Skip to content

Study · In vitro (cells) · 2026

5 results

BPC157 drives angiogenesis through FBXO22-dependent stabilization of BACH1.

Zhang J, Liu M, Ou H, Wang Z, He L, Xiao Y, Xie F, Yu D, Cao H, He W, Wang S, Zhang W and 4 more

Show all authors

Zhang K, Zhang Y, Li M, Hao Q

Cell communication and signaling : CCS29 Jan 2026Cited by 1 (Europe PMC)

PMID41606641 (opens in a new tab)PMCIDPMC12947506 (opens in a new tab)DOI10.1186/s12964-026-02694-6 (opens in a new tab)PepBankPUB-41606641
Read at sourcePubMedAsk about this study
Jump to 5 results

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: CC BY-NC-ND. Results still quote short attributed sentences.

Results from this study5

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

  1. 01LabIn vitro (cells)Mechanism

    In cells, intracellular BPC157 engaged the E3 ubiquitin ligase adaptor FBXO22 through its proline residue at position 3.

    In plain wordsIn cells, BPC157 attached to a protein called FBXO22 through one specific amino acid.

    Peptide
    BPC-157
    Outcome
    Not applicableBinding of BPC157 to FBXO22 through proline at position 3
    Study

    n: not reported in source

    Vascular endothelial cells
    Outcome group
    Angiogenesis · Cardiovascular
    Studied dose
    Dose not stated

    Source sentences

    Summary
    We revealed that intracellular BPC157 engages the E3 ubiquitin ligase adaptor protein FBXO22 through its proline residue at position 3.
    2 context sentences
    Summary · context
    The specific role of the proline residue at position 3 of BPC157 was also experimentally validated.
    Summary · context
    To investigate the molecular pathway underlying the proangiogenic effects of BPC157, we employed a combination of molecular, biochemical, and cellular approaches. These include techniques to identify protein‒protein interactions, assess ubiquitination status, and evaluate key cellular functions.
  2. 02LabIn vitro (cells)Mechanism

    In cells, the BPC157-FBXO22 complex suppressed ubiquitination and proteasomal degradation of BACH1, stabilizing BACH1 protein levels.

    In plain wordsIn cells, BPC157 helped keep the protein BACH1 from being broken down.

    Peptide
    BPC-157
    Outcome
    DecreaseBACH1 ubiquitination and degradation
    Study

    n: not reported in source

    Vascular endothelial cells
    Outcome group
    Angiogenesis · Cardiovascular
    Studied dose
    Dose not stated

    Source sentences

    Summary
    This interaction results in the formation of a protein complex that effectively suppresses the ubiquitination and subsequent proteasomal degradation of the transcription factor BACH1, leading to significant stabilization of BACH1 protein levels.
    1 context sentence
    Summary · context
    To investigate the molecular pathway underlying the proangiogenic effects of BPC157, we employed a combination of molecular, biochemical, and cellular approaches. These include techniques to identify protein‒protein interactions, assess ubiquitination status, and evaluate key cellular functions.
  3. 03LabIn vitro (cells)Mechanism

    In cells, BPC157 led to significant stabilization of BACH1 protein levels.

    In plain wordsIn cells, BPC157 raised levels of the protein BACH1.

    Peptide
    BPC-157
    Outcome
    IncreaseBACH1 protein level
    Study

    n: not reported in source

    Vascular endothelial cells
    Outcome group
    Angiogenesis · Cardiovascular
    Studied dose
    Dose not stated

    Source sentences

    Summary
    leading to significant stabilization of BACH1 protein levels.
    1 context sentence
    Summary · context
    To investigate the molecular pathway underlying the proangiogenic effects of BPC157, we employed a combination of molecular, biochemical, and cellular approaches. These include techniques to identify protein‒protein interactions, assess ubiquitination status, and evaluate key cellular functions.
  4. 04LabIn vitro (cells)Mechanism

    In vascular endothelial cells, BPC157-driven BACH1 accumulation enhanced cell proliferation.

    In plain wordsIn cells, BPC157 led to more growth of blood-vessel lining cells.

    Peptide
    BPC-157
    Outcome
    IncreaseEndothelial cell proliferation
    Study

    n: not reported in source

    Vascular endothelial cells
    Outcome group
    Angiogenesis · Cardiovascular
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The consequent accumulation of BACH1 was shown to enhance critical processes in vascular regeneration, namely, the proliferation
    1 context sentence
    Summary · context
    To investigate the molecular pathway underlying the proangiogenic effects of BPC157, we employed a combination of molecular, biochemical, and cellular approaches. These include techniques to identify protein‒protein interactions, assess ubiquitination status, and evaluate key cellular functions.
  5. 05LabIn vitro (cells)Mechanism

    In vascular endothelial cells, BPC157-driven BACH1 accumulation enhanced tube-forming capacity.

    In plain wordsIn cells, BPC157 improved the ability of blood-vessel lining cells to form tube structures.

    Peptide
    BPC-157
    Outcome
    IncreaseEndothelial tube-forming capacity
    Study

    n: not reported in source

    Vascular endothelial cells
    Outcome group
    Angiogenesis · Cardiovascular
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The consequent accumulation of BACH1 was shown to enhance critical processes in vascular regeneration, namely, the proliferation and tube-forming capacity of vascular endothelial cells.
    1 context sentence
    Summary · context
    To investigate the molecular pathway underlying the proangiogenic effects of BPC157, we employed a combination of molecular, biochemical, and cellular approaches. These include techniques to identify protein‒protein interactions, assess ubiquitination status, and evaluate key cellular functions.

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

    10 Oct 2026, 08:19 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, 02:56 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.