作者: Regis Doyonnas , James Yi-Hsin Chan , Lisa H. Butler , Irene Rappold , Jane E. Lee-Prudhoe
DOI: 10.4049/JIMMUNOL.165.2.840
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摘要: The novel sialomucin, CD164, functions as both an adhesion receptor on human CD34 + cell subsets in bone marrow and a potent negative regulator of hemopoietic progenitor proliferation. These diverse effects are mediated by at least two functional epitopes defined the mAbs, 103B2/9E10 105A5. We report here precise epitope mapping these mAbs together with that other CD164 N6B6 67D2. Using newly splice variants set soluble recombinant chimeric proteins encoded exons 1–6 gene, we demonstrate 105A5 map to distinct glycosylated regions within first mucin domain CD164. 67D2 contrast, recognize closely associated complex rely conformational integrity molecule encompass cysteine-rich 2 3. On basis their sensitivities reducing agents sialidase, O- sialoglycoprotease, N- glycanase treatments, have characterized grouped them into three classes analogy classification. class I is glycosidase, sialoglycoprotease sensitive; II glycanase, III not removed such enzyme treatments. Collectively, this study indicates previously observed differential expression adult tissues linked type specific post-translational modifications suggests role for epitope-associated carbohydrate structures function.