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Last Updated: 3 years ago

Possible Interaction: Epigallocatechin Gallate and Collagenases

Research Papers that Mention the Interaction

EGCG inhibited the expression of inflammatory markers (IL-6, and IL-8), collagenases (matrix metalloproteinases (MMP) 1, and MMP3), and pain mediators (iNOS, and prostaglandin-endoperoxide synthase 2 (PTGS2)) in nucleus pulposus (NP) tissue challenged with the diffusion of IL-1β and TNF-α.
International journal of molecular sciences  •  2018  |  View Paper
Pre-treatment of fibroblasts with EGCG also inhibited UV-B-induced production of collagenases , MMP-1, MMP-8 and MMP-13, in a dose-dependent manner.
Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association  •  2008  |  View Paper
EGCG reduced the stimulation of p54 JNK/SAPK phosphorylation by IL-1beta but did … phosphorylation, the degradation of IkappaB or the activating phosphorylation of NFkappaB. We conclude that EGCG reduces the IL-… of both collagenase and stromelysin mRNA species, an effect which … by inhibition of the JNK/SAPK pathway.
Matrix biology : journal of the International Society for Matrix Biology  •  2004  |  View Paper
Among the tea catechins tested, ECg and EGCg showed the most potent inhibitory effect on collagenase activity when an optimal concentration of tea catechins (100 micrograms/ml) was added to reaction mixture containing collagenase and collagen.
Preincubation of collagenase with tea catechins reduced the collagenase activity as well.
Journal of periodontology  •  1993  |  View Paper
EGCG caused a concentration dependent quenching of the intrinsic fluorescence of tyrosine residue in the FCP , indicating the occurrence of interactions between FCP and EGCG.
Excimer-like species and dityrosine were regularly formed with the addition of EGCG into the solution, and the interaction of FCP and EGCG partly disrupted the structure-of the protein.
It is interesting to observe that the CD intensity of FCP around 198 nm decreased with high EGCG concentration, and the peak maximum shifted to a larger wavelength (red shift).
Therefore, a better understanding of the interaction between FCP and EGCG would help to control their functional properties in food products during processing, transportation and storage when we facilitate FCP as the vehicles for EGCG.
This study provides a theoretical basis for fortifying FCP products with EGCG.
Guang pu xue yu guang pu fen xi = Guang pu  •  2015  |  View Paper
Both catechin and EGCG exhibited competitive mode of inhibition against collagenase.
Catechin and EGCG treated collagen exhibited 56 and 95% resistance, respectively, against collagenolytic hydrolysis by collagenase.
Higher inhibition of EGCG compared to catechin has been attributed to the ability of EGCG to exhibit better hydrogen bonding and hydrophobic interaction with collagenase.
The kinetics of inhibition of collagenase by catechin and EGCG has been deduced from the extent of hydrolysis of (2-furanacryloyl-L-leucyl-glycyl-L-prolyl-L-alanine), FALGPA.
Whereas direct interaction of catechin and EGCG with collagenase exhibited 70 and 88% inhibition, respectively, to collagenolytic activity of collagenase against collagen and the inhibition was found to be concentration dependent.
International journal of biological macromolecules  •  2007  |  View Paper
The degree of crosslinking, cartilage compressive stiffness, cartilage-bone interface strength, coefficient of friction, and residual mass after collagenase exposure all increased with an increasing EGCG concentration.
Journal of functional biomaterials  •  2017  |  View Paper
The SEM examination showed that 0.1% and 0.5% EGCG priming for 120 s significantly increased dentin collagen's resistance to collagenase.
Zhonghua kou qiang yi xue za zhi = Zhonghua kouqiang yixue zazhi = Chinese journal of stomatology  •  2016  |  View Paper
It is concluded that tannic acid, EGCG and ECG bind to collagen via extensive hydrogen bonding augmented by some hydrophobic interactions and prevent the free access of collagenase to active sites on the collagen chains.
Journal of materials science. Materials in medicine  •  2010  |  View Paper