Restricted human CD45 isoglycoforms serve as functional E-selectin ligands and delineate hematopoietic maturity.

ABSTRACT: CD45 is the most abundant glycoprotein on the surface of all nucleated hematopoietic-lineage cells, comprising multiple isoforms generated by alternative splicing of three exons ("A," "B," and "C"), which are exquisitely restricted across hematopoietic development. Despite the ubiquitous expression of CD45 on hematopoietic cells, its function(s) remain rather obscure. Here, we report that discrete CD45 isoforms expressed uniquely by immature human hematopoietic cells are distinguished as functional glycoforms ("isoglycoforms") that bind E-selectin. Moreover, our studies indicate that "CD45RA," a marker of human acute myeloid leukemia (AML) cells, identifies a distinct isoglycoform of CD45 containing all splice exon-encoded peptides. This isoglycoform, "CD45RABC-E," is directly upregulated

SUBMITTER: Ales E 

PROVIDER: S-EPMC12336693 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature