Abstract:
:The dependence of CMP-N-acetylneuraminate:GM1 sialyltransferase (SAT IV) activity of rat liver Golgi apparatus on GM1 ganglioside ceramide composition was evaluated. SAT IV activity was assayed on GM1 molecular species carrying homogeneous ceramide moieties containing long chain bases of different length (18 or 20 C atoms) unsaturated or not, linked to 14:0, 16:0, 18:0 or 22:0 fatty acids. The results obtained in the presence of the detergent Triton CF-54, when enzyme and substrate are presumably part of the same supramolecular structure, show that either the long chain base or the fatty acid composition can affect enzyme activity. This feature was not displayed when GM1 was embedded in dipalmitoylphosphatidylcholine vesicles in the absence of detergent. Under the latter conditions, the enzyme was not sensitive to the lipid composition of GM1 but to the ganglioside/phospholipid ratio in the vesicles. These results indicate for the first time that SAT IV is affected by the lipid composition of the substrate and strengthen the hypothesis that glycosyltranferases may contribute to control the cellular glycosphingolipid ceramide pattern.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Pitto M,Palestini P,Masserini Mdoi
10.1016/0014-5793(96)00262-1subject
Has Abstractpub_date
1996-04-01 00:00:00pages
223-6issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(96)00262-1journal_volume
383pub_type
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