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WM Parks, RD Gingrich, CE Dahle and JC Hoak
The purpose of these studies was to use monoclonal antibodies to identify
and characterize plasma membrane components unique to the vascular
endothelium. Our assumption is that such components may perform some of the
specialized functions of the endothelium and, by their identification with
antibody probes, we may be able to study further their function and
structure. Thus, primary cultures of human umbilical vein endothelium were
used to immunize mice whose spleen cells were fused with the mouse myeloma
cell NS-1. HEC-1 is a monoclonal antibody derived from such a fusion that
appears to react with an antigen located only on endothelial cells. The
antigen has been characterized by immunoprecipitation and polyacrylamide
gel electrophoresis as a glycoprotein with a mol wt of 180,000 daltons
under nonreducing conditions and 90,000 daltons under reducing conditions.
Despite a close resemblance to a membrane component shown by others to be a
receptor for transferrin, several lines of evidence reported in this paper
indicate that this is not the function of the HEC-1 antigen. These data
show that monoclonal antibodies can be used to identify and characterize
membrane components of the vascular endothelium. Moreover, these probes can
be used to inquire about the structure and function of the antigen with
which they react.
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