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

Iwata, Satoshi; Yamaguchi, Noriko; Munakata, Yasuhiko; Ikushima, Hideto; Lee, James F.; Hosono, Osamu; Schlossman, Stuart F.; Morimoto, Chikao

doi:10.1093/intimm/11.3.417

Cited by 97 publications

(69 citation statements)

References 37 publications

(29 reference statements)

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“…To study the possible influence of chemokines on the cell surface expression of TSP-1, we exposed anti-CD3-activated lymphocytes (generally Ͼ92% CD3 positive cells) in suspension and on a fibronectin substrate to CXCL12 and CCL5, two chemokines processed by CD26 (53,54). The cells were cultured in serum-free medium to exclude interference of exogenous TSP-1.…”

Section: Cxcl12 and Ccl5 Induce Cell Surface Expression Of Tsp-1 And mentioning

confidence: 99%

“…1 suggested that chemokines metabolized by CD26, such as CXCL12 and CCL5 (53,54,58), that cleave Nterminal dipeptides from various chemokines regulate the cell surface expression of CD91 and TSP-1 through CD26. Therefore, we examined the possible influence of the CD26 inhibitors diprotin A, KR 62436, and vildagliptin on the cell surface expression of TSP-1 in anti-CD3-activated lymphocytes using quantitative immunocytochemistry and SDS-PAGE of immunoprecipitated biotinylated cell surface proteins (Fig.…”

Section: Cd26 Influences Cell Surface Expression Of Tsp-1mentioning

confidence: 99%

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A CD26-Controlled Cell Surface Cascade for Regulation of T Cell Motility and Chemokine Signals

Liu

Christensson

Forslöw

et al. 2009

The Journal of Immunology

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Chemokines are key regulators of cell trafficking, and dipeptidyl peptidase IV/CD26 (CD26) inactivates chemokines. Here we show that the CD26-processed chemokines SDF1α/CXCL12 and RANTES/CCL5, in contrast to a control chemokine not processed by CD26, are potent inducers of cell surface expression of thrombospondin-1 (TSP-1) in T lymphocytes through a CD26-controlled mechanism and that TSP-1 stimulates expression of lipoprotein receptor related protein/CD91. Accordingly, intact TSP-1 and a peptide mimetic of a sequence in TSP-1 were sufficient to stimulate CD91 expression. The chemokine-induced expression of TSP-1 and CD91 was mimicked by inhibitors of CD26 and CXCL12 and CCL5 as well as inhibitors of CD26 stimulated polarized cytoplasmic spreading and migration through TSP-1. Silencing of CD26 using small interfering RNA or Ab-induced modulation of CD26 also increased TSP-1 expression and enhanced cytoplasmic spreading and T cell migration markedly. These results indicate that CD26 is an endogenous inhibitor of T cell motility through inhibition of TSP-1 expression and that chemokines stimulate cell polarity and migration through abrogation of the CD26-dependent inhibition. This suggests that T cell motility is regulated by a cascade of interacting cell surface molecules.

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Section: Cxcl12 and Ccl5 Induce Cell Surface Expression Of Tsp-1 And mentioning

confidence: 99%

Section: Cd26 Influences Cell Surface Expression Of Tsp-1mentioning

confidence: 99%

A CD26-Controlled Cell Surface Cascade for Regulation of T Cell Motility and Chemokine Signals

Liu

Christensson

Forslöw

et al. 2009

The Journal of Immunology

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“…Truncation of the cytokine RANTES (regulated on activation, normal T cell-expressed and secreted) by CD26 changes the specificity of receptor interactions and target cells, and this might be a physiologically significant control mechanism [186][187][188].…”

Section: Bp-1/6c3 (Glutamyl Aminopeptidase Ec 34117)mentioning

confidence: 99%

Ecto-enzymes: physiology meets pathology

Goding

2000

Journal of Leukocyte Biology

101

111

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Ecto-enzymes are catalytic membrane proteins with their active sites outside the cell. They include cholinesterase, which inactivates acetylcholine, and angiotensin-converting enzyme, which converts angiotensin I to biologically active angiotensin II, and numerous other peptidases, transpeptidases, nucleotidases, phosphodiesterases, and phosphatases. Many CD antigens of leukocytes are ecto-enzymes; some CD antigens for which no function is currently known are probably ectoenzymes. Expression is highly regulated and correlated with differentiation and activation. Some are highly restricted in distribution; others are ubiquitous. Many are shared between leukocytes and non-hematogenous cells. Biological functions appear to depend on the type and location of the cell in which expression occurs, and include recycling of nutrients, local control of response to cytokines and hormones, bone formation, cell mobility, invasion, and metastasis. Many novel regulatory functions of ecto-enzymes remain to be discovered, and may reveal new mechanisms of local extracellular control of cellular function.

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“…The CXCR4 natural ligand SDF-1␣ has the conserved NH 2 -X-Pro sequence (where X is any amino acid) at the NH 2 terminus, which is a consensus sequence for substrates of dipeptidyl peptidase IV activity of CD26. It has been demonstrated that SDF-1␣ can be processed by CD26 (4,9,11,32). Therefore the CD26⅐CXCR4 complex is likely a functional unit in which the expression of CD26 on the cell surface may modulate SDF-1␣-induced chemotaxis.…”

Section: Discussionmentioning

confidence: 99%

Comodulation of CXCR4 and CD26 in Human Lymphocytes

Herrera

Morimoto

Blanco

et al. 2001

Journal of Biological Chemistry

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We provide convergent and multiple evidence for a CD26/CXCR4 interaction. Thus, CD26 codistributes with CXCR4, and both coimmunoprecipitate from membranes of T (CD4 ؉ ) and B (CD4 ؊ ) cell lines. Upon induction with stromal cell-derived factor 1␣ (SDF-1␣), CD26 is cointernalized with CXCR4. CXCR4-mediated downregulation of CD26 is not induced by antagonists or human immunodeficiency virus (HIV)-1 gp120. SDF1␣؊mediated down-regulation of CD26 is not blocked by pertussis toxin but does not occur in cells expressing mutant CXCR4 receptors unable to internalize. Codistribution and cointernalization also occurs in peripheral blood lymphocytes. Since CD26 is a cell surface endopeptidase that has the capacity to cleave SDF-1␣, the CXCR4⅐CD26 complex is likely a functional unit in which CD26 may directly modulate SDF-1␣-induced chemotaxis and antiviral capacity. CD26 anchors adenosine deaminase (ADA) to the lymphocyte cell surface, and this interaction is blocked by HIV-1 gp120. Here we demonstrate that gp120 interacts with CD26 and that gp120-mediated disruption of ADA/CD26 interaction is a consequence of a first interaction of gp120 with a domain different from the ADA binding site. SDF-1␣ and gp120 induce the appearance of pseudopodia in which CD26 and CXCR4 colocalize and in which ADA is not present. The physical association of CXCR4 and CD26, direct or part of a supramolecular structure, suggests a role on the function of the immune system and the pathophysiology of HIV infection.

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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

Cited by 97 publications

References 37 publications

A CD26-Controlled Cell Surface Cascade for Regulation of T Cell Motility and Chemokine Signals

A CD26-Controlled Cell Surface Cascade for Regulation of T Cell Motility and Chemokine Signals

Ecto-enzymes: physiology meets pathology

Comodulation of CXCR4 and CD26 in Human Lymphocytes

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