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-Mediated Chemotaxis of Human Cord Blood CD34+ Progenitor Cells1
Department of Microbiology/Immunology and The Walther Oncology Center, Indiana University School of Medicine, Indianapolis, IN 46202; and The Walther Cancer Institute, Indianapolis, IN 46208
CD26/dipeptidylpeptidase IV (DPPIV) is a membrane-bound
extracellular peptidase that cleaves dipeptides from the N terminus of
polypeptide chains. The N terminus of chemokines is known to interact
with the extracellular portion of chemokine receptors, and removal of
these amino acids in many instances results in significant changes in
functional activity. CD26/DPPIV has the ability to cleave the chemokine
CXCL12/stromal cell-derived factor 1
(SDF-1) at its
position two proline. CXCL12/SDF-1 induces migration of hemopoietic
stem and progenitor cells, and it is thought that CXCL12 plays a
crucial role in homing/mobilization of these cells to/from the bone
marrow. We found that CD26/DPPIV is expressed by a subpopulation of
CD34+ hemopoietic cells isolated from cord blood and that
these cells have DPPIV activity. The involvement of CD26/DPPIV in
CD34+ hemopoietic stem and progenitor cell migration has
not been previously examined. Functional studies show that the
N-terminal-truncated CXCL12/SDF-1 lacks the ability to induce the
migration of CD34+ cord blood cells and acts to inhibit
normal CXCL12/SDF-1-induced migration. Finally, inhibiting the
endogenous CD26/DPPIV activity on CD34+ cells enhances the
migratory response of these cells to CXCL12/SDF-1. This process of
CXCL12/SDF-1 cleavage by CD26/DPPIV on a subpopulation of
CD34+ cells may represent a novel regulatory mechanism in
hemopoietic stem and progenitor cells for the migration, homing, and
mobilization of these cells. Inhibition of the CD26/DPPIV peptidase
activity may therefore represent an innovative approach to increasing
homing and engraftment during cord blood
transplantation.
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