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Study · In vitro (cells) · rat · 1992

3 results

[Thymosin alpha(1)--an endogenous modulator of alpha-thrombin recognition site].

Dugina TN, Strukova SM, Khlgatian SV, Ashmarin IP

Biulleten' eksperimental'noi biologii i meditsiny1 Sept 1992

PMID1477349 (opens in a new tab)PepBankPUB-01477349

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 study3

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

  1. 01LabIn vitro (cells)Mechanism

    In rat peritoneal mast cells, thymosin suppressed the thrombin-induced rise of intracellular pH above the resting level.

    In plain wordsIn rat cells, thymosin blocked the rise in cell pH that thrombin normally caused.

    Outcome
    DecreaseThrombin-induced intracellular pH increase
    Study

    ratn: not reported in source

    rat peritoneal mast cells
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thymosin suppressed thrombin-induced pHi increase above resting level.
    1 context sentence
    Summary · context
    Thrombin-induced pHi changes of RPMC were controlled with pH-sensitive fluorescent dye, BCECF.
  2. 02LabIn vitro (cell-free)Activity measurement

    Thymosin alpha‑1 inhibited the fibrinogen clotting activity of alpha-thrombin.

    In plain wordsIn lab tests, thymosin alpha‑1 reduced the ability of thrombin to clot fibrinogen.

    Outcome
    DecreaseFibrinogen clotting activity of alpha-thrombin
    Study

    n: not reported in source

    alpha-thrombin and fibrinogen
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thymosin alpha 1-inhibited fibrinogen clotting activity of alpha-thrombin, but not amidolysis of H-D-Phe-Pip-Arg-pNA.
  3. 03LabIn vitro (cell-free)Activity measurement

    Thymosin alpha‑1 did not inhibit the amidolysis of H-D-Phe-Pip-Arg-pNA by alpha-thrombin.

    In plain wordsIn lab tests, thymosin alpha‑1 did not block thrombin's action on a small test substrate.

    Outcome
    No significant changeAmidolysis of H-D-Phe-Pip-Arg-pNA by alpha-thrombin
    Study

    n: not reported in source

    alpha-thrombin and chromogenic substrate
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thymosin alpha 1-inhibited fibrinogen clotting activity of alpha-thrombin, but not amidolysis of H-D-Phe-Pip-Arg-pNA.

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 3Current

    12 Oct 2026, 17:28 UTC

    Study results updated

  2. Version 2

    9 Oct 2026, 03:03 UTC

    Study data updated · source update from Europe PMC

  3. Version 1

    9 Oct 2026, 03:02 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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