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1‐Deoxymannojirimycin inhibits Golgi‐mediated processing of glycoprotein in Xenopus oocytes
Author(s) -
Fabbrini Maria Serena,
Zoppè Monica,
Bollini Roberto,
Vitale Alessandro
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80144-3
Subject(s) - golgi apparatus , xenopus , glycoprotein , protein subunit , oocyte , messenger rna , microbiology and biotechnology , mannose , in vitro , biology , chemistry , biochemistry , gene , endoplasmic reticulum , embryo
We prepared in vitro an mRNA transcript coding for the erythroagglutinating subunit of the kidney bean glycoprotein phytohemagglutinin, E‐PHA. The mRNA, injected into Xenopus oocytes, synthesized E‐PHA carrying two Asn‐linked carbohydrate chains, one of which was processed and acquired resistance to endo‐β‐ N ‐acetylglucosaminidase H, as occurs in the native bean cells. When the mannose analog 1‐deoxymannojirimycin, an inhibitor of mammalian Golgi mannosidase I, was included in the oocyte culture medium, the acquisition of endo‐β‐ N ‐acetylglucosaminidase H resistance was abolished, indicating that also in an amphibian cell the inhibitor blocks a key reaction in Golgi‐mediated processing.