TI  - Coassociation of  <prot>CD26</prot>  (<prot>dipeptidyl peptidase IV</prot>) with  <prot>CD45</prot>  on the surface
      of human T lymphocytes.
PG  - 2514-7
AB  - In the present report, we demonstrated that modulation of  <prot>CD26</prot>  from T cell
      surface induced by  anti <prot>CD26</prot> (1F7)  led to enhanced phosphorylation of <prot>CD3</prot>
      zeta tyrosine residues and increased <prot>CD4</prot> associated p56lck tyrosine kinase
      activity. We further showed that <prot>CD26</prot> was comodulated on the T cell
      surface with <prot>CD45</prot>, a known membrane-linked protein tyrosine phosphatase
      and that anti-<prot>CD26</prot> was capable of precipitating <prot>CD45</prot> from T cell lysates.
      These findings strongly suggest that <prot>CD26</prot> may be closely associated with
      the <prot>CD45</prot> protein tyrosine phosphatase on T cell surface and further
      support the notion that the interaction of  <prot>CD26</prot>  with  <prot>CD45</prot>  results in
      enhanced tyrosine kinase activity, zeta chain phosphorylation, and T cell
      activation.
AD  - Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA
