MMP-25 can Promote the Ubiquitination of TRAF6
Inflammation is a complex natural immune process, which can provide effective protection in time when multicellular organisms are infected by the outside world. Excessive immune response can cause damage to the body, such as the heat shock response caused by LPS carried by gram-negative bacteria.
Matrix metalloproteinase (MMP, matrix metalloproteinase) is a large family, named after it requires Ca2+, Zn2+ and other metal ions as cofactors. Its family members have similar structures, which are generally composed of five domains with different functions: (1)Hydrophobic signal peptide sequence; (2)The main function of the propeptide region is to maintain the stability of the zymogen. When this area is cut by exogenous enzymes, MMPs zymogen is activated; (3)The catalytic activity area contains zinc ion binding site, which is very important for enzyme catalysis. (4) the hinge area rich in proline; (5)The carboxylic terminal region is related to substrate specificity of the enzyme. Among them, the catalytically active region and the propeptide region are highly conserved. There is a certain degree of substrate specificity among various MMPs, but it is not absolute. The same MMP can degrade multiple extracellular matrix components, and a certain extracellular matrix component can be degraded by multiple MMPs, but the degradation efficiency of different enzymes can be different. Previous studies have found that the activation of macrophages can trigger the up-regulation of MMP-25 expression. In vitro functional tests have also proved that MMP can effectively cut the components of the extracellular matrix, such as type IV collagen. Relevant studies have shown that MMP-25 is involved in the occurrence of many diseases, including multiple sclerosis, but its specific function is unknown. In order to study this issue, the research team of Carlos Lopez-Otın from the University of Oviedo in Spain conducted an in-depth study.
First, the researchers constructed MMP-25 deletion mutant mice and verified the expression of MMP-25. Furthermore, the researchers found through blood tests that the mutant mice had hypergammaglobulinemia, and the expression of IL-1a in their bodies was correspondingly low.
In order to study the role of MMP-25 in natural immunity, the researchers injected LPS into wild-type mice and mutant mice respectively for stimulation. The results showed that the survival rate of mutant mice after being stimulated by LPS was significantly higher than that of the control group. In addition, the degree of inflammatory damage in the lungs of the mutant mice was significantly lower than that of the control group. This shows that MMP-25 has a positive regulatory effect on the occurrence of inflammation.
The researchers further discovered that the activation of NF-KB in the mutant mice's macrophages was inhibited after being stimulated by LPS. On the other hand, researchers found through in vitro experiments that MMP-25 can promote the ubiquitination of TRAF6. The above experiments prove that MMP-25 can promote the ubiquitination of TRAF6, thereby mediating the activation of NF-KB and inflammation caused by LPS.
At present, Wuxi Donglin Sci & Tech Development Co.,Ltd. has developed a variety of ELISA products about MMP-25 . For more information, you can directly contact our professionals or visit our website:
http://www.dldevelop.com/Research-reagent/dl-mmp25-hu.html
Matrix metalloproteinase (MMP, matrix metalloproteinase) is a large family, named after it requires Ca2+, Zn2+ and other metal ions as cofactors. Its family members have similar structures, which are generally composed of five domains with different functions: (1)Hydrophobic signal peptide sequence; (2)The main function of the propeptide region is to maintain the stability of the zymogen. When this area is cut by exogenous enzymes, MMPs zymogen is activated; (3)The catalytic activity area contains zinc ion binding site, which is very important for enzyme catalysis. (4) the hinge area rich in proline; (5)The carboxylic terminal region is related to substrate specificity of the enzyme. Among them, the catalytically active region and the propeptide region are highly conserved. There is a certain degree of substrate specificity among various MMPs, but it is not absolute. The same MMP can degrade multiple extracellular matrix components, and a certain extracellular matrix component can be degraded by multiple MMPs, but the degradation efficiency of different enzymes can be different. Previous studies have found that the activation of macrophages can trigger the up-regulation of MMP-25 expression. In vitro functional tests have also proved that MMP can effectively cut the components of the extracellular matrix, such as type IV collagen. Relevant studies have shown that MMP-25 is involved in the occurrence of many diseases, including multiple sclerosis, but its specific function is unknown. In order to study this issue, the research team of Carlos Lopez-Otın from the University of Oviedo in Spain conducted an in-depth study.
First, the researchers constructed MMP-25 deletion mutant mice and verified the expression of MMP-25. Furthermore, the researchers found through blood tests that the mutant mice had hypergammaglobulinemia, and the expression of IL-1a in their bodies was correspondingly low.
In order to study the role of MMP-25 in natural immunity, the researchers injected LPS into wild-type mice and mutant mice respectively for stimulation. The results showed that the survival rate of mutant mice after being stimulated by LPS was significantly higher than that of the control group. In addition, the degree of inflammatory damage in the lungs of the mutant mice was significantly lower than that of the control group. This shows that MMP-25 has a positive regulatory effect on the occurrence of inflammation.
The researchers further discovered that the activation of NF-KB in the mutant mice's macrophages was inhibited after being stimulated by LPS. On the other hand, researchers found through in vitro experiments that MMP-25 can promote the ubiquitination of TRAF6. The above experiments prove that MMP-25 can promote the ubiquitination of TRAF6, thereby mediating the activation of NF-KB and inflammation caused by LPS.
At present, Wuxi Donglin Sci & Tech Development Co.,Ltd. has developed a variety of ELISA products about MMP-25 . For more information, you can directly contact our professionals or visit our website:
http://www.dldevelop.com/Research-reagent/dl-mmp25-hu.html
