Carbohydrate and peptide antigens in macrophage populations derived from human bone marrow and milk: an immunomorphological and immunochemical analysis |
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Authors: | S E Baldus J Thiele Y -O Park A Charles C Mross F -G Hanisch T K Zirbes C Wickenhauser and R Fischer |
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Institution: | (1) Institute of Pathology, University of Cologne, Joseph-Stelzmann-Str. 9, 50924 Cologne, Germany;(2) Institute of Immunobiology, University of Cologne, Kerpener Str. 15, 50924 Cologne, Germany |
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Abstract: | Summary An immunomorphological and immunochemical study was performed to elucidate the pattern of carbohydrate antigens and their
relationships to the cluster differentiation (CD) 68 epitopes on macrophages derived from human bone marrow and milk. Core
and backbone antigens recognized by lectins fromBauhinia purpurea (BPA),Helix pomatia (HPA),Arachis hypogaea (PNA),Glycine max. (SBA),Griffonia simplicifolia (GSA-I-B4),Lycopersicon esculentum (LEA) andErythrina cristagalli (ECA) were expressed by both macrophage populations. Additionally, they exhibited various peripheral type 1 and type 2 carbohydrate
antigens. In bone marrow trephine biopsies, the number of macrophages stained by the CD68-specific monoclonal antibody PG-M1
exceeded significantly (range 30–40%) the subpopulation expressing SBA, GSA-I-B4 and ECA binding sites as well as the Lewisa antigen. This result is very interesting since, fromin vitro studies, GSA-I-B4 and SBA are known to react especially with activated macrophages. Western blotting experiments on milk macrophage lysates
revealed that ECA, GSA-I-B4, BPA, PNA and MAA visualize a 110 kDa band isographic with the CD68 antigen detected by PG-M1, KP1 and Ki-M1P monoclonal
antibodies. These antibodies recognize peptide epitopes as shown by enzyme-linked immunosorbent assays after biochemical modification
of milk macrophage lysates. This result is in keeping with the assumption that the CD68 antigen consists of a highly glycosylated
mucin-type glycoprotein comprising various differentiation-dependent epitopes. |
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