Human monoclonal antibody (HMST-1) against lacto-series type 1 chain and expression of the chain in uterine endometrial cancers.

A human monoclonal antibody termed HMST-1 was produced by fusing lymphocytes from segments of human pelvic lymph nodes from an endometrial cancer patient with murine myeloma cells. The epitope recognized by HMST-1 was determined to be lacto-series type 1 chain-containing glycosphingolipid (Galβ1-3GlcNAcβ1-3Galβ1-4Glcβ1-1Cer) by isolating the antigen from endometrial cancer cell line SNG-II and analyzing with fast atom bombardment mass spectrometry, permethylation analysis, and exoglycosidase treatment. By the immunohistochemical avidin-biotin-peroxidase complex method, no normal endometrium and benign endometrial hyperplasia were stained with HMST-1, but HMST-1 reacted with about 35% of endometrial cancer cases. These facts indicate that the rate of expression of the antigen increases along with the course of malignancy in the endometrium. By sialidase treatment of the section, the positive rate increased to 57% in endometrial cancers and to 13% in normal endometrium, indicating that the antigen was masked with sialic acid and exposed by neuraminidase treatment. Immunohistochemistry also revealed that the antibody reacted with human fetal alimentary tract epithelium and mesothelium, indicating the oncodevelopmental nature of Galβ1-3GlcNAcβ1-3Galβ1-4Glcβ1-1Cer.