Proost P, Struyf S, Schols D, Durinx C, Wuyts A, Lenaerts J P, De Clercq E, De Meester I, Van Damme J
Laboratory of Molecular Immunology, Rega Institute for Medical Research, University of Leuven, Belgium.
FEBS Lett. 1998 Jul 31;432(1-2):73-6. doi: 10.1016/s0014-5793(98)00830-8.
The chemokine stromal-cell-derived factor-1alpha (SDF-1alpha) 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-1alpha was NH2-terminally cleaved to SDF-1alpha(3-68) by dipeptidyl-peptidase IV (CD26/DPP IV), which is present in blood in soluble and membrane-bound form. SDF-1alpha(3-68) lost both lymphocyte chemotactic and CXCR4-signaling properties. However, SDF-1alpha(3-68) still desensitized the SDF-1alpha(1-68)-induced Ca2+ response. In contrast to CD26/DPP IV-processed RANTES(3-68), SDF-1alpha(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.
趋化因子基质细胞衍生因子-1α（SDF-1α）可趋化淋巴细胞和CD34+造血祖细胞，并且是T嗜性HIV-1毒株的主要共受体CXCR4（CXC趋化因子受体4）的配体。二肽基肽酶IV（CD26/DPP IV）可将SDF-1α的氨基末端切割为SDF-1α(3-68)，该酶以可溶性和膜结合形式存在于血液中。SDF-1α(3-68)丧失了淋巴细胞趋化和CXCR4信号传导特性。然而，SDF-1α(3-68)仍能使SDF-1α(1-68)诱导的Ca2+反应脱敏。与CD26/DPP IV处理的RANTES(3-68)不同，SDF-1α(3-68)抑制HIV-1感染的效力减弱。因此，CD26/DPP IV损害趋化因子的炎症和造血效力，但在艾滋病中发挥双重作用。
