Furthermore, adhesion to thymosin beta4 was blocked by this seven amino acid peptide demonstrating it as the major thymosin beta4 cell binding site on the molecule. The adhesion and sprouting activity of thymosin beta4 was inhibited with the addition of 5-50 nM soluble actin. These results demonstrate that the actin binding motif of thymosin beta4 is an essential site for its angiogenic activity.

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The actin binding site on thymosin β₄promotes angiogenesis

et al. 2003

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“…Von Willebrand factor, which is associated with adverse cardiovascular events and endothelial cell dysfunction, is down‐regulated by Tβ 4 . Interestingly, terminal deoxynucleotidyl transferase is induced by Tβ 4 , and this may explain, in part, its antiapoptotic activity (31, 32). Many of the molecules regulated by Tβ 4 are important in wound repair and define possible mechanisms by which this protein has so many different effects in the repair process.…”

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Biological activities of thymosin ß₄defined by active sites in short peptide sequences

Sosne¹,

et al. 2010

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Thymosin beta(4), a small ubiquitous protein containing 43 aa, has structure/function activity via its actin-binding domain and numerous biological affects on cells. Since it is the major actin-sequestering molecule in eukaryotic cells and is found essentially in all cells and body fluids, thymosin beta(4) has the potential for significant roles in tissue development, maintenance, repair, and pathology. Several active sites with unique functions have been identified, including the amino-terminal site containing 4 aa (Ac-SDKP) that generally blocks inflammation and reduces fibrosis. Another active site at the amino terminus contains 15 aa, including Ac-SDKP, and promotes cell survival and blocks apoptosis, while a short sequence containing LKKTETQ, the central actin-binding domain (aa 17-23) plus 1 additional amino acid (Q), promotes angiogenesis, wound healing, and cell migration. Several additional biological activities have been identified but not yet localized in the molecule, including its antimicrobial activity, the induction of various genes (including laminin-5, MMPs, TGF beta, zyxin, terminal deoxynucleotidyl transferase, and angiogenesis-related proteins), and the ability to activate ILK/PINCH/Akt, and other signaling molecules important in both apoptosis and inflammatory pathways. This review details these important physiologically and pathologically active sites and their potential therapeutic uses.

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“…Moreover, Ta1 can reduce apoptosis of immune cells, as shown in mouse [55,56] and human [57,58] thymocytes, and increase stem cell expansion in immunosuppressed mice [59][60][61]. Additionally, Ta1 leads to increased expression of the thymopoetic cytokines IFN-alpha, IL-7, and IL-15 [37,57].…”

Section: Immune Stimulating Effectsmentioning

confidence: 99%

Thymosin Apha 1–A Peptide Immune Modulator with a Broad Range of Clinical Applications

King¹

2013

Clin Exp Pharmacol

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Modulation of terminal deoxynucleotidyl transferase activity by thymosin

Cited by 11 publications

References 25 publications

The actin binding site on thymosin β₄promotes angiogenesis

The actin binding site on thymosin β₄promotes angiogenesis

Biological activities of thymosin ß₄defined by active sites in short peptide sequences

Thymosin Apha 1–A Peptide Immune Modulator with a Broad Range of Clinical Applications

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Modulation of terminal deoxynucleotidyl transferase activity by thymosin

Cited by 11 publications

References 25 publications

The actin binding site on thymosin β4promotes angiogenesis

The actin binding site on thymosin β4promotes angiogenesis

Biological activities of thymosin ß4defined by active sites in short peptide sequences

Thymosin Apha 1–A Peptide Immune Modulator with a Broad Range of Clinical Applications

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Product

Resources

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The actin binding site on thymosin β₄promotes angiogenesis

The actin binding site on thymosin β₄promotes angiogenesis

Biological activities of thymosin ß₄defined by active sites in short peptide sequences