Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling.

Freeman KW, Bowman BR, Zetter BR

FASEB journal : official publication of the Federation of American Societies for Experimental Biology24 Nov 2010Cited by 61 (Europe PMC)

PMID21106936DOI10.1096/fj.10-169417PepBankPUB-21106936

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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study8

4 results from studies that gave the peptide. No result from this study comes from people.

01LabIn vitro (cells)Mechanism
Pulldown with biotinylated thymosin beta‑4 and mass spectrometry identified F1-F0 ATP synthase as an interacting protein.
In plain wordsIn lab tests, thymosin beta‑4 was found to interact with the enzyme ATP synthase.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableInteracting proteins identified by Tβ4 pulldown
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Source sentences
Summary
By this method, we identified F1-F0 ATP synthase, a known target of antiangiogenic angiostatin.
2 context sentences(design, population, supporting numbers)
Summary · context
We performed pulldown experiments with biotinylated thymosin β-4 (Tβ4) in comparison to neutravidin beads alone and used mass spectrometric analysis to identify differentially interacting proteins.
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
Report a problemFND-2110693602
02LabIn vitro (cells)Mechanism
In human umbilical vein endothelial cells, thymosin beta‑4 increased cell surface ATP levels via ATP synthase.
In plain wordsIn human blood vessel cells in a dish, thymosin beta‑4 raised ATP on the cell surface.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseCell surface ATP levels
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Cardiovascular
Studied dose
Dose not stated
Source sentences
Summary
we have identified an extracellular signaling pathway where Tβ4 increases cell surface ATP levels via ATP synthase
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
Report a problemFND-2110693603
03LabIn vitro (cells)Activity measurement
In human umbilical vein endothelial cells, thymosin beta‑4 increased migration in a transwell assay.
In plain wordsIn human blood vessel cells in a dish, thymosin beta‑4 increased cell migration.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseHUVEC migration
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Cardiovascular
Studied dose
Dose not stated
Source sentences
Summary
and the Tβ4-induced increase in HUVEC migration, as measured by transwell migration assay.
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
Report a problemFND-2110693604
04LabIn vitro (cell-free)Activity measurement
By surface plasmon resonance, thymosin beta‑4 bound the beta subunit of ATP synthase with a KD of 12 nM.
In plain wordsIn lab tests, thymosin beta‑4 bound tightly to a part of the enzyme ATP synthase.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableTβ4 binding to the β subunit of ATP synthase
Study
n: not reported in source
surface plasmon resonance
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Measurements
KD
12 nM
Tβ4 binding to the β subunit of ATP synthase
Source sentences
Summary
By surface plasmon resonance, we determined for Tβ4 binding to the β subunit of ATP synthase a K(D) of 12 nM.
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
Report a problemFND-2110693601

Studies that did not test the peptide alone4

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cells)Mechanism
In human umbilical vein endothelial cells, ATP synthase blocking antibodies and antagonists (oligomycin, piceatannol, angiostatin) inhibited the thymosin beta‑4-induced increase in cell surface ATP.
In plain wordsIn human blood vessel cells in a dish, ATP synthase blockers stopped the rise in surface ATP that thymosin beta‑4 caused.
Peptide
Thymosin beta-4 (human)
Outcome
DecreaseTβ4-induced cell surface ATP with ATP synthase blockers
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Cardiovascular
Source sentences
Summary
Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels, as measured by luciferase assay, and the Tβ4-induced increase in HUVEC migration, as measu…
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-2110693605
06LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cells)Mechanism
In human umbilical vein endothelial cells, ATP synthase blocking antibodies and antagonists inhibited the thymosin beta‑4-induced increase in migration.
In plain wordsIn human blood vessel cells in a dish, ATP synthase blockers stopped the extra cell movement that thymosin beta‑4 caused.
Peptide
Thymosin beta-4 (human)
Outcome
DecreaseTβ4-induced HUVEC migration with ATP synthase blockers
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Cardiovascular
Source sentences
Summary
Blocking antibodies and antagonists (oligomycin, IC(50) ∼1.8 μM; piceatannol, IC(50) ∼1.05 μM; and angiostatin, IC(50) ∼2.9 μg/ml) of ATP synthase inhibited the Tβ4-induced increase in cell surface ATP levels, as measured by luciferase assay, and the Tβ4-induced increase in HUVEC migration, as measu…
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-2110693606
07LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cells)Mechanism
In human umbilical vein endothelial cells, siRNA silencing of the P2X4 receptor blocked thymosin beta‑4-induced migration.
In plain wordsIn human blood vessel cells in a dish, switching off the P2X4 receptor stopped the extra cell movement that thymosin beta‑4 caused.
Peptide
Thymosin beta-4 (human)
Outcome
DecreaseTβ4-induced HUVEC migration with P2X4 silencing
Study
humann: not reported in source
HUVECs
Outcome group
Receptor activity and mechanism · Cardiovascular
Source sentences
Summary
Silencing of the ATP-responsive purinergic receptor P2X4 with siRNA also blocked Tβ4-induced HUVEC migration in a transwell assay.
1 context sentence(design, population, supporting numbers)
Summary · context
We were interested in identifying β-thymosin interactors and determining their importance in β-thymosins signaling in human vein endothelial cells (HUVECs).
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-2110693607
08Computer modelNot a test of Thymosin beta-4 (human) aloneIn silicoMechanism
In silico analysis found amphiphilic alpha-helical structural similarities between beta-thymosins and inhibitory factor 1 of ATP synthase.
In plain wordsIn a computer analysis, beta-thymosins shared structural features with a natural inhibitor of ATP synthase.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableStructural similarity of β-thymosins to ATP synthase inhibitory factor 1
Study
n: not reported in source
in silico structure comparison
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Furthermore, in silico we identified common amphiphilic α-helical structural similarities between β-thymosins and the inhibitory factor 1 (IF1), an inhibitor of ATP synthase hydrolysis.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-2110693608

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

Version 2Current
13 Oct 2026, 01:52 UTC
Study results updated
Version 1
12 Oct 2026, 18:17 UTC
First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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Journal Article

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