Phenotype - associated lectine - binding profiles of normal and transformed blood cells: a comparative analysis of mannose- and galactose- binding lectins from plants and human serum / placenta |
Journal/Book: Eur. J. Cell Biology 65, 145-151. 1994;
Abstract: Surface glycoconjugates of normal and transformed blood cells arecommonly characterized by plant lectins. To infer physiologicalsignificance of protein-carbohydrate interactions, mammalian lectins areobviously preferable as research tools. So far, human serum lectins havenot been used to assess their binding to immunophenotyped human normalor transformed blood cells. Thus, our study combines two groups oflectins with different specificity from plant and human sources. Besidesconcanavalin A (ConA) we have isolated the mannose-binding protein andserum amyloid P component from human serum. Especially themannose-binding protein is believed to play a role in host defenceagainst bacteria and yeast cells with unknown impact on normal and tumorcells. These three lectins establish the first group. In addition to theimmunomodulatory mistletoe lectin, whose binding can elicit enhancedcytokine secretion from mononuclear blood cells, we included thebeta-galactoside-binding lectin (14 kDa) from human placenta in thesecond group. The initial series of measurements was undertaken usingtwo-color flow cytometry to determine the phenotype-associated binding(based on cluster designation; CD) of the lectins to blood and bonemarrow cells from normal donors and the cell line CEM(T-lymphoblastoid), KG1-A (primitive myeloid leukemia) and Croco II(B-lymphoblastoid). Heterogeneity was apparent for each lectin in theCD-defined cell populations. Significant differences in binding werenoted between Viscum album agglutinin (VAA) and other lectins for CD4+cells from blood and between mannose-binding protein (MBP) and VAAversus 14 kDa, ConA and serum amyloid P component (SAP) for CD19+ cellsfrom bone marrow.(ABSTRACT TRUNCATED AT 250 WORDS) Author.
Keyword(s): BLOOD-CELLS/ ME (metabolism)
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