Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.

Ballweber E, Hannappel E, Niggemeyer B, Mannherz HG

European journal of biochemistry1 Jul 1994Cited by 11 (Europe PMC)

PMID8055911DOI10.1111/j.1432-1033.1994.tb19009.xPepBankPUB-08055911

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 study10

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

01LabIn vitro (cell-free)Activity measurement
In a cell-free system, the Kd of the actin:thymosin beta‑4 complex was 0.4 microM in 1 mM MgCl2 without KCl.
In plain wordsIn lab tests, the actin:thymosin beta‑4 complex had a Kd of 0.4 microM in 1 mM MgCl2 without KCl.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableKd of actin:Tb4 complex
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Measurements
Kd
0.4 µM
1 mM MgCl2, no KCl
Source sentences
Summary
This Kd was found to be 0.4 microM in the presence of 1 mM MgCl2 and the absence of KCl and, thus, close to the critical concentration of actin polymerization under these conditions.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
Report a problemFND-0805591108

Studies that did not test the peptide alone9

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).

02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, phalloidin polymerized actin from the actin:thymosin beta‑4 complex in the presence of 1 mM MgCl2.
In plain wordsIn lab tests, phalloidin made actin form filaments from the actin:thymosin beta‑4 complex.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin polymerization from actin:Tb4 complex with phalloidin
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
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 MgCl2
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591101
03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, rabbit skeletal muscle myosin subfragment 1 polymerized actin from the actin:thymosin beta‑4 complex in the presence of 1 mM MgCl2.
In plain wordsIn lab tests, a muscle myosin fragment made actin form filaments from the actin:thymosin beta‑4 complex.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin polymerization from actin:Tb4 complex with skeletal myosin subfragment 1
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
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 MgCl2.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591102
04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, chicken intestinal myosin I polymerized actin from the actin:thymosin beta‑4 complex in the presence of 1 mM MgCl2.
In plain wordsIn lab tests, chicken intestinal myosin I made actin form filaments from the actin:thymosin beta‑4 complex.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin polymerization from actin:Tb4 complex with intestinal myosin I
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
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 MgCl2.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591103
05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, phalloidin-induced polymerization of skeletal muscle actin from the thymosin beta‑4 complex was accompanied by hydrolysis of actin-bound ATP to ADP.
In plain wordsIn lab tests, phalloidin-induced actin polymerization from the thymosin beta‑4 complex came with breakdown of actin-bound ATP to ADP.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseATP hydrolysis during phalloidin-induced polymerization
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Polymerization of skeletal muscle actin from the complex with thymosin beta 4 by phalloidin is accompanied by the hydrolysis of the actin-bound ATP to ADP.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591104
06LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, sonicated F-actin with many free filament ends induced polymerization from the actin:thymosin beta‑4 complex.
In plain wordsIn lab tests, broken-up actin filaments with many free ends made actin polymerize from the thymosin beta‑4 complex.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin polymerization from actin:Tb4 complex with sonicated F-actin
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Polymerization was also induced by sonicated F-actin which possessed a high concentration of free filament ends.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591105
07LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, gelsolin-severed F-actin with free, slowly growing ends could not induce polymerization of actin from the thymosin beta‑4 complex.
In plain wordsIn lab tests, actin filaments with free slowly growing ends did not start actin polymerization from the thymosin beta‑4 complex.
Peptide
Thymosin beta-4 (human)
Outcome
No significant changeActin polymerization from actin:Tb4 complex with free slowly growing filament ends
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
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 beta 4 complex.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591106
08LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, gelsolin alone or with two actin molecules promoted actin repolymerization from actin:thymosin beta‑4 when its concentration was close to the Kd of actin:thymosin beta‑4.
In plain wordsIn lab tests, gelsolin made actin polymerize from the thymosin beta‑4 complex, but only at a concentration near the complex's Kd.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin repolymerization from actin:Tb4 complex with gelsolin
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
However, when gelsolin on its own or in complex with two actin molecules was added to actin:thymosin beta 4 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 beta 4.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591107
09LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, the source of actin did not change polymerization from the thymosin beta‑4 complex: rabbit skeletal muscle and porcine brain actin polymerized with equal efficiency.
In plain wordsIn lab tests, rabbit muscle actin and pig brain actin both formed filaments from the thymosin beta‑4 complex equally well.
Peptide
Thymosin beta-4 (human)
Outcome
No significant changeEffect of actin source on polymerization from Tb4 complex
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
The source of actin did not influence its polymerization from the thymosin beta 4 complex; rabbit skeletal muscle actin and porcine brain actin were polymerized with equal efficiency from their complexes with thymosin beta 4 by both phalloidin and myosin subfragment 1.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591109
10LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Mechanism
In a cell-free system, skeletal muscle actin, but not cytoplasmic actin, also polymerized from the thymosin beta‑4 complex when CaCl2 was raised above 1 mM.
In plain wordsIn lab tests, muscle actin, but not cytoplasmic actin, also formed filaments from the thymosin beta‑4 complex at higher calcium levels.
Peptide
Thymosin beta-4 (human)
Outcome
IncreaseActin polymerization from Tb4 complex with CaCl2 above 1 mM
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
Skeletal muscle, but not cytoplasmic actin, was found to be also polymerized in the presence of increased CaCl2 concentrations to values above 1 mM.
1 context sentence(design, population, supporting numbers)
Title · context
Induction of the polymerization of actin from the actin:thymosin beta 4 complex by phalloidin, skeletal myosin subfragment 1, chicken intestinal myosin I and free ends of filamentous actin.
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-0805591110

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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