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Study · In vitro (cell-free) · 2004

6 results

Factor XIIIa incorporates thymosin beta4 preferentially into the fibrin(ogen) alphaC-domains.

Makogonenko E, Goldstein AL, Bishop PD, Medved L

Biochemistry1 Aug 2004Cited by 11 (Europe PMC)

Summary

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

Results from this study6

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

  1. 01LabIn vitro (cell-free)Mechanism

    In lab tests, no significant noncovalent interaction between thymosin beta4 and fibrinogen, fibrin or their fragments was detected without activated factor XIII.

    In plain wordsIn lab tests, thymosin beta4 did not bind fibrinogen or fibrin without activated factor XIII.

    Outcome
    No significant changeNoncovalent interaction of thymosin beta4 with fibrin(ogen) without factor XIIIa
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    No significant noncovalent interaction between them was detected in the absence of activated factor XIII
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.
  2. 02LabIn vitro (cell-free)Mechanism

    In lab tests with activated factor XIII, thymosin beta4 was effectively incorporated into fibrin and to a lesser extent into fibrinogen.

    In plain wordsIn lab tests with activated factor XIII, thymosin beta4 was built into fibrin, and less so into fibrinogen.

    Outcome
    Not applicableIncorporation of thymosin beta4 into fibrin and fibrinogen with activated factor XIII
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    while in its presence thymosin beta(4) was effectively incorporated into fibrin and to a lesser extent into fibrinogen.
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.
  3. 03LabIn vitro (cell-free)Mechanism

    In lab tests at physiological concentrations, molar incorporation ratios of thymosin beta4 to fibrinogen and fibrin were 0.2 and 0.4, respectively.

    In plain wordsIn lab tests, thymosin beta4 was built into fibrin at a higher molar ratio than into fibrinogen.

    Outcome
    Not applicableMolar incorporation ratio of thymosin beta4
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Molar incorporation ratio
    0.2 mol/mol
    fibrinogen
    Molar incorporation ratio
    0.4 mol/mol
    fibrin

    Source sentences

    Summary
    The incorporation at physiological concentrations of fibrin(ogen) and factor XIII was significant with molar incorporation ratios of thymosin beta(4) to fibrinogen and fibrin of 0.2 and 0.4, respectively.
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.
  4. 04LabIn vitro (cell-free)Mechanism

    In fibrin, the alphaC-domain was the major site where activated factor XIII incorporated thymosin beta4.

    In plain wordsIn lab tests, thymosin beta4 was mainly built into a part of fibrin called the alphaC-domain.

    Outcome
    Not applicableMajor incorporation site in fibrin
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    in fibrin the latter serves as the major incorporation site.
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.
  5. 05LabIn vitro (cell-free)Mechanism

    The incorporation site was localized to the COOH-terminal portion of the alphaC-domain, including residues 392-610.

    In plain wordsIn lab tests, the site where thymosin beta4 was built in lay in the end part of the alphaC-domain.

    Outcome
    Not applicableLocalization of incorporation site within alphaC-domain
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Measurements

    Residues of incorporation site
    392 to 610 residues
    alphaC-domain

    Source sentences

    Summary
    This site was further localized to the COOH-terminal portion of the alphaC-domain including residues 392-610.
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.
  6. 06LabIn vitro (cell-free)Mechanism

    In lab tests, activated factor XIII incorporated thymosin beta4 into the isolated gamma-module and the alphaC-domain.

    In plain wordsIn lab tests, activated factor XIII built thymosin beta4 into two separate fibrin fragments.

    Outcome
    Not applicableIncorporation of thymosin beta4 into isolated gamma-module and alphaC-domain
    Study

    n: not reported in source

    purified fibrinogen, fibrin and recombinant fragments
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Further experiments revealed that although activated factor XIII incorporates thymosin beta(4) into the isolated gamma-module and alphaC-domain, in fibrin the latter serves as the major incorporation site.
    1 context sentence
    Summary · context
    To clarify the mechanism of this incorporation, we studied the interaction of thymosin beta(4) with fibrinogen, fibrin, and their recombinant fragments, the gamma-module (gamma-chain residues 148-411), and the alphaC-domain (Aalpha-chain residues 221-610) and its truncated variants by immunoblot and ELISA.

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.

  1. Version 2Current

    13 Oct 2026, 01:52 UTC

    Study results updated

  2. 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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