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Processing by CD26/dipeptidyl‐peptidase IV reduces the chemotactic and anti‐HIV‐1 activity of stromal‐cell‐derived factor‐1α
Author(s) -
Proost Paul,
Struyf Sofie,
Schols Dominique,
Durinx Christine,
Wuyts Anja,
Lenaerts Jean-Pierre,
De Clercq Erik,
De Meester Ingrid,
Van Damme Jo
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00830-8
Subject(s) - dipeptidyl peptidase , stromal cell , haematopoiesis , chemokine , chemotaxis , cxcr4 , cxcl14 , receptor , stem cell factor , progenitor cell , cd34 , microbiology and biotechnology , cxc chemokine receptors , chemistry , immunology , chemokine receptor , biology , stem cell , cancer research , biochemistry , enzyme
The chemokine stromal‐cell‐derived factor‐1α (SDF‐1α) chemoattracts lymphocytes and CD34 + haematopoietic progenitors and is the ligand for CXCR4 (CXC chemokine receptor 4), the main co‐receptor for T‐tropic HIV‐1 strains. SDF‐1α was NH 2 ‐terminally cleaved to SDF‐1α(3‐68) by dipeptidyl‐peptidase IV (CD26/DPP IV), which is present in blood in soluble and membrane‐bound form. SDF‐1α(3‐68) lost both lymphocyte chemotactic and CXCR4‐signaling properties. However, SDF‐1α(3‐68) still desensitized the SDF‐1α(1‐68)‐induced Ca 2+ response. In contrast to CD26/DPP IV‐processed RANTES(3‐68), SDF‐1α(3‐68) had diminished potency to inhibit HIV‐1 infection. Thus, CD26/DPP IV impairs the inflammatory and haematopoietic potency of chemokines but plays a dual role in AIDS.