A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid.

ABSTRACT: In the transmembrane domain and cytoplasmic domain of human CD44 protein there are two cysteine residues. These two cysteines are conserved in all known mammalian CD44 proteins. The functions of these cysteine residues are not known. Site-specific mutagenesis was used to create CD44 mutant proteins lacking either one or both of these cysteine residues. Wild-type CD44 and mutant CD44 genes were transfected into CD44- Jurkat cells to establish stable transfectants. These transfectants were used to study whether these two cysteine residues are important in the binding of CD44(H) to fluorescein-conjugated hyaluronic acid (F-HA). Jurkat transfectant bearing wild-type CD44 did not bind F-HA, unless they were stimulated in vitro with immobilized anti-CD3 monoclonal antibody. Anti-CD3 antibody als

SUBMITTER: Liu D 

PROVIDER: S-EPMC2192584 | biostudies-literature | 1996 May

REPOSITORIES: biostudies-literature