Glycosylation of glycoproteins is regulated by several factors, including glycosyltransferase enzymes, suitable acceptor sites on proteins, Dol-P levels in tissues, and oligosaccharide-protein transferase activity. Different cells express different glycosyltransferases, and some require prior action of other enzymes. Glycosylation patterns can also differ between species and cells of the same species, influencing properties like the half-life of therapeutic proteins.
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Several Factors Regulate Glycosylation of Glycoproteins
3. Suitable acceptor sites in proteins.
The tissue level of Dol-P.
The activity of the oligosaccharide:protein transferase.
5. Different cells give different enzymes.
Certain glycosyltransferases act only on the
oligosaccaride chain if it has already been acted
upon by another previous enzyme.
EX: action of GlcNAc is important for Golgi
alpha-mannosaidase.
During which some genes are
turned on & others are turned off.
6. Each enzyme has its own destination for insertion.
Ex:HMG.CoA reductase ER membrane it may never
encounter Golgi-located processing enzyme.
Differences in proteins conformation
may hinder access of proccessing
enzymes.
7. The same cells(ex:fibroblast) of
different species exhibit
different patterns of processing
enzymes.
Species variation is an
important factor which is used
for production of Glycoproteins
of Therapeutic use by
Recombinant DNA tech.
EX:synthesized
Erythropoietin (EPO)
9. 1. Synthesized EPO is administered
to patients with chronic anemia in
order to stimulate Erythropoiesis.
2. The half-life of EPO in plasma is
influenced by the nature of its
glycosylation pattern.
3. Some species give patterns with
short HL, others give them with
normal HL.