PubMed · 111353
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M Brixy. 1979-06-20. [Blood groups].. https://pubmed.ncbi.nlm.nih.gov/111353/
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Deletion or reduction of histo-blood group A or B antigen in tumors of A or B individuals is clearly correlated with the degree of malignancy and metastatic potential in many types of human cancer. Haptotactic motility of A+H- or B+H- colonic or gastric tumor cell lines produced by transfection of A or B gene was significantly lower than that of parental A-H+ or B-H+ cells. This is ascribable to reduced function of alpha3 or alpha6/beta1 integrin receptor as we have recently shown. However, phenotypic changes resulting from gene transfection may not reflect physiological states associated with deletion or reduction vs. continuous expression of A or B antigen in tumors. We now describe the separation and phenotype characterization of A- cells from A+ tumor cell lines derived originally from colonic tumors of patients with histo-blood group A. A+ and A- populations were detected in originally A+ tumor cell lines SW480 and HT29. A- separated from A+ populations isolated from SW480 and HT29 were characterized by greatly enhanced haptotactic motility associated with reduced or deleted A expression at alpha3, alpha6, and beta1 integrin receptors which control cell motility. Nevertheless, expression of integrin receptors at the surface of A populations is the same as that for A+ populations for both SW480 and HT29 cells. Thus, A vs. H glycosylation in integrin receptors may alter their haptotactic function. Cell proliferation as reflected by 3H-thymidine incorporation was also reduced significantly in A+ as compared to A- populations. Our findings indicate that the degree of haptotactic motility and proliferation of colonic tumor cells are physiologically associated with the deletion or reduction vs. continuous expression of the histo-blood group A antigen.
We generated nonfimbriated mutants from both Vi-positive and -negative Salmonella typhi to analyze the role of type 1 fimbriae and Vi-antigen in bacterial invasion. A Vi-defective mutant of S. typhi GIFU 10007-3 was more invasive than the wild-type strain GIFU 10007. The wild-type strain expressing Vi-antigen did not agglutinate both Saccharomyces cerevisiae and human erythrocytes but Vi-defective mutants were able to agglutinate S. cerevisiae and human erythrocytes. Nonfimbriated mutants from Vi-negative GIFU 10007-3 lost the ability to adhere to S. cerevisiae but still could agglutinate human erythrocytes. The Vi-negative mutant increased secreted proteins and became 5-fold more invasive than the wild-type strain. Nonfimbriated Vi mutants became 50-120-fold more invasive than the wild-type GIFU 10007. To determine why nonfimbriated Vi mutants still agglutinate human red blood cells, we searched bacterial proteins that could bind human blood-type antigens. We finally identified a candidate 37 kDa outer membrane protein that recognized fucosyl-galactose, a structure common to blood type A, B and H antigens.