Platinum nanoparticles （NPs） are reported to mimic various anfioxidant enzymes and thus may produce a positive biological effect by reducing reactive oxygen species （ROS） levels. In this manuscript, we report Pt N...Platinum nanoparticles （NPs） are reported to mimic various anfioxidant enzymes and thus may produce a positive biological effect by reducing reactive oxygen species （ROS） levels. In this manuscript, we report Pt NPs as an enzyme mimic of ferroxidase by depositing platinum nanodots on gold nanorods （Au@Pt NDRs）. Au@Pt NDRs show pH-dependent ferroxidase-like activity and have higher activity at neutral pH values. Cytotoxicity results with human cell lines （lung adenocarcinoma A549 and normal bronchial epithelial cell line HBE） show that Au@Pt NDRs are taken up into cells via endocytosis and translocate into the endosome/lysosome. Au@Pt NDRs have good biocompatibility at NDR particle concentrations lower than 0.15 nM. However, in the presence of H202, lysosome- located NDRs exhibit peroxidase-like activity and therefore increase cytotoxicity. In the presence of FeE＋, the ferroxidase-like activity of the NDRs protects cells from oxidative stress by consuming H202. Thorough consideration should be given to this behavior when employinK Au@Pt NDRs in biological svstems.展开更多
Iron(Fe)deficiency is common in agricultural crops and affects millions of people worldwide.Translocation of Fe in the xylem is a key step for Fe distribution in plants.The mechanism controlling this process remains l...Iron(Fe)deficiency is common in agricultural crops and affects millions of people worldwide.Translocation of Fe in the xylem is a key step for Fe distribution in plants.The mechanism controlling this process remains largely unknown.Here,we report that two Arabidopsis ferroxidases,LPR1 and LPR2,play a crucial and redundant role in controlling Fe translocation in the xylem.LPR1 and LPR2 are mainly localized in the cell walls of xylem vessels and the surrounding cells in roots,leaves,and stems.Knockout of both LPR1 and LPR2 increased the proportion of Fe(II)in the xylem sap,and caused Fe deposition along the vascular bundles especially in the petioles and main veins of leaves,which was alleviated by blocking blue light.The lpr1 lpr2 double mutant displayed constitutive expression of Fe deficiency response genes and overaccumulation of Fe in the roots and mature leaves under Fe-sufficient supply,but Fe deficiency chlorosis in the new leaves and inflorescences under low Fe supply.Moreover,the lpr1 lpr2 double mutant showed lower Fe concentrations in the xylem and phloem saps,and impaired 57Fe translocation along the xylem.In vitro assays showed that Fe(III)-citrate,the main form of Fe in xylem sap,is easily photoreduced to Fe(II)-citrate,which is unstable and prone to adsorption by cell walls.Taken together,these results indicate that LPR1 and LPR2 are required to oxidize Fe(II)and maintain Fe(III)-citrate stability and mobility during xylem translocation against photoreduction.Our study not only uncovers an essential physiological role of LPR1 and LPR2 but also reveals a new mechanism by which plants maintain Fe mobility during long-distance translocation in the xylem.展开更多
文摘Platinum nanoparticles （NPs） are reported to mimic various anfioxidant enzymes and thus may produce a positive biological effect by reducing reactive oxygen species （ROS） levels. In this manuscript, we report Pt NPs as an enzyme mimic of ferroxidase by depositing platinum nanodots on gold nanorods （Au@Pt NDRs）. Au@Pt NDRs show pH-dependent ferroxidase-like activity and have higher activity at neutral pH values. Cytotoxicity results with human cell lines （lung adenocarcinoma A549 and normal bronchial epithelial cell line HBE） show that Au@Pt NDRs are taken up into cells via endocytosis and translocate into the endosome/lysosome. Au@Pt NDRs have good biocompatibility at NDR particle concentrations lower than 0.15 nM. However, in the presence of H202, lysosome- located NDRs exhibit peroxidase-like activity and therefore increase cytotoxicity. In the presence of FeE＋, the ferroxidase-like activity of the NDRs protects cells from oxidative stress by consuming H202. Thorough consideration should be given to this behavior when employinK Au@Pt NDRs in biological svstems.
基金This work was supported by the Natural Science Foundation of Jiangsu Province(grant no.BK20190544)the Natural Science Foundation of China(grant no.41977375)+1 种基金the Fundamental Research Funds for the Central Universities(grant no.KYT201802KYCXJC2022002).
文摘Iron(Fe)deficiency is common in agricultural crops and affects millions of people worldwide.Translocation of Fe in the xylem is a key step for Fe distribution in plants.The mechanism controlling this process remains largely unknown.Here,we report that two Arabidopsis ferroxidases,LPR1 and LPR2,play a crucial and redundant role in controlling Fe translocation in the xylem.LPR1 and LPR2 are mainly localized in the cell walls of xylem vessels and the surrounding cells in roots,leaves,and stems.Knockout of both LPR1 and LPR2 increased the proportion of Fe(II)in the xylem sap,and caused Fe deposition along the vascular bundles especially in the petioles and main veins of leaves,which was alleviated by blocking blue light.The lpr1 lpr2 double mutant displayed constitutive expression of Fe deficiency response genes and overaccumulation of Fe in the roots and mature leaves under Fe-sufficient supply,but Fe deficiency chlorosis in the new leaves and inflorescences under low Fe supply.Moreover,the lpr1 lpr2 double mutant showed lower Fe concentrations in the xylem and phloem saps,and impaired 57Fe translocation along the xylem.In vitro assays showed that Fe(III)-citrate,the main form of Fe in xylem sap,is easily photoreduced to Fe(II)-citrate,which is unstable and prone to adsorption by cell walls.Taken together,these results indicate that LPR1 and LPR2 are required to oxidize Fe(II)and maintain Fe(III)-citrate stability and mobility during xylem translocation against photoreduction.Our study not only uncovers an essential physiological role of LPR1 and LPR2 but also reveals a new mechanism by which plants maintain Fe mobility during long-distance translocation in the xylem.
