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Alpha-Mannosidase-II Deficiency Results in Dyserythropoiesis and Unveils an Alternate Pathway in Oligosaccharide Biosynthesis
Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts.
Although the primary defect in CDGS is not identified, these studies show that intracellular mannose is limited and that some patients might benefit from includingMannose in their regular diets.
Direct utilization of mannose for mammalian glycoprotein biosynthesis.
The results suggest that mammals use mannose transporters to deliverMannose from blood to the liver and other organs for glycoprotein biosynthesis, and that Extracellular mannoses may also make a significant contribution to glycop protein biosynthesis in the intact organism.
Mannose supplementation corrects GDP-mannose deficiency in cultured fibroblasts from some patients with Congenital Disorders of Glycosylation (CDG).
The results confirm directly that deficiencies in PMM and PMI result in lowered cellular GDP-Man levels that are corrected by the addition of mannose, and suggest that the regulation of Man-P-Dol synthesis and utilization may be more complex than is currently understood.
Two Proteins Modulating Transendothelial Migration of Leukocytes Recognize Novel Carboxylated Glycans on Endothelial Cells1
- G. Srikrishna, K. Panneerselvam, V. Westphal, Violet Abraham, A. Varki, H. Freeze
- BiologyThe Journal of Immunology
- 1 April 2001
The results suggest that the carboxylated glycans play important roles in leukocyte trafficking by interacting with proteins known to modulate extravasation.
GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli.
A novel strategy for site-directed PEGylation using glycosyltransferases to attach PEG to O-glycans is presented, which was applied to three therapeutic polypeptides, granulocyte colony stimulating factor (G-CSF), interferon-alpha2b (IFN- alpha2b), and granulocytes/macrophage colony stimulation factor (GM- CSF), which are currently in clinical use.
Mannose Enters Mammalian Cells Using a Specific Transporter That Is Insensitive to Glucose (*)
It is shown that the uptake of D-mannose by different mammalian cell lines involves a mannose-specific transporter(s) with a K of about 30-70 μM and a V which is probably sufficient to account for the bulk ofMannose needed for glycoprotein synthesis.
Human Fibroblasts Prefer Mannose over Glucose as a Source of Mannose for N-Glycosylation
- K. Panneerselvam, J. Etchison, H. Freeze
- Biology, ChemistryThe Journal of Biological Chemistry
- 12 September 1997
Results show that when fibroblasts are provided with physiological concentrations of mannose, they use theMan-6-P-specific transporter to supply the majority ofmannose needed for glycoprotein synthesis.
Abnormal metabolism of mannose in families with carbohydrate-deficient glycoprotein syndrome type 1.
- K. Panneerselvam, J. Etchison, F. Skovby, H. Freeze
- Biology, MedicineBiochemical and molecular medicine
- 1 August 1997
The results suggest that the reduced blood mannose level is a consequence of the PMM deficiency in CDGS Type 1 patients and their parents, the first inherited disorder in human metabolism that shows a decrease in available mannosed.
A Novel Anionic Modification of N-Glycans on Mammalian Endothelial Cells Is Recognized by Activated Neutrophils and Modulates Acute Inflammatory Responses1
Results indicate that these novel carboxylated N-glycans are constitutively expressed on vascular endothelium and participate in acute inflammatory responses by interaction with activated neutrophils.