About: CD26/dipeptidylpeptidase IV—chemokine interactions: double‐edged regulation of inflammation and tumor biology

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About: CD26/dipeptidylpeptidase IV—chemokine interactions: double‐edged regulation of inflammation and tumor biology Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	CD26/dipeptidylpeptidase IV—chemokine interactions: double‐edged regulation of inflammation and tumor biology
Creator	Proost, Paul Gouwy, Mieke Damme, Jo Mortier, Anneleen Struyf, Sofie
Source	Medline; PMC
abstract	Post‐translational modification of chemokines is an essential regulatory mechanism to enhance or dampen the inflammatory response. CD26/dipeptidylpeptidase IV, ubiquitously expressed in tissues and blood, removes NH(2)‐terminal dipeptides from proteins with a penultimate Pro or Ala. A large number of human chemokines, including CXCL2, CXCL6, CXCL9, CXCL10, CXCL11, CXCL12, CCL3L1, CCL4, CCL5, CCL11, CCL14, and CCL22, are cleaved by CD26; however, the efficiency is clearly influenced by the amino acids surrounding the cleavage site and although not yet proven, potentially affected by the chemokine concentration and interactions with third molecules. NH(2)‐terminal cleavage of chemokines by CD26 has prominent effects on their receptor binding, signaling, and hence, in vitro and in vivo biologic activities. However, rather than having a similar result, the outcome of NH(2)‐terminal truncation is highly diverse. Either no difference in activity or drastic alterations in receptor recognition/specificity and hence, chemotactic activity are observed. Analogously, chemokine‐dependent inhibition of HIV infection is enhanced (for CCL3L1 and CCL5) or decreased (for CXCL12) by CD26 cleavage. The occurrence of CD26‐processed chemokine isoforms in plasma underscores the importance of the in vitro‐observed CD26 cleavages. Through modulation of chemokine activity, CD26 regulates leukocyte/tumor cell migration and progenitor cell release from the bone marrow, as shown by use of mice treated with CD26 inhibitors or CD26 knockout mice. As chemokine processing by CD26 has a significant impact on physiologic and pathologic processes, application of CD26 inhibitors to affect chemokine function is currently explored, e.g., as add‐on therapy in viral infection and cancer.
has issue date	2016-01-07(xsd:dateTime)
bibo:doi	10.1189/jlb.3mr0915-401r
bibo:pmid	26744452
has license	no-cc
sha1sum (hex)	e4c1a95a7e0982325ea7d3eb258483a4c7b32bd7
schema:url	https://doi.org/10.1189/jlb.3mr0915-401r
resource representing a document's title	CD26/dipeptidylpeptidase IV—chemokine interactions: double‐edged regulation of inflammation and tumor biology
has PubMed Central identifier	PMC7166560
has PubMed identifier	26744452
schema:publication	J Leukoc Biol
resource representing a document's body	covid:e4c1a95a7e0982325ea7d3eb258483a4c7b32bd7#body_text
is schema:about of	named entity 'stromal cell-derived factor 1' named entity 'CD26' named entity 'progenitor cell' named entity 'tumor cell' named entity 'CD26' named entity 'cleaved' named entity 'JUNE' named entity 'CLEAVED' named entity 'KNOCKOUT MICE' named entity 'ACTIVITY' covid:arg/e4c1a95a7e0982325ea7d3eb258483a4c7b32bd7 named entity 'continued' named entity 'HPC' named entity 'dipeptides' named entity 'leukocyte' named entity 'CCL11' named entity 'affect' named entity 'Abbreviations' named entity 'NH 2' named entity 'CD26' named entity 'receptor recognition' named entity 'cleavage' named entity 'CXCL12' named entity 'HSC' named entity 'influenced' named entity 'glycosaminoglycan' named entity 'amino acids' named entity 'gastric inhibitory peptide' named entity 'GLP-1' named entity 'signaling' named entity 'induced' named entity 'CD26' named entity 'tissue factor pathway' named entity 'GIP' named entity 'cleavage' named entity 'activity' named entity 'CXCL12' named entity 'chemokine' named entity 'leukocyte' named entity 'chemokine' named entity 'CCL3L1' named entity 'oncogene' named entity 'tissue factor pathway inhibitor' named entity 'GPCR' named entity 'receptor binding' named entity 'progenitor cell' named entity 'chemokine' named entity 'chemokines' named entity 'IP-10' named entity 'cleavage site' named entity 'stromal cell' named entity 'isoforms' named entity 'chemokine receptor' named entity 'CXCL6' named entity 'CD26' named entity 'CD26' named entity 'pathologic processes' named entity 'dipeptides' named entity 'inflammation' named entity 'tissues' named entity 'NH 2' named entity 'chemokines' named entity 'CXCL12' named entity 'chemotaxis' named entity 'CCR1' named entity 'antitumor' named entity 'chemokines' named entity 'HPCs' named entity 'cord blood' named entity 'CCL3L1' named entity 'CD26' named entity 'incretin' named entity 'CXCL10' named entity 'angiostatic' named entity 'infection' named entity 'bone marrow' named entity 'eosinophil'

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