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Blood, 15 August 2000, Vol. 96, No. 4, pp. 1438-1442
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
HIV-1 gp120- and gp160-induced apoptosis in cultured
endothelial cells is mediated by caspases
Christina K. Ullrich,
Jerome E. Groopman, and
Ramesh
K. Ganju
From the Divisions of Experimental Medicine and
Hematology/Oncology, Beth Israel Deaconess Medical Center, Harvard
Medical School, Boston, MA.
The immune dysfunction and cell destruction that occur in the human
immunodeficiency virus (HIV)-infected host appear to result from the
direct cytopathic effects of viral infection and the effects of viral
proteins on uninfected bystander cells. Recently, the  -chemokine
receptor CXCR4 has been reported to mediate apoptosis in neuronal cells
and in CD4+ and CD8+ T cells after its binding
to HIV-1 envelope proteins. In the current study, it was observed that
human umbilical vein endothelial cells (HUVEC) undergo apoptosis after
their treatment with the HIV-1 envelope proteins gp120/160. Anti-CXCR4
monoclonal antibody decreased HIV-1 gp120/160-induced apoptosis,
suggesting that the CXCR4 chemokine receptor mediates the apoptotic
effects of these HIV envelope glycoproteins. Further studies revealed
that caspases play an important role in this process because the
pretreatment of cells with a general caspase enzyme inhibitor decreased
the extent of HUVEC apoptosis induced by gp120/160. In addition, it was
found that caspase-3 was activated on HIV-1 gp120/160 treatment of
these cells. It was also observed that gp120/160 treatment slightly
increased the expression of the pro-apoptotic molecule Bax. These
results suggest that HIV-1 envelope glycoproteins can disrupt
endothelial integrity through the interaction with CXCR4, thereby
facilitating virus transit out of the bloodstream and contributing to
the vascular injury syndromes seen in acquired immunodeficiency syndrome.
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