Key findings
- In rat tendon explants and cultured tendon fibroblasts, outgrowth, migration, spreading and survival under hydrogen peroxide stress rose, while proliferation measured by MTT in the same work did not change. [1]
- Growth hormone receptor was one of the most abundantly up-regulated genes in exposed tendon fibroblasts, and proliferation of those cells rose only once growth hormone was added alongside the peptide. [2]
- In human vascular endothelial culture, VEGFR2 messenger RNA and protein rose while VEGF-A did not, receptor internalization increased, and both the signalling change and the tube formation increase were suppressed by the endocytosis inhibitor dynasore. [3][4]
- Mass spectrometry of material taken from confiscated vials assigned the sequence GEPPPGKPADDAGLV, and separate labelled incubation work mapped the metabolites that form in vitro. [5][6]
Identity and structure
- Sequence
- Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, written GEPPPGKPADDAGLV in the cited analytical work [5][7]
- Nominal molecular mass
- 1419, as stated for the pentadecapeptide in the cited tendon transection paper [7]
- Origin
- Described as a partial sequence of a body protection compound isolated from human gastric juice [1][5]
- Form as supplied
- Sterile lyophilized powder
Mechanism as studied
In tendon fibroblast culture the authors tie migration and spreading to the FAK and paxillin pathway. Phosphorylation of both proteins rose with peptide concentration while their total amounts were unchanged, and F-actin formation was induced in the same cells. The paper separates this from proliferation, which its MTT assay did not move. [1]
Two endothelial papers describe different routes to the same tube formation endpoint. One reports raised VEGFR2 expression with receptor internalization and VEGFR2-Akt-eNOS activation, both lost when endocytosis was inhibited. The other attributes the culture changes to ERK1/2 phosphorylation with its c-Fos, c-Jun and Egr-1 targets, alongside raised VEGF-a expression. [3][4]
More recent work places an intracellular interaction upstream of the vascular readouts: the peptide engaged the E3 ubiquitin ligase adaptor FBXO22 through its proline at position 3, which suppressed ubiquitination of the transcription factor BACH1 and let BACH1 protein accumulate. A separate line reports raised growth hormone receptor expression that only translated into proliferation when growth hormone was supplied with it. [8][2]
Research findings
Ex vivo
- System
- Rat Achilles tendon explants and tendon fibroblasts isolated from rat Achilles tendon
- Measured
- Outgrowth from explants, proliferation by MTT assay, survival under hydrogen peroxide stress, migration in a transwell filter assay, spreading on culture dishes, F-actin by FITC-phalloidin staining, and FAK and paxillin phosphorylation by Western blot
- Reported
- Outgrowth from explants accelerated, survival under hydrogen peroxide stress rose, and migration and spreading rose with increasing peptide concentration. Proliferation of the cultured fibroblasts was not directly affected in the MTT assay. F-actin formation was induced, and phosphorylation of FAK and paxillin rose while the total amounts of both proteins were unaltered. [1]
In vitro
- System
- Tendon fibroblasts isolated from the Achilles tendon of male Sprague-Dawley rats
- Measured
- Gene expression by cDNA microarray, growth hormone receptor messenger RNA and protein by RT real time PCR and Western blot, proliferation by MTT with PCNA expression, and Janus kinase 2 activation
- Reported
- Growth hormone receptor was among the most abundantly up-regulated genes and rose at both the messenger RNA and the protein level with peptide concentration and over time. Proliferation and PCNA expression rose when growth hormone was added to the exposed fibroblasts, and Janus kinase 2 was activated over time under that combination. [2]
In vitro
- System
- Human vascular endothelial cells in culture
- Measured
- Endothelial tube formation, VEGFR2 and VEGF-A messenger RNA and protein, VEGFR2 internalization with and without the endocytosis inhibitor dynasore, and VEGFR2-Akt-eNOS signalling over time
- Reported
- Tube formation rose in the endothelial cultures. VEGFR2 messenger RNA and protein rose while VEGF-A did not, receptor internalization increased, and both the signalling activation and the tube formation increase were suppressed in the presence of dynasore. [3]
In vitro
- System
- Human umbilical vein endothelial cells in culture
- Measured
- Proliferation by MTT and cell cycle analysis, migration in transwell and scratch assays, vascular tube formation, VEGF-a expression, and phosphorylation of ERK1/2 with its c-Fos, c-Jun and Egr-1 targets
- Reported
- Proliferation, migration and tube formation all rose in the endothelial cultures and VEGF-a expression was up-regulated. The authors linked those changes to the phosphorylation level of ERK1/2 and of its downstream c-Fos, c-Jun and Egr-1 targets. [4]
In vitro
- System
- Vascular endothelial cells, studied with a combination of molecular, biochemical and cellular approaches
- Measured
- Interaction between the peptide and the E3 ubiquitin ligase adaptor FBXO22, ubiquitination status of the transcription factor BACH1, BACH1 protein levels, endothelial proliferation and tube forming capacity, and experimental validation of the specific role of the proline residue at position 3
- Reported
- The peptide engaged FBXO22 through its proline residue at position 3. Ubiquitination and subsequent proteasomal degradation of BACH1 were suppressed, BACH1 protein accumulated, and the proliferation and tube forming capacity of the endothelial cells rose. [8]
Analytical
- System
- Peptide isolated from confiscated vials, studied alongside a mechano-growth factor variant, with plasma and urine in-vitro metabolism experiments
- Measured
- Amino acid sequence of the vial content, stability and metabolite formation in plasma, stability in urine, and validation of a weak cation exchange solid phase extraction method for urine
- Reported
- The vial content carried the amino acid sequence GEPPPGKPADDAGLV. The peptide formed a stable metabolite in the plasma incubations and was stable in urine for at least four days, and the method reached a detection limit of 0.1 ng/mL with precision under 20 percent and linearity of 0.998. [5]
Analytical
- System
- 13C and 15N labelled peptide incubated in two in-vitro incubation models, with a method then applied to human urine samples
- Measured
- Isotope pair picking by ultra high performance liquid chromatography with high resolution mass spectrometry, the metabolites produced, and the detection limits and linearity of the resulting method
- Reported
- One metabolite from a previously unreported pathway and eight from the conventional amide bond breaking pathway were found across the two incubation models. The resulting detection method reached limits of 0.01 to 0.11 ng/mL with linearity above 0.999. [6]
In vitro
- System
- Cultured tendocytes exposed to 4-hydroxynonenal
- Measured
- Growth of cultured tendocytes with the peptide alone, with 4-hydroxynonenal, and with the two added in either order, under serum containing and serum deprived conditions
- Reported
- The peptide on its own had no effect on the growth of the cultured cells. Combined with 4-hydroxynonenal it reversed that aldehyde's growth inhibiting effect into growth stimulation, and added after the aldehyde it abolished the inhibiting activity, in both serum conditions. [7]
Handling for in-vitro work
- Solvent in cited work
- Dissolved in saline with no carrier added in the cited tendon transection work [7]
- Stability reported in analytical work
- Stable in urine for at least four days in the cited detection method [5]
- Storage
- Lyophilized at -20 °C, dark and dry; reconstituted aliquots kept cold and used promptly
Open questions
- The cited work identifies no receptor for the peptide; the FBXO22 interaction is the closest binding partner reported and has not been reproduced elsewhere in the cited set.
- Migration, survival and proliferation moved differently in the same tendon fibroblast assays, so a result for one endpoint cannot be read as a result for the others.
- The endothelial papers propose VEGFR2 internalization and ERK1/2 signalling as separate routes to the same tube formation endpoint, and the cited work does not reconcile them.
- Analytical identity in the cited work comes from confiscated vials rather than from a characterised reference standard, so a supplied lot still needs its own sequence confirmation.
A clinical literature on this sequence exists and concerns finished formulations; it is out of scope for a research material profile.
Lot records
Check the record for the exact material you order. A published paper and a batch certificate answer different questions.
- RV-24-0001-3 ↗BPC-157 · 99.40% HPLC2026-09-22
- RV-24-0001-2 ↗BPC-157 · 99.40% HPLC2026-09-16
- RV-24-0001-1 ↗BPC-157 · 99.40% HPLC2026-09-16
References
- Chang CH, Tsai WC, Lin MS, et al. The promoting effect of pentadecapeptide BPC 157 on tendon healing involves tendon outgrowth, cell survival, and cell migration. Journal of applied physiology (Bethesda, Md. : 1985). 2011.
- Chang CH, Tsai WC, Hsu YH, et al. Pentadecapeptide BPC 157 enhances the growth hormone receptor expression in tendon fibroblasts. Molecules (Basel, Switzerland). 2014.
- Hsieh MJ, Liu HT, Wang CN, et al. Therapeutic potential of pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation. Journal of molecular medicine (Berlin, Germany). 2017.
- Huang T, Zhang K, Sun L, et al. Body protective compound-157 enhances alkali-burn wound healing in vivo and promotes proliferation, migration, and angiogenesis in vitro. Drug design, development and therapy. 2015.
- Cox HD, Miller GD, Eichner D Detection and in vitro metabolism of the confiscated peptides BPC 157 and MGF R23H. Drug testing and analysis. 2017.
- Tian T, Jing J, Li Y, et al. Stable Isotope Labeling-Based Nontargeted Strategy for Characterization of the In Vitro Metabolic Profile of a Novel Doping BPC-157 in Doping Control by UHPLC-HRMS. Molecules (Basel, Switzerland). 2023.
- Staresinic M, Sebecic B, Patrlj L, et al. Gastric pentadecapeptide BPC 157 accelerates healing of transected rat Achilles tendon and in vitro stimulates tendocytes growth. Journal of orthopaedic research : official publication of the Orthopaedic Research Society. 2003.
- Zhang J, Liu M, Ou H, et al. BPC157 drives angiogenesis through FBXO22-dependent stabilization of BACH1. Cell communication and signaling : CCS. 2026.
Publication records fetched from PubMed on 2026-09-20. Profile text reviewed 2026-09-20.