Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations.

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

doi:10.1073/pnas.78.2.1162

Cited by 267 publications

(154 citation statements)

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“…First identified from a cytokine-like activity, Tβs play significant roles in various physiological processes. (Low et al, 1981). Later studies showed that Tβs' mRNA and protein levels were changed rapidly during differentiation or by different stimuli (Hall, 1991;Huff et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Characterization of two thymosins as immune-related genes in common carp (Cyprinus carpio L.)

Xiao

Shen

Hong

et al. 2015

Developmental & Comparative Immunology

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Section: Introductionmentioning

confidence: 99%

Characterization of two thymosins as immune-related genes in common carp (Cyprinus carpio L.)

Xiao

Shen

Hong

et al. 2015

Developmental & Comparative Immunology

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“…In 1990, Safer et al [l] identified a peptide of approximately 5 kDa in platelets that preferentially binds to G-actin, even in the presence of high salt, thus stabilizing the monomeric pool of G-actin. This protein was found to be identical to thymosin p4 (Tp4) [2], a peptide originally believed to be a thymic hormone [3] and able to modulate the immune responsiveness of peripheral lymphocytes [4, pected presence of Tp4 and related peptides at high concentrations in almost any eukaryotic cell shed doubts on this function [l, [6][7][8][9][10].…”

mentioning

confidence: 99%

Induction of the polymerization of actin from the actin:thymosin β4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin

Ballweber

Hannappel

Niggemeyer

et al. 1994

European Journal of Biochemistry

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Thymosin /34 is able to form 1 : 1 complexes with monomeric (G) actin, thereby stabilizing the intracellular pool of unpolymerized actin. We have searched for factors that are able to induce the polymerization of actin from the actin : thymosin p4 complex. Phalloidin, subfragment 1 isolated from rabbit skeletal muscle myosin and chicken intestinal myosin I are demonstrated to be able to polymerize the actin from this complex in the presence of 1 mM MgCl,. Polymerization of actin was verified by the DNase I inhibition assay, by cosedimentation and from the fluorescence increase of pyrene-labelled actin. Actin filaments formed under the influence of subfragment 1 or phalloidin were visualized under the electron microscope after negative staining. Polymerization of skeletal muscle actin from the complex with thymosin p4 by phalloidin is accompanied by the hydrolysis of the actin-bound ATP to ADP. Polymerization was also induced by sonicated F-actin which possessed a high concentration of free filament ends. F-actin was severed by 0.01 M human cytoplasmic gelsolin, which is known to possess blocked + ends. Free, slowly growing -ends were unable to induce polymerization of actin from the thymosin p4 complex. However, when gelsolin on its own or in complex with two actin molecules was added to actin:thymosin p4 under nucleating conditions, it was found to be able to promote actin repolymerization provided that its concentration was close to the dissociation constant (Kd) of actin:thymosin p4. This Kd was found to be 0.4 yM in the presence of 1 mM MgC1, and the absence of KC1 and, thus, close to the critical concentration of actin polymerization under these conditions. The source of actin did not influence its polymerization from the thymosin p4 complex ; rabbit skeletal muscle actin and porcine brain actin were polymerized with equal efficiency from their complexes with thymosin /34 by both phalloidin and myosin subfragment 1. Skeletal muscle, but not cytoplasmic actin, was found to be also polymerized in the presence of increased CaC1, concentrations to values above 1 mM.Actin is present at a high concentration in virtually all types of eukaryotic cells. About 50% of the intracellular actin is stabilized in the monomeric form, although the ionic conditions of the cytoplasm favour its complete polymerization to F-actin. There is now ample evidence that approximately 50% of the intracellular actin is stabilized in the monomeric form in complexes with sequestering factors. This unpolymerized actin is able to enter the polymeric pool after an appropriate intracellular or extracellular signal. In 1990, Safer et al. [l] identified a peptide of approximately 5 kDa in platelets that preferentially binds to G-actin, even in the presence of high salt, thus stabilizing the monomeric pool of G-actin. This protein was found to be identical to thymosin p4 (Tp4) [2], a peptide originally believed to be a thymic hormone [3] and able to modulate the immune responsiveness of peripheral lymphocytes [4, 51. However, the unex-

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“…Thymosin-β4 was first isolated from calf thymosin fraction 5; it is also found in various organs such as the spleen, thymus, liver that exhibit biological activity on the immune system cells. Thymosin-β4 has been reported to suppress the mixed lymphocyte proliferative response, 14 induce the expression of terminal deoxynucleotidyl transferase in T cells, 15 inhibit the migration of macrophages in vitro, 16 and inhibit cytokine production by neutrophils after tumor necrosis factor (TNF)-α stimulation. 17 TGF-β, which can be released by thymocyte and thymic epithelial cells, almost inhibits all lymphocyte proliferation, including mitogen-and allogenic antigen-induced T-cell proliferation and Staphylococcus aureus Cowan I (SAC)-induced and IL-2 independent B-cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

Acute Electrical Stimulation of Nucleus Ambiguus Enhances Immune Function in Rats

Mei¹,

Yang²,

Wang³

et al. 2008

Can. j. neurol. sci.

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It is well known that there exists bidirectional regulation in the central nervous system (CNS) and immune system. [1][2][3] The CNS can have a widespread effect on the immune system following the activation of the hypothalamic-pituitary-adrenal axis 4,5 and the sympathetic nervous system. 3,6,7 Thus far, many regions in the brain such as the hypothalamic nuclei, brain reward system, limbic structures, cortex, midbrain periaqueductal gray matter, cerebellum, circumventricular organs, and vagal complex have been identified as "immunoactive" areas. 8 The nucleus ambiguous (Amb), that is a nucleus of the vagus nerve, is located in the ventrolateral reticulate structure of the medulla oblongata. Thus far, probably owing to traditional ideas regarding this area, study of the Amb ABSTRACT: Background: Up to now, many ''immunoactive'' brain areas have been identified, such as hypothalamic nuclei, brain reward system; but the nucleus ambiguous (Amb), a nucleus nervi vagis of medulla oblongata, was less well studied in neuroimmunomodulation. Methods: In order to obtain more profound comprehension and more knowledge on Amb, we studied the effect of acute electrical stimulation of Amb on thymus and spleen activity in rat. A stimulator was applied to stimulate the Amb of the anaesthetic rats using the parameter at 100μA×5ms ×100 Hz every 1s for 1 min. The levels of TGF-β and thymosin-β4 mRNA in thymus, the release of IL-2 and IL-6 at splenocyte in vitro and splenic lymphocyte proliferation were measured at hour 0.5,1,2,3 following the electrical stimulation. Results: The results showed that concanavalin A (Con A)-induced splenic lymphocyte proliferation and the release of IL-2 and IL-6 were all significantly enhanced at 0.5, 1, and 2 h following effective Amb stimulation as compared to in the control group. However, as compared to in the control group, the levels of TGF-β and thymosin-β4 mRNA in the thymus were both remarkably reduced at 0.5, 1, and 2 h following effective Amb stimulation. Conclusions: These findings reveal that the Amb participates in the modulation of animal immune functions.RÉSUMÉ: La stimulation électrique aiguë du noyau ambigu stimule la fonction immunitaire chez le rat. Contexte : Plusieurs zones immunoactives du cerveau ont été identifiées jusqu'à maintenant, dont les noyaux hypothalamiques (corps de Luys, noyau sous-thalamique), le système de récompense du cerveau. Cependant, il existe peu d'études sur le rôle du noyau ambigu (Amb), le noyau du nerf vague situé dans le bulbe rachidien, dans la neuro-immunomodulation. Méthodes

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Complete amino acid sequence of bovine thymosin beta 4: a thymic hormone that induces terminal deoxynucleotidyl transferase activity in thymocyte populations.

Abstract: The amino acid sequence of thymosinj,84, a polypeptide isolated from calf thymus, was determined. Thymosin 184 is composed of 43 amino acid residues and has a molecular weight of 4982 and an isoelectric point of 5.

Cited by 267 publications

References 33 publications

Characterization of two thymosins as immune-related genes in common carp (Cyprinus carpio L.)

Characterization of two thymosins as immune-related genes in common carp (Cyprinus carpio L.)

Induction of the polymerization of actin from the actin:thymosin β4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin

Acute Electrical Stimulation of Nucleus Ambiguus Enhances Immune Function in Rats

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