1-Deoxymannojirimycin inhibits Golgi-mediated processing of glycoprotein in Xenopus oocytes.
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-beta-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-beta-N-acetylglucosaminidase H resistance was abolished, indicating that also in an amphibian cell the inhibitor blocks a key reaction in Golgi-mediated processing.
Fabbrini
M S
MS
Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, Milano, Italy.
Zoppè
M
M
Bollini
R
R
Vitale
A
A
D017485:1-Deoxynojirimycin; D000818:Animals; D005260:Female; D005944:Glucosamine / Q000031:analogs & derivatives / Q000494:pharmacology; D006023:Glycoproteins / Q000235:genetics*; D006056:Golgi Apparatus / Q000187:drug effects / Q000378:metabolism*; D009865:Oocytes / Q000187:drug effects / Q000378:metabolism*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics; D014981:Xenopus
D006023:Glycoproteins; D012333:RNA, Messenger; D017485:1-Deoxynojirimycin; D005944:Glucosamine