muramidase has been researched along with baicalin* in 3 studies
3 other study(ies) available for muramidase and baicalin
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Kidney-targeted baicalin-lysozyme conjugate ameliorates renal fibrosis in rats with diabetic nephropathy induced by streptozotocin.
Diabetic nephropathy (DN) is one of the most common and serious complications of diabetes, and is the most important cause of death for diabetic patients. Baicalin (BAI) has anti-oxidative, anti-inflammatory and anti-apoptotic activities, which play a role in attenuating insulin resistance and protecting the kidney. Moreover, cell-specific targeting of renal tubular cells is an approach to enhance drug accumulation in the kidney.. Forty-five Sprague-Dawley rats were divided into four groups. A diabetes model was created using streptozotocin (STZ) intraperitoneally injection. The four groups included: Control group (n = 10), DN (n = 15), BAI treatment (BAI; n = 10) and BAI-LZM treatment (BAI-LZM; n = 10) groups. In the current study, the renoprotection and anti-fibrotic effects of BAI-lysozyme (LZM) conjugate were further investigated in rats with DN induced by STZ compared with BAI treatment alone.. The results suggest that BAI-LZM better ameliorates renal impairment, metabolic disorder and renal fibrosis than BAI alone in rats with DN, and the potential regulatory mechanism likely involves inhibiting inflammation via the nuclear factor-κB signaling pathway, inhibiting extracellular matrix accumulation via the transforming growth factor-β/Smad3 pathway and regulating cell proliferation via the insulin-like growth factor (IGF)-1/IGF-1 receptor/p38 Mitogen-activated protein kinase (MAPK) pathway. BAI and the kidney-targeted BAI-LZM can utilize the body's cytoprotective pathways to reactivate autophagy (as indicated by the autophagy markers mechanistic target of rapamycin and sirtuin 1 to ameliorate DN outcomes.. Our data support the traditional use of S. baicalensis as an important anti-DN traditional chinese medicine (TCM), and BAI, above all BAI-LZM, is a promising source for the identification of molecules with anti-DN effects. Topics: Animals; Anti-Inflammatory Agents, Non-Steroidal; Blood Glucose; Cholesterol; Diabetes Mellitus, Experimental; Diabetic Nephropathies; Drug Carriers; Drug Delivery Systems; Fibrosis; Flavonoids; Insulin; Kidney; Malondialdehyde; Muramidase; Rats; Triglycerides | 2020 |
Baicalin promotes the bacteriostatic activity of lysozyme on S. aureus in mammary glands and neutrophilic granulocytes in mice.
Staphylococcus aureus causes mastitis as a result of community-acquired or nosocomial infections. Lysozyme (LYSO) is an enzyme that is upregulated in many organisms during the innate immune response against infection by bacterial pathogens. Baicalin is a bioactive flavonoid that can bind to enzymes, often to potentiate their effect. Here we tested the effects of baicalin on the activity of LYSO using the S. aureus mastitis mouse model and neutrophilic granulocyte model of S. aureus infection. In our experiments, S. aureus counts decreased with increasing baicalin concentration. Furthermore, qPCR and western blot analyses showed that LYSO expression was unaffected by baicalin, while fluorescence quenching and UV fluorescence spectral analyses showed that baicalin binds to LYSO. To test whether this binding increased LYSO activity, we assessed LYSO-induced bacteriostasis in the presence of baicalin. Our results showed that LYSO-induced S. aureus bacteriostasis increased with increasing concentrations of baicalin, and that baicalin binding to LYSO synergistically increased the antibacterial activity of LYSO. These results demonstrate that baicalin enhances LYSO-induced bacteriostasis during the innate immune response to S. aureus. They suggest baicalin is a potentially useful therapeutic agent for the treatment of bacterial infections. Topics: Animals; Anti-Infective Agents; Blotting, Western; Cells, Cultured; Female; Flavonoids; Host-Pathogen Interactions; Mammary Glands, Animal; Mastitis; Mice, Inbred BALB C; Microbial Viability; Muramidase; Neutrophils; Protein Binding; Reverse Transcriptase Polymerase Chain Reaction; Spectrometry, Fluorescence; Staphylococcal Infections; Staphylococcus aureus | 2017 |
Comparative studies on interactions of baicalein, baicalin and scutellarin with lysozyme.
The interactions of baicalein, baicalin and scutellarin with lysozyme (LYSO) were studied by fluorescence and UV spectroscopy. The results showed that all the three flavones can quench the fluorescence of LYSO via static quenching with the distance between the donor and acceptor less than 7 nm. The hydroxyl at B-ring gave flavones an advantage to binding with LYSO. Electrostatic forces played a major role in stabilizing baicalein-LYSO complex and baicalin-LYSO complex, whereas hydrophobic interactions in scutellarin-LYSO. Furthermore, the presence of pantothenic acid can increase the binding constant and the number of binding sites between flavones and LYSO. Topics: Animals; Anti-Infective Agents; Apigenin; Chickens; Enzyme Inhibitors; Flavanones; Flavonoids; Glucuronates; Muramidase; Pantothenic Acid; Protein Binding; Spectrometry, Fluorescence | 2011 |