The presence of N-glycosylated proteins in cell nuclei.
The protein-DNA crosslinking capability of cis-dichloro diammineplatinum has been exploited to check the intranuclear location of N-glycosylated proteins. When intact liver cells were treated with this reagent, a number of glycoproteins, recognized by Concanavalin A, have been shown to become crosslinked to DNA; many of them have been recognized as nuclear matrix components. The recognition by this lectin was abolished by treatment with N-glycosidase F, showing the presence of N-glycosidic bonds between the sugar moiety and the protein. Most of the glycoproteins appeared to have high mannose oligosaccharide chains, but sialic acid containing oligosaccharides were also identified.
Ferraro
A
A
Department of Biochemical Sciences A. Rossi Fanelli, University La Sapienza, Rome.
Grandi
P
P
Eufemi
M
M
Altieri
F
F
Cervoni
L
L
Turano
C
C
D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D002945:Cisplatin / Q000494:pharmacology*; D003208:Concanavalin A; D003432:Cross-Linking Reagents; D004247:DNA / Q000302:isolation & purification / Q000378:metabolism*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006031:Glycosylation; D008099:Liver / Q000378:metabolism*; D011485:Protein Binding; D013552:Swine
D003432:Cross-Linking Reagents; D006023:Glycoproteins; D003208:Concanavalin A; D004247:DNA; D002945:Cisplatin