Therapeutic efficacy of Chymotrypsin in acute bovine mastitis

G, Marco Leal

doi:10.21897/rmvz.607

Cited by 2 publications

(2 citation statements)

References 25 publications

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Section: Discussionmentioning

confidence: 99%

“…63 In a study of bovine mastitis, chymotrypsin was considered an effective treatment when combined with beta-lactams as it reduced the production of fibrin and hence allowed more effective distribution of the antibiotic drugs, in addition to its proteolytic activity. 64 In line with its protective effects, rats given α-ch had significantly lowered MDA and NO levels and higher GSH levels and SOD activity compared with the septic rats. Several studies supported the antioxidant effect of α-ch.…”

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confidence: 81%

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Alpha-Chymotrypsin Protects Against Acute Lung, Kidney, and Liver Injuries and Increases Survival in CLP-Induced Sepsis in Rats Through Inhibition of TLR4/NF-κB Pathway

Senousy¹,

Ahmed²,

Abdelhafeez³

et al. 2022

DDDT

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Inflammation and oxidative stress play a major role in the development of sepsis and its associated complications, leading to multiple organ failure and death. The lungs, liver, and kidneys are among the early affected organs correlated with mortality in sepsis. Alpha-chymotrypsin (α-ch) is a serine protease that exerts anti-inflammatory, anti-edematous, and anti-oxidant properties. Purpose This study was undertaken to elucidate if the anti-inflammatory and anti-oxidant effects of α-ch observed in previous studies can alleviate lung, liver, and kidney injuries in a cecal ligation and puncture (CLP)-induced sepsis model, and thus decrease mortality. Materials and Methods Septic animals were given α-ch 2 h post CLP procedure. Sepsis outcomes were assessed in the lungs, liver, and kidneys. Separate animal groups were investigated for a survival study. Results CLP resulted in 0% survival, while α-chymotrypsin post-treatment led to 50% survival at the end of the study. Administration of α-chymotrypsin resulted in a significant attenuation of sepsis-induced elevated malonaldehyde (MDA) and total nitrite/nitrate (NOx) levels. In addition, there was a significant increase in reduced glutathione (GSH) content and superoxide dismutase (SOD) activity in the lungs, liver, and kidneys. Administration of α-ch reduced elevated tissue expression of toll-like receptor-4 (TLR4), nuclear factor kappa-B (NF-κB), myeloperoxidase (MPO), and inducible nitric oxide synthase (iNOS). Alpha-chymotrypsin resulted in a significant reduction in serum levels of tumor necrosis factor-alpha (TNF-α), interleukin-1 beta (IL-1β), and interleukin-6 (IL-6). Alpha-chymotrypsin attenuated the rise in serum creatinine, cystatin C, blood urea nitrogen (BUN), alanine aminotransferase (ALT), and aspartate aminotransferase (AST) levels that was observed in the septic group. In addition, α-ch significantly reduced the lung wet/dry weight ratio, total protein content, and leukocytic counts in bronchoalveolar lavage fluid (BALF). Histopathological examination of the lungs, liver, and kidneys confirmed the protective effects of α-ch on those organs. Conclusion α-ch has protective potential against sepsis through lowering tissue expression of TLR4, NF-κB, MPO, and iNOS leading to decreased oxidative stress and inflammatory signals induced by sepsis. This effect appeared to alleviate the damage to the lungs, liver, and kidneys and increase survival in rats subjected to sepsis.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 81%

Alpha-Chymotrypsin Protects Against Acute Lung, Kidney, and Liver Injuries and Increases Survival in CLP-Induced Sepsis in Rats Through Inhibition of TLR4/NF-κB Pathway

Senousy¹,

Ahmed²,

Abdelhafeez³

et al. 2022

DDDT

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Interactions of Polydopamine Nanoparticles with Serine and Cysteine Proteases: Implications for Enhancing Protein Stabilization and Enzyme Activity

Chahar,

Yadav,

Venkatesu

2024

ACS Appl. Nano Mater.

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The interactions between polydopamine nanoparticles (PDA NPs) with serine protease α-chymotrypsin (α-CT) and cysteine protease stem bromelain (SB) have prompted significant emphasis due to their potential implications in biocatalysis and therapeutic applications. This study addresses the structural integrity, binding kinetics, and catalytic potential of α-CT and SB in the presence of PDA NPs by employing a combination of spectroscopic techniques and thermodynamic and kinetic analyses. The spectroscopic results reveal that PDA NPs bind to both enzymes (α-CT and SB) to create a stable complex without disrupting their active sites. Furthermore, fluorescence, circular dichroism (CD), and dynamic light scattering (DLS) analysis clearly demonstrate that the binding between α-CT and PDA NPs is strong compared to SB + PDA NPs. The thermodynamic data implies that PDA NPs significantly enhance the thermal stability of both α-CT and SB, as evidenced by the increased thermal transition temperature (T m ) by 2.68 ± 0.50 °C in α-CT and 3.35 ± 0.50 °C in SB. Interestingly, ζ-potential and microscopic results such as TEM and FESEM pointed toward the adsorption of both proteases over the surface of PDA NPs. Additionally, spectrophotometric assay and kinetic studies confirm the retention of enzyme activity of both proteases upon conjugation with PDA NPs. Further, kinetic (V max , K m ) and thermodynamic (ΔG u , ΔH m , ΔS m , ΔC p ) parameters also concluded the formation of a stable enzyme−NP complex. This study conveys the potential of PDA NPs in developing advanced enzyme−NPs integrated for enhancing protein stability and activity in diverse biomedical and industrial applications.

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Therapeutic efficacy of Chymotrypsin in acute bovine mastitis

Cited by 2 publications

References 25 publications

Alpha-Chymotrypsin Protects Against Acute Lung, Kidney, and Liver Injuries and Increases Survival in CLP-Induced Sepsis in Rats Through Inhibition of TLR4/NF-κB Pathway

Alpha-Chymotrypsin Protects Against Acute Lung, Kidney, and Liver Injuries and Increases Survival in CLP-Induced Sepsis in Rats Through Inhibition of TLR4/NF-κB Pathway

Interactions of Polydopamine Nanoparticles with Serine and Cysteine Proteases: Implications for Enhancing Protein Stabilization and Enzyme Activity

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