MB1, a quail leukocyte/vascular endothelium antigen: characterization of the lymphocyte-surface form and identification of its secreted counterpart as α2-macroglobulin

Abstract

A monoclonal antibody (α-MB1) binds to a cell surface marker expressed throughout ontogeny and adult life by vascular endothelial and hemopoietic cells of the quail, with the exception of erythrocytes, although it was raised against the heavy chain of quail immunoglobulin M. In addition to an 80 kDa polypeptide accounting for immunoglobulin μ chain, α-MB1 stains intensely a 180-kDa band on Western blots of reduced plasma proteins. We have previously characterized MB1 antigens of quail endothelial cells as glycoproteins of apparent molecular masses ranging from 80 to 200 kDa and provided evidence for the participation of vascular endothelium in the secretion of α-MB1-positive plasma components. We demonstrate here that this circulating material is the proteinase inhibitor α₂-macroglobulin. Furthermore, the MB1 antigens immunoprecipitated from lymphocytes are shown to be essentially similar to their endothelial counterparts, suggesting that the same molecular complex is expressed by all the elements of the hemangioblastic cell lineage. Finally, the cross reactivity of the α-MB1 antibody with immunoglobulin μ chain is confirmed and shown to occur via a carbohydrate epitope.