Nuclear Glycoproteins and Glycosaminoglycans

Stein, Gary S.; Roberts, R. M.; Stein, Janet L.; Davis, Jeudi

doi:10.1016/b978-0-12-147609-0.50017-4

Cited by 6 publications

(9 citation statements)

References 34 publications

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“…Presence of N-glycosylated proteins among the acidic nuclear NHP It has been reported previously that some of the nuclear NHP are glycoproteins (for review, see Stein et al, 1981). In the present report, we have confirmed and expanded these observations.…”

Section: Discussionsupporting

confidence: 94%

Demonstration that some of the nonhistone proteins, inducible to translocate into the nucleus, are glycosylated

Polet

Molnár

1988

Journal Cellular Physiology

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Con A, NaF, and eserine (lysosomotropic agents) induced marked translocation of acidic [3H] nonhistone proteins (NHP) from the cytoplasm to the nucleus in lymphocytes prelabeled with [3H]-2-mannose. The nuclear [3H] NHP contents were 38-120% higher in cells treated with these agents than in control cells. Tunicamycin, a strong inhibitor of N-glycosylation via the dolichol pathway, caused a concentration-dependent inhibition of [3H]-2-mannose incorporation into the nuclear [3H] NHP. Considerable amounts of nuclear [3H] NHP from lymphocytes labeled with either [3H]-2-mannose or [3H] leucine, bound specifically to Con A-Sepharose and could be eluted by alpha-methyl mannoside. Con A and NaF caused also nuclear translocation of acidic [3H] NHP in cells labeled with [3H] glucosamine, [3H] galactose, or [3H] fucose. Fractionation of the nuclear proteins by isoelectric focusing in a pH gradient of 2.5-6.5 showed that multiple species of acidic NHP were labeled with each of the four 3H-sugars. These results indicate that a fraction of the acidic nuclear NHP are N-glycosylated proteins and that gene activation and mitogenesis are associated with the translocation of these glycoproteins to the nucleus. Considering the known intracellular traffic of nascent glycoproteins our results suggest that at least some of the acidic NHP are synthesized and glycosylated in the endoplasmic reticulum and the Golgi (secretory pathway). It is likely that these proteins, after completion of synthesis and glycosylation, emerge from the trans-stack of the Golgi packaged in vesicles and accumulate in the cytoplasm. Induction of nuclear translocation of such NHP by various agents may be mediated by a vesicular transport mechanism.

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Section: Discussionsupporting

confidence: 94%

Demonstration that some of the nonhistone proteins, inducible to translocate into the nucleus, are glycosylated

Polet

Molnár

1988

Journal Cellular Physiology

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“…It is well known that this glycosylation takes place in the cytosolic compartment by the action of the O-GlcNAcpolypeptide N-acetylglucosaminyltransferase [Haltiwanger et al, 1990]. The presence of nuclear proteins bearing N-linked oligosaccharide chains has also been reported [Stein et al, 1975[Stein et al, , 1981Reeves et al, 1981;Ferraro et al, 1991;Codogno et al, 1992]. But, to the best of our knowledge, it is the first time that both N-and O-linked oligosaccharides chains are found on a same nuclear glycoprotein.…”

Section: How and Where Can Such A Nuclearmentioning

confidence: 81%

“…All these elements were available for cytoplasmic glycoproteins. However, despite the accumulation of evidence demonstrating that glycoproteins are present in animal cell nuclei [reviewed in Hart et al, 1989;Hubert et al, 1989;Stein et al, 1975Stein et al, , 1981, the biosynthesis, structure, and sugar composition of nuclear glycoproteins remain poorly documented. Most of the data currently available derive from cytological studies using lectin histochemistry [Roth, 1983;Sève et al, 1984;Kan and Pinto da Silva, 1986;Kinoshita et al, 1988], labeled glycosidases [Londono and Bendayan, 1987], or autoradiography after incorporation of radiolabeled sugars into cells [Bennet and Hemming, 1986].…”

mentioning

confidence: 98%

CBP70, a glycosylated nuclear lectin

et al. 1997

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Some years ago, a lectin designated CBP70 that recognized glucose (Glc) but had a stronger affinity for N-acetylglucosamine (GlcNAc), was first isolated from HL60 cell nuclei. Recently, a cytoplasmic form of this lectin was described, and one 82 kDa nuclear ligand was characterized for the nuclear CBP70. In the present study, the use of Pronase digestion and the trifluoromethanesulphonic acid (TFMS) procedure strongly suggest that the nuclear and the cytoplasmic CBP70 have a same 23 kDa polypeptide backbone and, consequently, could be the same protein. In order to know the protein better and to obtain the best recombinant possible in the future, the post-translational modification of the nuclear and cytoplasmic CBP70 was analyzed in terms of glycosylation. Severals lines of evidence indicate that both forms of CBP70 are N- and O-glycosylated. Surprisingly, this glycosylation pattern differs between the two forms, as revealed by beta-elimination, hydrazinolysis, peptide-N-glycosydase F (PNGase F), and TFMS reactions. The two preparations were analyzed by affinity chromatography on immobilized lectins [Ricinus communis-l agglutinin (RCA-I), Arachis hypogaea agglutinin (PNA), Galanthus nivalis agglutinin (GNA), and wheat germ agglutinin (WGA)] and by lectin-blotting analysis Sambucus nigra agglutinin (SNA), Maackia amurensis agglutinin (MAA), Lotus tetragonolobus (Lotus), succinylated-WGA, and Psathyrella velutina agglutinin (PVA)]. Both forms of CBP70 have the following sugar moities: terminal beta Gal residues, Gal beta 1-3 GalNAc, Man alpha 1-3 Man, sialic acid alpha 2-6 linked to Gal or GalNAc; and sialic acid alpha 2-3 linked to Gal. However, only nuclear CBP70 have terminal GlcNAc and alpha-L-fucose residues. All these data are consistent with the fact that different glycosylation pattern found for each form of CBP70 might act as a complementary signal for cellular targeting.

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“…It has been thought [Hubert et al, 19891 that nuclear lectins might play their role by interacting with the sugar moieties of glycoproteins which are also known to be present in the nucleus. Although there is a line of evidence suggesting the existence of nuclear glycoproteins containing N-linked complex-oligosaccharide chains [Stein et al, 1975[Stein et al, , 1981Ferraro et al, 1991;Codogno et al, 19921, the only wellcharacterized nuclear glycoproteins bear Nacetylglucosamine residues attached in O-linkages (termed 0-GlcNAc) [Holt and Hart, 1986;reviewed in Haltiwanger et al, 19911. Some results obtained in vitro by different groups support the possible involvement of interactions between these glycoproteins and endogenous lectins in nuclear activities.…”

mentioning

confidence: 99%

Identification of two nuclear N‐acetylglucosamine‐binding proteins

Felin

Doyennette-Moyne

Hadj-Sahraoui

et al. 1994

J of Cellular Biochemistry

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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. CBP70 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 O-N-acetylglucosamine glycoproteins, strongly argues for possible intranuclear glycoprotein-lectin interactions.

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Nuclear Glycoproteins and Glycosaminoglycans

Cited by 6 publications

References 34 publications

Demonstration that some of the nonhistone proteins, inducible to translocate into the nucleus, are glycosylated

Demonstration that some of the nonhistone proteins, inducible to translocate into the nucleus, are glycosylated

CBP70, a glycosylated nuclear lectin

Identification of two nuclear N‐acetylglucosamine‐binding proteins

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