PMID- 10221653
OWN - NLM
STAT- MEDLINE
DCOM- 19990629
LR  - 20190513
IS  - 0953-8178 (Print)
IS  - 0953-8178 (Linking)
VI  - 11
IP  - 3
DP  - 1999 Mar
TI  - CD26/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells
      and monocytes toward RANTES: possible mechanism for the switch from innate to
      acquired immune response.
PG  - 417-26
AB  - CD26, a 110 kDa cell surface glycoprotein, exhibits dipeptidyl peptidase IV
      (DPPIV; EC 3.4.14.5) enzyme activity and plays an important role in T cell
      co-stimulation. In the present study, the function of CD26/DPPIV in
      transendothelial migration was examined using beta-chemokines as
      chemoattractants. When soluble recombinant CD26 (sCD26/DPPIV+) was added to the
      transendothelial chemotaxis system, chemotactic migration of T cells toward
      RANTES was significantly enhanced. Addition of sCD26 to 50 ng/ml of RANTES
      enhanced the migratory response by a factor of two compared to RANTES alone,
      whereas mutant soluble CD26 (mCD26), lacking the DPPIV enzyme activity, had no
      enhancing effect on RANTES-induced T cell migration. In the process of analyzing 
      the mechanisms of the enhancement of T cell migration by sCD26, we showed that
      RANTES was cleaved by sCD26 under physiologic conditions at the precise site
      characteristic of its enzyme specificity. However, synthesized RANTES which lacks
      two N-terminal amino acids showed a chemotactic activity equivalent to
      full-length RANTES on T cells. Furthermore, addition of sCD26 showed enhancement 
      of T cell migration induced by both forms of RANTES. In contrast to T cells, the 
      truncated RANTES is inactive in chemotaxis of purified monocytes and supplement
      of sCD26 but not mCD26 reduced the migratory response of monocytes to RANTES.
      These results suggest that CD26/DPPIV differentially regulate the chemotactic
      response of T cells and monocytes to RANTES.
FAU - Iwata, S
AU  - Iwata S
AD  - Dana-Farber Cancer Institute, and Department of Medicine, Harvard Medical School,
      Boston, MA 02115, USA.
FAU - Yamaguchi, N
AU  - Yamaguchi N
FAU - Munakata, Y
AU  - Munakata Y
FAU - Ikushima, H
AU  - Ikushima H
FAU - Lee, J F
AU  - Lee JF
FAU - Hosono, O
AU  - Hosono O
FAU - Schlossman, S F
AU  - Schlossman SF
FAU - Morimoto, C
AU  - Morimoto C
LA  - eng
GR  - AI12069/AI/NIAID NIH HHS/United States
GR  - AI29530/AI/NIAID NIH HHS/United States
GR  - AR33713/AR/NIAMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Int Immunol
JT  - International immunology
JID - 8916182
RN  - 0 (Chemokine CCL5)
RN  - 0 (Peptide Fragments)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
SB  - IM
MH  - Amino Acid Sequence
MH  - Chemokine CCL5/metabolism/*pharmacology
MH  - Chemotaxis, Leukocyte/*drug effects
MH  - Dipeptidyl Peptidase 4/metabolism/*pharmacology
MH  - Drug Interactions
MH  - Endothelium, Vascular/physiology
MH  - Humans
MH  - Molecular Sequence Data
MH  - Monocytes/*drug effects
MH  - Peptide Fragments/pharmacology
MH  - Solubility
MH  - T-Lymphocytes/*drug effects
EDAT- 1999/04/30 00:00
MHDA- 1999/04/30 00:01
CRDT- 1999/04/30 00:00
PHST- 1999/04/30 00:00 [pubmed]
PHST- 1999/04/30 00:01 [medline]
PHST- 1999/04/30 00:00 [entrez]
AID - 10.1093/intimm/11.3.417 [doi]
PST - ppublish
SO  - Int Immunol. 1999 Mar;11(3):417-26. doi: 10.1093/intimm/11.3.417.