Description

Bronchogen Peptide

 

CAS Number	N/A
Other Names	Ala-Glu-Asp-Leu (AEDL)
IUPAC Name	N/A
Molecular Formula	C₁₈H₃₀N₄O₉
Molecular Weight	446.45
Purity	≥99% Pure (LC-MS)
Liquid Availability	N/A
Powder Availability	10 milligrams vial (lyophilized/freeze-dried)
Storage Condition	Store cold, keep refrigerated. Do NOT freeze.
Terms	All products are for laboratory developmental research USE ONLY. Products are not for human consumption.

**Important Information: Each peptide comes lyophilized/freeze-dried and must be reconstituted with Bacteriostatic Water in order to be dispensable in liquid form.

Watch How To Reconstitute Peptide Video Here

 

What is Bronchogen?

Bronchogen is a tetrapeptide supplement designed to support respiratory health by promoting lung function and tissue regeneration. As a bioactive peptide, Bronchogen is believed to aid in repairing damaged lung tissue, reducing inflammation, and enhancing overall pulmonary resilience. It is often considered for individuals with respiratory conditions such as chronic obstructive pulmonary disease (COPD), asthma, or lung fibrosis. Current research shows that by targeting cellular repair mechanisms, Bronchogen may help improve breathing efficiency and support recovery from environmental stressors, infections, or chronic lung disorders

 

Main Research Findings

1) Administration of Bronchogen has the potential to reduce symptoms associated with remodeling of lung tissue and bronchial epithelium in cases of COPD.

2) Following administration of Bronchogen, there were notable changes in the expression of age-related differentiation factors CXCL12, Hoxa3, and WEGC1 in the bronchial epithelium.

 

Selected Data
1) The research team of Kuzabova et al examined the effects of Bronchogen on tissue remodeling in the bronchial epithelium. The study was conducted on male Wistar rats weighing between 150-170 grams, obtained from the Rappolovo nursery under the Russian Academy of Medical Sciences. The primary objective of the study was to develop a model of chronic obstructive pulmonary disease (COPD) and evaluate the effects of Bronchogen, a tetrapeptide derived from bronchial mucosa polypeptides, on disease progression [1].

To simulate the gradual onset of COPD, the researchers exposed the rats to nitrogen dioxide inhalation, which mimics both acute and chronic damage to the respiratory system. The exposure process took place in a specialized chamber connected to a laboratory NO₂ generator. The gas was produced through the reaction of sodium nitrite with sulfuric acid, yielding a mixture of nitrogen oxides. When exposed to atmospheric oxygen, the colorless nitric oxide (NO) converts into the more stable yellow-brown NO₂. The concentration of NO₂ in the chamber was maintained at 30-40 mg/m³ and was measured using a colorimetric method. The rats underwent 60 days of exposure, with three 30-minute inhalation sessions per day, each separated by a 30-minute interval.

Following the initial 60-day exposure period, the animals were randomly assigned into two groups. Group 1, consisted of 13 rats that received Bronchogen for 30 days in a dosage equivalent to the daily human recommendation, recalculated for rats. The supplement was administered as a suspension through a gastric tube. Group 2, composed of nine rats, served as the control group and was given 0.9% sodium chloride (NaCl) through the same administration route. Additionally, an intact group of nine rats, which had not been exposed to NO₂, was maintained for comparison. After the 30-day experimental period, the animals were euthanized using CO₂ inhalation.

To evaluate the effects of Bronchogen on lung health, bronchoalveolar lavage was performed by flushing isolated lungs with sterile physiological saline at 35-37°C. The collected lavage fluid was centrifuged, and both total and differential cell counts were measured. For histological analysis, the lungs were fixed using a 10% formaldehyde solution infused through the trachea. The fixed lung specimens were embedded in paraffin, sectioned into 5-7 micrometer-thick slices, and stained using hematoxylin and eosin, van Gieson staining, and periodic acid-Schiff staining to visualize goblet cells [1].
Morphometric analysis was carried out using the VideoTest-Morfologiya 5.2 hardware-software complex. The analysis included measurements of key structural components of the bronchial system, such as bronchial area, cell infiltration, bronchial lumen, alveolar structure, thickness of interalveolar septa, and the total area of the mucosa, muscle layer, and connective tissue in the bronchial wall. These measurements provided insights into the extent of lung damage and the potential protective effects of Bronchogen [1].

Additionally, key inflammatory markers in the bronchoalveolar lavage fluid were assessed using enzyme-linked immunosorbent assay. The biomarkers included tumor necrosis factor-alpha, interleukin-8, neutrophil elastase, and secretory immunoglobulin A. These markers were selected to evaluate the inflammatory response and immune modulation in the lungs following NO₂ exposure and Bronchogen treatment.

The collected data was processed using statistical software programs. The primary software used for general data analysis was Statistica 6.0, and statistical significance was determined using Student’s t-test. Morphometric data, which involved comparisons across multiple groups, were analyzed using the Kruskal-Wallis test in SPSS 15.0 software. These statistical methods ensured the reliability of the study’s findings and allowed for meaningful comparisons between the experimental groups.

Overall, this study provided a structured approach to investigating the impact of Bronchogen on a NO₂-induced COPD model in rats. By combining histological, biochemical, and statistical analyses, the research aimed to assess whether Bronchogen could mitigate lung damage, reduce inflammation, and improve respiratory function in rats with chemically induced COPD [1].

2) The research team of Khavinson et al examined the effects of Pancragen, Vesugen, and Bronchogen on transcription factors WEDC1, Hoxa3, and CXCL12 in lung and pancreatic cells as well as fibroblasts. The experiments were conducted on embryonic cultures of pancreatic acinar cells and bronchial epithelial cells, sourced from the Institute of Cytology at the Russian Academy of Sciences and the Research Institute of Influenza, respectively. The study also involved human prostate fibroblast cultures obtained from Cambrex Bioscience. Cell cultures were categorized into three groups based on passage number: young (passage 1), mature (passage 7), and aged (passage 14), in accordance with the recommendations of the International Association of Cell Culture Studies [2].

Each cell culture was exposed to a specific peptide supplement to assess their effects on transcription factor expression. Bronchial epithelial cells were treated with Bronchogen, acinar pancreatic cells with Pancragen, and fibroblast cultures with Vesugen. Control cultures were treated with physiological saline. Preliminary experiments determined that non-specific peptides (e.g., Bronchogen for pancreatic cells or Pancragen for bronchial epithelial cells) did not influence transcription factor expression. This confirmed the tissue-specific activity of each peptide supplement.

The pancreatic acinar cells were cultured in 25 cm² flasks containing Dulbecco’s Modified Eagle’s Medium supplemented with L-glutamine, 15% fetal calf serum, and 1% penicillin-streptomycin. The bronchial epithelial cells were grown in Minimum Essential Medium with similar supplements, except with 10% fetal calf serum instead of 15%. Fibroblast cultures were maintained in 24-well plates at 37°C and 5% CO₂ using RPMI-1640 medium. These controlled environments ensured optimal growth and differentiation of each cell type, allowing the researchers to accurately assess the effects of peptide treatment [2].

To evaluate the impact of peptides on transcription factor expression, immunocytochemical analysis was performed using a computer-assisted microscopic image analysis system. This system included a Nikon Eclipse E400 microscope, a Nikon DXM1200 digital camera, and Videotest-Morphology 5.0 software. At least five fields of view were analyzed at ×200 magnification in each experiment. The expression area was calculated as the ratio of immunopositive cells to the total cell area, expressed as a percentage. This parameter served as a measure of the intensity of transcription factor synthesis in the cultured cells [2].

Additionally, immunofluorescent confocal microscopy was conducted on non-fixed cell suspensions to visualize the expression of specific signaling molecules. Primary antibodies targeting CXCL12 and WEDC1 proteins were applied to the cells, with visualization achieved using Vector Red kits for immunofluorescent labeling of alkaline phosphatase. To prevent interference from endogenous enzyme activity, levamisole at 1.25 mM was included in the incubation step. The labeled preparations were examined using a Leica TCS SP5 confocal microscope at ×400 and ×1000 magnification. A Bio-Rad MRC-1024 system with LaserSharp 5.0 software was used for confocal image analysis. In each case, at least ten fields of view were analyzed at ×400 magnification to assess the extent of protein expression.
For statistical analysis, the data were processed using Statistica 7.0 software to evaluate differences between groups. This allowed researchers to determine the significance of peptide-induced changes in transcription factor expression and cellular function. The findings from these experiments provided insight into the tissue-specific effects of Bronchogen, Pancragen, and Vesugen, as well as their potential roles in modulating transcription factor activity and cellular regeneration. Overall, this study demonstrated the specificity and effectiveness of peptide supplements in influencing cellular function. By targeting transcription factor expression in different cell types, the peptides may have therapeutic potential in tissue regeneration and disease treatment [2].

Discussion
1) The results of the study conducted by Kuzabova et al revealed that morphological analysis of the bronchial epithelium in control rats exposed to nitrogen dioxide revealed structural changes typical of chronic obstructive pulmonary disease (COPD). These included goblet cell hyperplasia, an increased number of epithelial cell layers, focal epithelial degeneration, atrophy, and squamous cell metaplasia. In the control group, the ratio of ciliated to goblet cells was significantly altered compared to intact rats, indicating a loss of normal bronchial epithelial composition [1].
Additionally, significant lymphocytic infiltration, with the formation of lymphoid follicles, was observed in the lamina propria and around the bronchi. Other structural changes included widened respiratory bronchioles and alveolar ducts, along with the presence of emphysematous lesions in subpleural compartments. Morphometric analysis demonstrated thickening of the interalveolar septa and bronchial muscle layer, along with a twofold increase in the area occupied by cellular infiltration. The alveolar lumens also exhibited a tendency to increase, further reflecting the pathological changes characteristic of COPD.

In comparison, rats treated with Bronchogen showed markedly reduced bronchial epithelium hyperplasia. The ciliated-to-goblet cell ratio improved, with no more than one to two goblet cells for every five ciliated cells, indicating a restoration of epithelial integrity. Notably, signs of epithelial atrophy and squamous metaplasia, as well as emphysema, were absent in the Bronchogen-treated group. While mild lymphocytic infiltration persisted around the large bronchi, there was no evidence of lymphoid follicle formation. Morphometric parameters in the Bronchogen-treated rats closely resembled those of the intact control group, suggesting that the peptide supplement played a role in reversing NO₂-induced lung damage [1].

A key pathological feature of COPD is the persistence of inflammation even after exposure to harmful agents, such as smoking or environmental pollutants, has ceased. In the control group, inflammatory markers remained elevated one month after the initial COPD induction. The concentration of neutrophils in the bronchoalveolar lavage fluid was five times higher than in intact rats measuring at 25.9% and 5.2%, respectively, while lymphocyte levels were twice as high at 18.5% and 9.1%, respectively. The levels of proinflammatory cytokines, tumor necrosis factor-alpha, and interleukin-8, which are primarily produced by alveolar macrophages, remained significantly elevated. Macrophages constituted over 53% of the total bronchoalveolar lavage fluid cells in the control group, indicating an ongoing immune response.

One of the primary mediators of lung damage in COPD is neutrophilic elastase, an enzyme released by activated neutrophils in response to TNF-alpha and IL-8. In the control rats, the concentration of neutrophilic elastase in bronchoalveolar lavage fluid was twice as high as in intact rats. Excess elastase activity leads to the degradation of elastin, a key structural protein in the lung’s extracellular matrix, contributing to emphysema formation. Additionally, neutrophilic elastase degrades surfactant protein A, which plays a role in local immune defense. A major consequence of chronic inflammation in COPD is the impairment of bronchial immune function. A key marker of local immunity, secretory immunoglobulin A, was significantly reduced in the control group. Goblet cell hyperplasia, which is linked to severe damage to ciliary cells, was associated with a significant loss of secretory immunoglobulin A on the epithelial surface, further compromising the lung’s defense against pathogens and irritants [1].

Treatment with Bronchogen led to substantial improvements in the inflammatory and immune profiles of bronchoalveolar lavage fluid. The percentage of neutrophils decreased significantly compared to the control group measuring at 9.0% and 25.9%, respectively, while macrophage levels increased to 76.5%. The concentration of TNF-alpha, IL-8, and neutrophilic elastase in bronchoalveolar lavage fluid decreased to levels similar to those of intact rats. Moreover, the synthesis of secretory immunoglobulin A significantly increased, surpassing the levels observed in both the control and intact groups. These findings indicate that Bronchogen not only suppressed inflammation but also enhanced the lung’s immune defenses [1].

Further investigations using bronchial mucosa tissue cultures demonstrated that Bronchogen stimulated the proliferation and functional activity of bronchial epithelial cells. It inhibited spontaneous cell death and promoted cellular regeneration and adaptation. The effects of short peptides like Bronchogen are believed to be mediated through direct interactions with DNA, modulating the activity of transcription factors involved in cell repair and regeneration. By reprogramming cellular signaling pathways, these peptides appear to enhance the regenerative potential of resident stem cells within the bronchial tree, including Clara cells, basal cells, and type 2 alveolar cells.

The beneficial effects of Bronchogen treatment were reflected in the restoration of bronchial epithelial structure and function. The peptide therapy reversed the major COPD-associated changes, including goblet cell hyperplasia, squamous metaplasia, and lymphocytic infiltration, while also preventing emphysema formation. Importantly, the structural recovery was accompanied by functional improvements, as indicated by increased sIgA levels and normalization of immune responses in bronchoalveolar lavage fluid. By reducing neutrophilic inflammation and restoring immune balance, Bronchogen demonstrated potential as a therapeutic agent for mitigating lung damage in COPD [1].

These findings suggest that short peptides can serve as regulators of resident stem cells in the lungs, promoting the reparative regeneration of bronchial epithelium and preventing pathological remodeling associated with COPD. The ability of Bronchogen to restore epithelial integrity, suppress inflammation, and enhance immune function makes it a promising candidate for future therapeutic applications in chronic lung diseases [1].

2) As it was previously mentioned, the research team of Khavinson et al conducted a study in order to investigate the expression of key differentiation markers, including CXCL12, Hoxa3, and WEDC1, in pancreatic acinar cells, bronchial epithelial cells, and prostate fibroblast cultures at different stages of aging. Control cultures were analyzed to determine baseline expression levels, and the effects of tissue-specific peptides, Pancragen, Bronchogen, and Vesugen, were examined to assess their potential role in promoting cellular differentiation and functional activity [2].

The results of the study revealed that aging was associated with a significant decline in the expression of differentiation markers across all cell types. In pancreatic acinar cells, the expression of Hoxa3 decreased notably with age, with young cultures showing 1.2- to 2-fold higher expression than mature and aged cultures. Similarly, the area of CXCL12 expression declined by 22% in mature cultures and 12% in aged cultures. In fibroblast cultures, the expression of WEDC1 was particularly affected, with a 60% reduction at passage 4 and an 81% reduction at passage 7 compared to passage 1. These declines indicate a reduced differentiation capacity of cells as they age, which is likely linked to the gradual loss of functional activity in the pancreas, bronchi, and prostate over time.

The addition of Pancragen to pancreatic acinar cell cultures had a significant effect on marker expression. CXCL12 expression decreased by 21% in young cultures and by 86% and 72% in mature and aged cultures, respectively. However, Pancragen strongly stimulated Hoxa3 expression, with increases of 60% in young cultures and 90% in mature cultures. The most pronounced response was observed in aged cultures, where Hoxa3 expression increased by 2.8 times compared to control levels. This suggests that Pancragen may play a crucial role in restoring differentiation potential in aging pancreatic cells by upregulating transcription factors associated with cellular renewal [2].

Vesugen, which was tested on fibroblast cultures, had a substantial impact on the expression of differentiation markers CXCL12 and WEDC1. In young cultures, CXCL12 expression increased by 1.2 times, and WEDC1 expression rose by 1.5 times. In mature cultures, both markers were significantly upregulated, with increases of 8 times for CXCL12 and 8.2 times for WEDC1. The most dramatic effect was seen in aged fibroblast cultures, where CXCL12 expression increased 7.6 times and WEDC1 expression rose 16 times compared to control levels. These findings indicate that Vesugen plays a powerful role in stimulating differentiation in aging fibroblast cells, which could have implications for maintaining prostate function and possibly delaying age-related degenerative changes.

Finally, Bronchogen treatment of bronchial epithelial cells also enhanced differentiation, particularly in terms of Hoxa3 expression. The marker’s expression increased by 1.7 times in young cultures, 1.4 times in mature cultures, and 1.7 times in aged cultures. Interestingly, unlike Pancragen’s effect on pancreatic cells, Bronchogen did not alter CXCL12 expression in bronchial epithelial cells at any stage of aging. This specificity suggests that different peptides may exert their effects through distinct molecular pathways, targeting particular differentiation factors relevant to each tissue type [2].

Overall, the study confirmed that aging is associated with a natural decline in the expression of differentiation factors, leading to reduced cellular renewal and function in the pancreas, bronchi, and prostate. However, the administration of short peptides such as Pancragen, Vesugen, and Bronchogen, was able to counteract this decline by significantly enhancing the expression of differentiation markers. These results support previous findings that peptides can stimulate glandular and endothelial tissues, thereby promoting cellular differentiation and functional maintenance [2].

The proposed mechanism behind this peptide-induced differentiation enhancement is likely epigenetic. Since differentiation factors such as CXCL12, Hoxa3, and WEDC1 play a role in transcription, it is hypothesized that short peptides interact with regulatory pathways at the genetic level to modify transcriptional activity. This suggests that peptide therapy could be a potential strategy for modulating aging processes by stimulating epigenetic pathways that promote cell differentiation and regeneration. These findings highlight the potential for peptide-based interventions in age-related degenerative diseases affecting the pancreas, bronchi, and prostate for the maintenance of organ function and delayed onset of age-related decline [2].

Disclaimer

**LAB USE ONLY**
*This information is for educational purposes only and does not constitute medical advice. THE PRODUCTS DESCRIBED HEREIN ARE FOR RESEARCH USE ONLY. All clinical research must be conducted with oversight from the appropriate Institutional Review Board (IRB). All preclinical research must be conducted with oversight from the appropriate Institutional Animal Care and Use Committee (IACUC) following the guidelines of the Animal Welfare Act (AWA).

 

Citations

[1] Kuzubova NA, Lebedeva ES, Dvorakovskaya IV, Surkova EA, Platonova IS, Titova ON. Modulating Effect of Peptide Therapy on the Morphofunctional State of Bronchial Epithelium in Rats with Obstructive Lung Pathology. Bull Exp Biol Med. 2015 Sep;159(5):685-8. doi: 10.1007/s10517-015-3047-x. Epub 2015 Oct 15. PMID: 26468022.

[2] Khavinson VKh, Linkova NS, Polyakova VO, Kheifets OV, Tarnovskaya SI, Kvetnoy IM. Peptides tissue-specifically stimulate cell differentiation during their aging. Bull Exp Biol Med. 2012 May;153(1):148-51. doi: 10.1007/s10517-012-1664-1. PMID: 22808515.

 

 

PEPTIDES PREFER THE COLD
Keep peptide vials refrigerated at all times to reduce peptide bond breakdown. DO NOT FREEZE. Most peptides, especially shorter ones, can be preserved for weeks if careful.
Always swab the top of the vial with an alcohol wipe, rubbing alcohol or 95% ethanol before use.
Before drawing solution from any dissolved peptide vial, fill the pin with air to the same measurement you will be filling with solution, ie. if you plan to take 0.1 ml, first fill the pin with 0.1ml of air, push the air into the vial, and then draw the peptide back up to the 0.1 ml marker. Doing so will maintain even pressure in the vial. Always remember to remove air bubbles from the pin by flicking it gently, pin side up, and pushing bubbles out. In addition, push out a tiny amount of solution to ensure there is no air left in the metal tip.

ONLY MIX WITH STERILE BACTERIOSTATIC WATER
The purity and sterility of bacteriostatic water are essential to prevent contamination and to preserve the shelf-life of dissolved peptides.
Push the pin through the rubber stopper at a slight angle, so that you inject the bacteriostatic water toward the inside wall of the vial, not directly onto the powder.
Lyophilized peptide should be stored at -20°C (freezer), and the reconstituted peptide solution at 4°C (refrigerated). Do not freeze once reconstituted.
NEVER SHAKE A VIAL TO MIX.

Air bubbles are unfavorable to the stability of proteins.

Bronchogen is sold for laboratory research use only. Terms of sale apply. Not for human consumption, nor medical, veterinary, or household uses. Please familiarize yourself with our Terms & Conditions prior to ordering.

 

 

 

 

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