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The glycosylation of GcMAF: T420
The vitamin D binding protein, Gc globulin, has in recent years received some attention for its role as precursor for the extremely potent macrophage activating factor (GcMAF). An O-linked trisaccharide has been allocated to the threonine residue at position 420 in two of the three most common isoforms of Gc globulin (Gc1s and Gc1f). A substitution for a lysine residue at position 420 in Gc2 prevents this isoform from being glycosylated at that position. It has been suggested that Gc globulin subjected sequentially to sialidase and galactosidase treatment generates GcMAF in the form of Gc globulin with only a single GalNAc attached to T420.
In this study we confirm the location of a linear trisaccharide on T420. Furthermore, we provide the first structural evidence of the generation of the proposed GcMAF by use of glycosidase treatment and mass spectrometry. Additionally the generated GcMAF candidate was tested for its effect on cytokine release from macrophages in human whole blood.
| The glycosylation and characterization of the candidate Gc macrophage activating factor. | |
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MedLine Citation:
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PMID: 20079467 Owner: NLM Status: Publisher |
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Abstract/OtherAbstract:
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The vitamin D binding protein, Gc globulin, has in recent years received some attention for its role as precursor for the extremely potent macrophage activating factor (GcMAF). An O-linked trisaccharide has been allocated to the threonine residue at position 420 in two of the three most common isoforms of Gc globulin (Gc1s and Gc1f). A substitution for a lysine residue at position 420 in Gc2 prevents this isoform from being glycosylated at that position. It has been suggested that Gc globulin subjected sequentially to sialidase and galactosidase treatment generates GcMAF in the form of Gc globulin with only a single GalNAc attached to T420. In this study we confirm the location of a linear trisaccharide on T420. Furthermore, we provide the first structural evidence of the generation of the proposed GcMAF by use of glycosidase treatment and mass spectrometry. Additionally the generated GcMAF candidate was tested for its effect on cytokine release from macrophages in human whole blood. |
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Authors:
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Tina Ravnsborg; Dorthe T Olsen; Anna Hammerich Thysen; Maja Christiansen; Gunnar Houen; Peter H??jrup |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2010-1-13 |
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Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1804 ISSN: 0006-3002 ISO Abbreviation: – Publication Date: 2010 Apr |
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Date Detail:
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Created Date: 2010-2-26 Completed Date: – Revised Date: - |
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Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: - |
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Other Details:
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Languages: ENG Pagination: 909-917 Citation Subset: - |
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Copyright Information:
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Copyright ?? 2010 Elsevier B.V. All rights reserved. |
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Affiliation:
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Institute of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark. |
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Source: http://www.biomedsearch.com/nih/glycosylation-characterization-candidate-Gc-macrophage/20079467.html
