Alteration And Regulation Of Protein Glycosylation During Head Regeneration Of Planarian Dugesia Japonica

Glycosylation is an important post-translational modification,which plays a crucial role on cell differentiation,cell proliferation,cell migration and cell recognition.Mammalian regeneration is a complex procedure,and few researches has been focused on protein glycosylation regulation during regeneration.In the current experiment,we detected protein glycosylation changes during head regeneration of planarian Dugesia japonica with lectin microarray.We found 6 kinds of lectin binding glycans up-regulated(fold change>1.5)and 16 kinds down-regulated(fold change<0.67),and the LCA binding core fucosylation was significantly up-regulated(fold change>1.5,***p<0.001).The result of lectin histochemistry indicated that core fucosylation intensified apparently within the wound and blastemal area.Lectin histochemistry and BrdU labeling showed the core fucosylation observed in neoblasts or cells derived from neoblasts membrane.Interestingly,we found that Fut8 gene expression was significantly up-regulated at 1 dpa during planarian head regeneration.In addition,53 core fucose-binding glycoproteins were identified during regeneration including neoblasts marker DjPIWIA,DjPIWIB,DjVLGA,DjVLGB and the proteins relation to regeneration of nervous system DjTBH,DjCHC,DjCAM.Furthermore,we found planarian head regenerationwas significantly retarded by treating with the fucosylation inhibitor,including cell proliferation,eye spots regeneration,nervous system formation.Overall,our study provides direct evidence for the involvement of protein core fucosylation during planarian head regeneration.