Identification of two nuclear N-acetylglucosamine-binding proteins

✍ Scribed by Murielle Felin; Marie-Agnès Doyennette-Moyne; Yasmina Hadj-sahraoui; Michèle Aubery; Jean Hubert; Dr. Annie-Pierre Sève

• Publisher: John Wiley and Sons
• Year: 1994
• Tongue: English
• Weight: 818 KB
• Volume: 56
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240560413

✦ Synopsis

Using neoglycoproteins, lectins that recognize different sugars, including N-acetylglucosamine residues, were previously detected in animal cell nuclei. We report herein the isolation of two N-acetylglucosamine-binding proteins from HL60 cell nuclei: i) a 22 kDa polypeptide (CBP22) with an isoelectric point of 4.5 was isolated for the first time and ii) a 70 kDa polypeptide with an isoelectric point of 7.8. This latter protein corresponds to the glucose-binding protein (CBP70) previously isolated, based on the following similarities: i) they have the same molecular mass, ii) they have the same isoelectric point, iii) they are recognized by antibodies raised against CBP70, and iv) both are lectins from the C group of Drickamer's classification. CBP7O appeared to recognize glucose and N-acetylglucosamine; however, its affinity for N-acetylglucosamine was found to be twice that for glucose. The presence in the nucleus of two nuclear N-acetylglucosamine-binding proteins and their potential ligands, such as 0-N-acetylglucosamine glycoproteins, strongly argues for possible intranuclear glycoprotein-lectin interactions.