Abstract:
BACKGROUND:Human cytomegalovirus (CMV) uses different strategies to escape from human host defense reactions. Previously we have observed that infection of endothelial cells with CMV in vitro leads to enhanced activity of endothelial ectonucleotidases. These ectoenzymes are responsible for hydrolysis of extracellular adenine nucleotides, resulting in the formation of adenosine. Infection with CMV in vivo therefore may result in local increase of adenosine production, providing an anti-inflammatory and antiaggregatory microenvironment, which may facilitate entry of the virus into the target cell. METHODS:The present study focuses on the expression of P2 type purinergic receptors on endothelial cells after infection with CMV. Human endothelial cells were infected with CMV and compared with either uninfected cells or endothelial cells infected with other herpesviruses (herpes simplex virus [HSV] 1 or 2) for the expression of P2 receptors such as P2Y1, P2Y2, or P2X7. For comparison, cells stimulated with nonspecific agents were also studied. RESULTS:A strong upregulation of the P2 receptors tested was shown, exclusively in CMV-infected cells. Stimulation with either HSV-1 or HSV2, nonspecific stimulants, or various cytokines did not affect the expression of these P2 receptors significantly. CONCLUSION:Infection of endothelium with CMV causes significant upregulation of the P2 receptors studied. As these receptors may potentially be able to concentrate nucleotides along the ectonucleotidases of the endothelial cell membrane, rapid local hydrolysis of adenosine triphosphate and adenosine diphosphate may be facilitated by enhanced P2 receptor expression. Such a CMV induced mechanism might enable the virus to escape from an important host defense response, such as local microthrombus formation.
journal_name
Transplantationjournal_title
Transplantationauthors
Zandberg M,van Son WJ,Harmsen MC,Bakker WWdoi
10.1097/01.tp.0000287598.25493.a5subject
Has Abstractpub_date
2007-11-27 00:00:00pages
1343-7issue
10eissn
0041-1337issn
1534-6080pii
00007890-200711270-00017journal_volume
84pub_type
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