Cells Tissues OrgansBiochemistryPeer-reviewed journal article
Down regulation of Engase in Caenorhabditis elegans may improve its stresses adaptivity
Xinrong Lu, Yongliang TongiD, Mengting WuiD, Shaoxian Lyu, Jiale FaniD, Junyu Zheng, Lin ZouiD, Danfeng SheniD, Lin RaoiD, Linlin HouiD, Cuiying CheniD, Xunjia ChengiD, Guiqin SuniD, Zhiyong ShaoiD, Li CheniD
Abstract
Endo-beta-N-acetylglucosaminidase (ENGASE) is one of the key enzymes involved in the regulation of structure and function of glycoproteins. It is conserved from prokaryotic to eukaryotic cells. Although their activities in vitro and applications have been well studied, the biological function of ENGASE remains to be illustrated. In this study, we analyzed the molecular and physiological function of Engase from Caenorhabditis elegans homolog eng-1(CeEngase). We found that CeEngase knockout or knockdown increased the environmental stresses adaptability, such as heat stress and osmotic stress. Preliminary glycomics analysis showed that the basement membrane proteins of extracellular matrix may be the main targets of CeENGASE. In addition, CeENGASE may selectively prefer to N2H7 glycans on glycoproteins. In conclusion, our data illustrated that the defection and/or down regulation of CeEngase may provide a beneficially adaptation for stresses.
- organism: C. elegans
- assay: proteomics
- research focus: cell type annotation
- research focus: cell signaling & trafficking
- research focus: development & morphogenesis
- approach: experimental assay
- Citations
- 4
- FWCI
- 0.96
- Field percentile
- top 30%
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