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char = i;code = 105
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char = s;code = 115
char = .;code = 46
result sql = Glycosylation status of vitamin D binding protein in cancer patients.
Glycosylation status of vitamin D binding protein in cancer patients.
char = O;code = 79
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char = t;code = 116
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char = e;code = 101
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char = m;code = 109
char = o;code = 111
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char = i;code = 105
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char = (;code = 40
char = G;code = 71
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char = A;code = 65
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char = D;code = 68
char = B;code = 66
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char = .;code = 46
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char = i;code = 105
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char = d;code = 100
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char = e;code = 101
char = e;code = 101
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char = ;code = 32
char = O;code = 79
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result sql = On the basis of the results of activity studies, previous reports have suggested that vitamin D binding protein (DBP) is significantly or even completely deglycosylated in cancer patients, eliminating the molecular precursor of the immunologically important Gc macrophage activating factor (GcMAF), a glycosidase-derived product of DBP. The purpose of this investigation was to directly determine the relative degree of O-linked trisaccharide glycosylation of serum-derived DBP in human breast, colorectal, pancreatic, and prostate cancer patients. Results obtained by electrospray ionization-based mass spectrometric immunoassay showed that there was no significant depletion of DBP trisaccharide glycosylation in the 56 cancer patients examined relative to healthy controls. These results suggest that alternative hypotheses regarding the molecular and/or structural origins of GcMAF must be considered to explain the relative inability of cancer patient serum to activate macrophages.

Publication: Protein Sci. 2009 Oct ;18(10)::2036-42. :doi: 10.1002/pro.214.
Publication Date: 2009 Oct
Study Author(s): Rehder, Douglas S;Nelson, Randall W;Borges, Chad R;
Institution: The Biodesign Institute at Arizona State University, Tempe, 85287, USA.
Shortcut link to this study:
On the basis of the results of activity studies, previous reports have suggested that vitamin D binding protein (DBP) is significantly or even completely deglycosylated in cancer patients, eliminating the molecular precursor of the immunologically important Gc macrophage activating factor (GcMAF), a glycosidase-derived product of DBP. The purpose of this investigation was to directly determine the relative degree of O-linked trisaccharide glycosylation of serum-derived DBP in human breast, colorectal, pancreatic, and prostate cancer patients. Results obtained by electrospray ionization-based mass spectrometric immunoassay showed that there was no significant depletion of DBP trisaccharide glycosylation in the 56 cancer patients examined relative to healthy controls. These results suggest that alternative hypotheses regarding the molecular and/or structural origins of GcMAF must be considered to explain the relative inability of cancer patient serum to activate macrophages.
PMID: 19642159

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