Thymosin beta 4: a ubiquitous peptide in rat and mouse tissues.

Hannappel, Ewald; Xu, Guangli; Morgan, James I.; Hempstead, J.; Horecker, B.L.

doi:10.1073/pnas.79.7.2172

Cited by 141 publications

(102 citation statements)

References 14 publications

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“…For the extract derived from 28 g of tissue, 28 such sets of three cartridges (84 total) were required. The cartridges containing the adsorbed peptides were washed with buffer A (20 ml for each set of three cartridges), and each set was eluted with 10 ml of the same buffer containing 20% 1-propanol (11). The recovery of immunoreactive mat'rial in the combined eluates was 63% of that present in the solution applied to the Sep-Paks.…”

Section: Methodsmentioning

confidence: 99%

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Haritos¹,

Goodall²,

Horecker³

1984

Proc. Natl. Acad. Sci. U.S.A.

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193

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A polypeptide containing -112 amino acid residues, with the thymosin a, sequence at its NH2 terminus, has been isolated from rat thymus by using a radioimmunoassay with an antibody prepared against synthetic thymosin ap. The new polypeptide, named "prothymosin a," was found to be the major substance crossreacting with thymosin a, antiserum in rat thymus extracts; peptides corresponding to thymosin a, or thymosin a,, were not detected. In gel filtration at pH 2.8, prothymosin a emerged as a single symmetrical peak corresponding to an apparent molecular weight of 32,000, approximately 3 times larger than the minimum molecular weight calculated from its amino acid composition. Thymosin a,, a peptide containing 28 amino acid residues, was isolated by Goldstein and coworkers (1) from thymosin fraction 5, a mixture of peptides from calf thymus (2). Thymosin fraction 5 had been reported earlier to restore parameters of immunocompetence in neonatally thymectomized mice (3). Thymosin a1 was found to be active in some of the in vitro tests used for thymosin fraction 5 (4), and it was considered to be one of the factors that modulated steps in the maturation of T cells (5).We have reported (6) our inability to detect thymosin a1 in guanidinium chloride extracts of calf thymus. The suggestion that thymosin a1 might represent a proteolytic fragment of a larger native polypeptide was supported by the finding that preparations of calf thymosin fraction 5 contained at least two other related peptides (7). One of these, designated des-(25-28)-thymosin a1, contained only the first 24 amino acid residues; the other, named thymosin all, contained the sequence of thymosin a1 plus seven additional residues at the COOH terminus.In an effort to isolate the native thymic polypeptide from which these fragments appeared to be derived, we developed a radioimmunoassay based on an antibody prepared against synthetic thymosin a1. With this assay and a procedure designed to eliminate any possibility of proteolytic modification, we isolated a major polypeptide, =112 amino acid residues long, that contains the thymosin a1 sequence at its NH2 terminus. We named this polypeptide prothymosin a because it appears to be the source of the thymosin a1-related peptide fragments found in preparations of thymosin fraction 5. MATERIALS AND METHODSRat thymuses from male Charles River CD rats, 5 weeks old, were excised immediately after sacrifice of the animals by decapitation, quickly frozen in liquid nitrogen, and stored at -700C. Synthetic thymosin a, (8) was provided by A. Felix of Hoffmann-La Roche. Trypsin (L-1-tosylamido-2-phenylmethyl chloromethyl ketone-treated) and Staphylococcus aureus V8 protease were from Worthington and Miles Laboratories respectively. Fluorescamine was a gift of W. E. Scott of Hoffmann-La Roche. Sephacryl S-200 (superfine) was purchased from Pharmacia. Other reagents and solvents were chromatography-grade commercial preparations; the solvents were redistilled as required.For preparation of the antibody, rabbits were in...

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Section: Methodsmentioning

confidence: 99%

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Haritos¹,

Goodall²,

Horecker³

1984

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

193

158

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“…6). Its highly conserved structure suggests that it has an important biological function, but its proposed role as a thymic hormone (1) has been brought into question by the relatively large amounts found in tissues other than the thymus (2,4) and the finding that it is actively synthesized by cells unrelated to the reticuloendothelial system (5).…”

mentioning

confidence: 99%

“…More recently, thymosin 384 was shown to be widely distributed in cells and tissues of vertebrate species ranging from amphibia to mammals (refs. [2][3][4][5]; for a review, see ref. 6).…”

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confidence: 99%

Cloning and sequence analysis of cDNA for rat spleen thymosin beta 4.

Wodnar-Filipowicz¹,

Gubler²,

Furuichi³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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Molecular cloning of a cDNA has established the sequence of the translated portion of the mRNA for rat spleen thymosin beta 4. The presence of a methionyl initiator codon immediately preceding the codon for the first seryl residue of mature thymosin beta 4 is consistent with previous results indicating the absence of a signal peptide in the product translated in vitro from rat spleen mRNA. The cDNA sequence analysis also established the presence of two terminator codons immediately following the codon for the COOH-terminal seryl residue. Thymosin beta 4 is thus synthesized as a 5100-dalton peptide containing 44 amino acid residues. Removal of the initiator methionyl residue and acetylation of the NH2-terminal serine residue would yield mature thymosin beta 4 containing 43 amino acids. The absence of a signal peptide makes it unlikely that thymosin beta 4 is a secreted peptide.

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“…Thymosin 134 (T134), a 43 residue peptide, is the most abundant member of this family and it is present in all mammalian species accompanied by its structural homologue thymosin 1310 (T~m) in many cell types [3,4]. Although T13a and T13m coexist in many tissues at varying ratios, the biological meaning of this association has still to be elucidated.…”

Section: Introductionmentioning

confidence: 99%

Thymosin β₁₀ mRNA expression during early postimplantation mouse development

et al. 1996

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The ~thymosins are a family of monomeric actin sequestering peptides that regulate actin dynamics within the cells. During embryogenesis the control of actin polymerization is essential in processes such as cell migration, angiogenesis and neurogenesis. Here we report that the levels of thymosin 1~10 (T~10) mRNA strongly increase during early postimplantation mouse embryogenesis as well as during in vitro P19 cell differentiation, indicating that this peptide plays an important role in early development. Moreover, analysis of the spatial distribution of Till0 mRNA in 9.5-12.5 days postcoitum mouse embryos showed a remarkable presence of this transcript in mesenchymal structures as well as in the mantle layer of spinal cord. Interestingly, we observed differences in the distribution of the mRNAs encoding Till0 and T134, another member of the ~-thymosin family, suggesting different roles for these peptides during mouse embryogenesis.Key words: Thymosin 1310; Actin-binding peptide; P19 cell; Mouse embryogenesis activated during early phases of neuroembryogenesis [13] and also in the mature brain [7,9,14]. We have previously shown that T134 mRNA is very abundant in different embryonic tissues, principally nerve structures [l 3] and cardiovascular tissues [15], suggesting that this peptide plays an important role in the development of mouse nervous system as well as in angiogenesis. However, little is known about the expression of the T1310 gene during early postimplantation mouse development.In the present work we studied the levels of T~10 mRNA in culture systems that can undergo cell differentiation. For this purpose we employed the murine P19 embryonal carcinoma cell line, a well-established model for studying cell differentiation as it relates to the early stages of embryogenesis [16]. We also analyzed the spatial and temporal distribution of T[310 mRNA during early mouse development. We show that the T~10 gene is expressed early during development mostly in mesenchymal structures and in some areas of the nervous system.

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Thymosin beta 4: a ubiquitous peptide in rat and mouse tissues.

Cited by 141 publications

References 14 publications

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Cloning and sequence analysis of cDNA for rat spleen thymosin beta 4.

Thymosin β₁₀ mRNA expression during early postimplantation mouse development

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Thymosin beta 4: a ubiquitous peptide in rat and mouse tissues.

Cited by 141 publications

References 14 publications

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.

Cloning and sequence analysis of cDNA for rat spleen thymosin beta 4.

Thymosin β10 mRNA expression during early postimplantation mouse development

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Thymosin β₁₀ mRNA expression during early postimplantation mouse development