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NUCLEAR GLYCOCONJUGATES AND THEIR RELATION TO MALIGNANCY
Author(s) -
STODDART R. W.
Publication year - 1979
Publication title -
biological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.993
H-Index - 165
eISSN - 1469-185X
pISSN - 1464-7931
DOI - 10.1111/j.1469-185x.1979.tb01010.x
Subject(s) - sialic acid , glycoconjugate , biochemistry , nuclear membrane , nuclear matrix , chemistry , nucleus , glycosylation , nuclear lamina , membrane , nucleoplasm , cell nucleus , glycoprotein , golgi apparatus , microbiology and biotechnology , chromatin , nuclear protein , biology , cell , dna , cytoplasm , gene , transcription factor , nucleolus
Summary 1. The nucleus has a distinctive carbohydrate chemistry, the main features of which are the lack of glycosphingolipid, the high density of carbohydrate per unit area of nuclear membrane, the presence of glycosaminoglycan in the nuclear matrix and possibly the nuclear membranes, and the existence of glycosylated non‐histone proteins. 2. The nucleus has considerable autonomy in its metabolism of glycosaminoglycan and has a capacity for glycosyl transfers involving glycosyl dolichyl phosphates and pyrophosphates. This latter activity probably resides in the nuclear membranes. 3. The soluble fraction of the nucleoplasm contains the total cellular CMP‐sialic‐acid synthetase and, hence, all sialic acid metabolism passes through the nucleus, which may have a regulatory role. Uncertainty remains as to the sialic acid content of the glycoproteins of the nucleus and it is likely to vary between cell types. 4. Malignancy is associated with several alterations in the glycosylation of nuclear membranes, including increased levels of sialic acids in the glycoproteins of the inner nuclear membrane: changes in glycosylation of the matrix and chromatin are not yet well defined. In malignancy, some nuclear glycoproteins may possibly appear in other cellular membranes.